Record 1 from database: MEDLINE
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Title

Acute aluminium intoxication: a study of the efficacy of several antidotal treatments in mice.

Author

Domingo JL; Llobet JM; Gómez M; Corbella J

Address

Source

Res Commun Chem Pathol Pharmacol, 1986 Jul, 53:1, 93-104

Abstract

The effect of the chelating agents deferoxamine mesylate (DFOA), sodium salicylate, citric acid, Na2Ca-ethylendiaminetetracetate (EDTA), nitrilotriacetic acid (NTA), L-cysteine, N-acetyl-L-cysteine (NAC) and 2, 3-dimercaptosuccinic acid (DMSA) on the lethality, elimination and tissue retention of aluminum was investigated on male Swiss mice. To determine the effect of the various chelators on the lethality of aluminium, various doses of Al (NO3)3.9H2O (3.0 - 7.5 mmol/kg) were given intraperitoneally followed immediately by the ip administration of the chelator (at dose equal to one-third of their respective LD50). Survival was recorded at the end of 14 days. Significant increases in survival were noted with citric acid and DFOA. A decrease of the aluminium concentration in various tissues, and an increase in urinary and fecal elimination of aluminium were also noted with citric acid, DFOA, and sodium salicylate. Citric acid appear to be the most effective agent of those tested in the prevention of acute aluminum intoxication.

Language of Publication

English

Unique Identifier

86315107

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MeSH Heading (Major)

Aluminum|ME/*TO; Chelating Agents|*PD

MeSH Heading

Animal; Citrates|PD; Cysteine|PD; Deferoxamine|PD; Lethal Dose 50; Male; Mice; Sodium Salicylate|PD; Tissue Distribution

Publication Type

JOURNAL ARTICLE

ISSN

0034-5164

Country of Publication

UNITED STATES

Record 2 from database: MEDLINE
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Title

Isolation and characterization of wheat aluminum-regulated genes: possible involvement of aluminum as a pathogenesis response elicitor.

Author

Hamel F; Breton C; Houde M

Address

DÆepartement des Sciences biologiques, UniversitÆe du QuÆebec Äa MontrÆeal, Canada.

Source

Planta, 1998 Aug, 205:4, 531-8

Abstract

Using differential screening of a root tip cDNA library prepared from an Al-tolerant wheat cultivar (Triticum aestivum L. cv. Atlas-66) exposed to Al, we have isolated and characterized several wheat aluminum-regulated (War) cDNAs. Sequence comparison revealed that genes up-regulated by Al correspond to peroxidase (war4.2), cysteine proteinase (war5.2), phenylalanine-ammonia lyase (war7.2), and oxalate oxidase (war13.2). Two wheat cultivars that differ in their level of tolerance (cv. Atlas-66: tolerant, and cv. Fredrick: sensitive) were used to evaluate the relationship between the accumulation of War mRNAs and Al toxicity, as measured by root growth inhibition (RGI). The mRNA accumulation was modulated to similar levels in both cultivars compared at equivalent RGIs. This indicates that War mRNA accumulation is associated with the toxicity of Al rather than with the cultivar's tolerance. It appears that most of the genes found to be up-regulated by Al share homologies with genes induced by pathogens. This suggests that Al may act as an elicitor of a pathogenesis-related transduction pathway. The potential functions of the up-regulated war genes in cell wall strengthening and Al trapping are discussed.

Language of Publication

English

Unique Identifier

98348982

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MeSH Heading (Major)

Aluminum|*ME/PD; Cysteine Endopeptidases|*GE/ME; Genes, Plant|*; Oxidoreductases|*GE/ME; Plant Proteins|*GE; Wheat|*EN/GE

MeSH Heading

Amino Acid Sequence; Base Sequence; DNA, Plant; Gene Expression Regulation, Plant; Molecular Sequence Data; Plant Roots|GD; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't; Up-Regulation (Physiology)

Publication Type

JOURNAL ARTICLE

ISSN

0032-0935

Country of Publication

GERMANY

Record 3 from database: MEDLINE
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Title

The influence of various adjuvants on antibody synthesis following immunization with an hapten.

Author

Kellner J; Erhard M; Schranner I; Lösch U

Address

Institut fÂur Physiologie, Physiologische Chemie und ErnÂahrungsphysiologie, TierÂarztliche FakultÂat, Ludwig-Maximilians-UniversitÂat MÂunchen, Germany.

Source

Biol Chem Hoppe Seyler, 1992 Jan, 373:1, 51-5

Abstract

For the production of specific antibodies to the hapten MATP (4-Amino-1,2,2-trimethyl-phenylphosphonate) in Balb/c mice various non-toxic adjuvants were compared to Freund's complete adjuvant (FCA). For immunization the hapten MATP was coupled to the carrier human serum albumin (HSA). The immunostimulating effect of the synthetic lipopeptides Pam3Cys-OH, Pam3Cys-Ser-Ser-Asn-Ala and different concentrations of the lipohexapeptide Pam3Cys-Ser-(Lys)4 (Pam3Cys = S-[2,3-bis(palmitoyloxy)-(2RS)-propyl]-N- palmitoyl-(R)-cysteine as well as of aluminium hydroxide were tested. IgG antibody titers in serum were determined in ELISA. In dose-response studies 50 micrograms Pam3Cys-Ser-(Lys)4 per mouse was the most effective dose with a long period of high antibody levels after the second booster. Pam3Cys-Ser-Ser-Asn-Ala provoked only low antibody titers. Immunostimulation with Pam3Cys--OH did not result in an increased production of specific antibodies. Compared to the control group an enhanced antibody synthesis could be provoked with aluminium hydroxide. However, the increase was much smaller than by using FCA. The lipopeptide Pam3Cys-Ser-(Lys)4 turned out to be a very potent adjuvant. One week after booster injection into mice 50 micrograms of this substance helped to elicit a higher antibody titer than FCA. Hence, as far as the degree of antibody production is concerned, Pam3Cys-Ser--(Lys)4 represents an alternative adjuvant to FCA.

Language of Publication

English

Unique Identifier

92162200

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MeSH Heading (Major)

Adjuvants, Immunologic|*PD; Antibody Formation|*DE

MeSH Heading

Aluminum Hydroxide|PD; Amino Acid Sequence; Animal; Cysteine|AA/PD; Freund's Adjuvant|PD; Haptens|IM; Immunization; Lipoproteins|PD; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Oligopeptides|PD

Publication Type

JOURNAL ARTICLE

ISSN

0177-3593

Country of Publication

GERMANY

Record 4 from database: MEDLINE
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Title

The inhibition of metabolic oxalate production by sulfhydryl compounds.

Author

Bais R; Rofe AM; Conyers RA

Address

Division of Clinical Chemistry, Institute of Medical and Veterinary Science, Adelaide, Australia.

Source

J Urol, 1991 Jun, 145:6, 1302-5

Abstract

A number of sulfhydryl compounds were shown to inhibit CO2 and oxalate formation from glyoxylate by rat liver homogenates and hepatocytes. The most significant inhibition occurred with cysteine and this inhibition was concentration-dependent. In rats made hyperoxaluric by administering ethylene glycol in their drinking water, daily intraperitoneal injections of cysteine caused a rapid and marked decrease in urinary oxalate excretion which was maintained over the duration of the treatment (28 days). Over this time period, the level of urinary oxalate excretion in these ethylene glycol-treated rats was reduced to that of the controls. It is postulated that the decrease is due to the formation of a cysteine-glyoxylate adduct, 2-carboxy-4-thiazolidine carboxylate, which prevents glyoxylate being further oxidized to oxalate. Cysteine or similar sulphydryl compounds may therefore have potential as therapeutic agents in the prevention of renal stones.

Language of Publication

English

Unique Identifier

91237921

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MeSH Heading (Major)

Aluminum|*AI; Liver|*DE; Oxalates|*ME/UR; Sulfhydryl Compounds|*PD

MeSH Heading

Animal; Carbon Dioxide|ME; Cysteine|PD; Ethylene Glycols; Hyperoxaluria|CI/DT/UR; In Vitro; Rats; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0022-5347

Country of Publication

UNITED STATES

Record 5 from database: MEDLINE
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Title

Factor X-activating procoagulant in normal and malignant breast tissue.

Author

el Baruni K; Taylor I; Roath S; Francis JL

Address

University Department of Haematology, Southampton General Hospital, U.K.

Source

Hematol Oncol, 1990 Nov, 8:6, 323-32

Abstract

Factor X-activating activity (FXAA) was determined by a chromogenic assay in normal and malignant breast tissue. FXAA was found in all tissue (n = 38) irrespective of pathology, and the activity of normal tissue was similar to that of tumours. FXAA correlated with tissue hemoglobin in normal breast (p less than 0.02) but not in tumours. FXAA was markedly reduced by aluminium hydroxide, barium citrate, anti-human factor VII, DFP, PMSF and phospholipase C, but was unaffected by iodoacetamide and mercuric chloride. It is concluded that FXAA is a serine protease with the properties of a tissue factor-factor VII complex. FXAA occurs in normal and malignant breast tissue, although the 'normal' activity may be an artefact of the homogenization process.

Language of Publication

English

Unique Identifier

91139080

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MeSH Heading (Major)

Breast|*CH; Breast Neoplasms|*CH; Cysteine Endopeptidases|*AN/ME

MeSH Heading

Adsorption; Aluminum Hydroxide|PD; Citrates|PD; Factor VII|PD; Female; Hemoglobins|AN; Human; Isoflurophate|PD; Neoplasm Proteins|AN; Phenylmethylsulfonyl Fluoride|PD; Phospholipase C|PD

Publication Type

JOURNAL ARTICLE

ISSN

0278-0232

Country of Publication

ENGLAND

Record 6 from database: MEDLINE
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Title

Conformational changes at the carboxyl terminus of Galpha occur during G protein activation.

Author

Yang CS; Skiba NP; Mazzoni MR; Hamm HE

Address

Department of Physiology & Biophysics, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612, USA.

Source

J Biol Chem, 1999 Jan, 274:4, 2379-85

Abstract

To understand the dynamics of conformational changes during G protein activation, surface exposed cysteine residues on Galpha were fluorescently labeled. Limited trypsinolysis and mutational analysis of recombinant Galphat/Galphai1 determined that two cysteines are the major fluorescent labeling sites, Cys210, located in the switch II region, and Cys347 at the C terminus. Mutants with serines replacing Cys210 (Chi6a) and Cys347 (Chi6b) were single fluorescently labeled with lucifer yellow (LY), while a double mutant (Chi6ab) was no longer labeled. When Chi6b was labeled with LY on Cys210, AlF4- caused a 220% increase in LY fluorescence, indicating that the fluorescent group at Cys210 is a reporter of conformational change in the switch II region. Chi6a labeled at Cys347 also showed an AlF4--dependent increase in LY fluorescence (91%), indicating that Galpha activation leads to a conformational change at the COOH terminus. Preactivation of the protein with AlF4- before labeling led to a decreased incorporation of LY into Cys347 suggesting that Galpha activation buries Cys347. This COOH-terminal conformational change may provide the structural basis for communication between the GDP-binding site on Galpha and activated receptors, and may contribute to dissociation of activated Galpha subunit from activated receptor.

Language of Publication

English

Unique Identifier

99107896

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MeSH Heading (Major)

GTP-Binding Proteins|CH/*ME

MeSH Heading

Aluminum Compounds|CH; Chimeric Proteins|CH/ME; Chromatography, High Pressure Liquid; Cysteine|CH; Fluorescent Dyes|CH; Fluorides|CH; Isoquinolines|CH; Protein Conformation; Solvents; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0021-9258

Country of Publication

UNITED STATES

Record 7 from database: MEDLINE
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Title

Importance of F1-ATPase residue alpha-Arg-376 for catalytic transition state stabilization.

Author

Nadanaciva S; Weber J; Wilke Mounts S; Senior AE

Address

Department of Biochemistry and Biophysics, University of Rochester Medical Center, New York 14642, USA.

Source

Biochemistry, 1999 Nov, 38:47, 15493-9

Abstract

The functional role of essential residue alpha-Arg-376 in the catalytic site of F1-ATPase was studied. The mutants alpha R376C, alpha R376Q, and alpha R376K were constructed, and combined with the mutation beta Y331W, to investigate catalytic site nucleotide-binding parameters, and to assess catalytic transition state formation by measurement of MgADP-fluoroaluminate binding. Each mutation caused large impairment of ATP synthesis and hydrolysis. Despite the apparent proximity of alpha-Arg-376 to bound nucleoside di- and triphosphate in published X-ray structures, the mutations had little effect on MgADP or MgATP binding affinities, particularly at the highest affinity catalytic site, site 1. Both Cys and Gln mutants abolished transition state formation, demonstrating that alpha-Arg-376 is normally involved at this step of catalysis. A model of the F1-ATPase catalytic transition state structure is presented and discussed. The Lys mutant, although severely impaired, supported transition state formation, suggesting that an additional essential role for the alpha-Arg-376 guanidinium group exists, likely in alpha/beta conformational signal transmission required for steady-state catalysis. Parallels between alpha-Arg-376 and GAP/G-protein "arginine finger" residues are evident.

Language of Publication

English

Unique Identifier

20039872

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MeSH Heading (Major)

Arginine|*CH/GE/ME; H(+)-Transporting ATP Synthase|*CH/GE/ME

MeSH Heading

Adenosine Diphosphate|ME; Adenosine Triphosphate|ME; Aluminum|ME; Binding Sites|GE; Catalysis; Cysteine|GE; Enzyme Stability|GE; Escherichia coli|EN/GE; Fluorine|ME; Glutamine|GE; Lysine|GE; Models, Molecular; Mutagenesis, Site-Directed; Spectrometry, Fluorescence; Support, U.S. Gov't, P.H.S.; Tryptophan|GE; Tyrosine|GE

Publication Type

JOURNAL ARTICLE

ISSN

0006-2960

Country of Publication

UNITED STATES

Record 8 from database: MEDLINE
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Title

Sulphydryl-containing agents: a new approach to the problem of refractory peptic ulceration.

Author

Salim AS

Address

University Department of Surgery, Medical City, Baghdad, Iraq.

Source

Pharmacology, 1992, 45:6, 301-6

Abstract

Refractory peptic ulceration is the term applied to those gastric and duodenal ulcers which remain unhealed despite active treatment for at least 3 months. Sulphydryl-containing agents stimulate the formation of gastrointestinal mucus, bind the oxygen-derived free radicals that mediate tissue damage and play an important role in protein synthesis. This is the first report which suggests that these agents stimulate the healing of refractory gastric and duodenal ulceration without any adverse events.

Language of Publication

English

Unique Identifier

93141659

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MeSH Heading (Major)

Anti-Ulcer Agents|*TU; Peptic Ulcer|*DT; Sulfhydryl Compounds|*TU

MeSH Heading

Adult; Aluminum Hydroxide|TU; Antacids|TU; Cimetidine|TU; Cysteine|TU; Drug Combinations; Drug Therapy, Combination; Endoscopy, Gastrointestinal; Female; Human; Magnesium Hydroxide|TU; Male; Middle Age; Vitamin U|TU

Publication Type

JOURNAL ARTICLE

ISSN

0031-7012

Country of Publication

SWITZERLAND

Record 9 from database: MEDLINE
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Title

High performance liquid chromatographic separation of cisplatin and its hydrolysis products on alumina and application to studies of their interaction with cysteine.

Author

Shearan P; Alvarez JM; Zayed N; Smyth MR

Address

School of Chemical Sciences, Dublin City University, Ireland.

Source

Biomed Chromatogr, 1990 Mar, 4:2, 78-82

Abstract

An alumina stationary phase has been assessed in the study of the retention behaviour of the anticancer drug cisplatin and its major hydrolysis products. Parameters such as buffer concentration in the mobile phase, pH, organic modifier and competing ion have been investigated in order to optimize chromatographic separation with ultraviolet detection. The separation scheme developed has been used to monitor the hydrolysis of cisplatin in aqueous and saline media, and to monitor the interaction of hydrolysed solutions of cisplatin with the amino acid cysteine. A new peak was observed in the chromatograms of such mixtures when they had been allowed to stand for periods of greater than 16 h and, from analysis of the data obtained, it was concluded that this new peak was due to a complex formed between the mono-aquo hydrolysis product of cisplatin and the amino acid.

Language of Publication

English

Unique Identifier

90275314

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MeSH Heading (Major)

Aluminum|*; Aluminum Oxide|*; Chromatography, High Pressure Liquid|*; Cisplatin|*IP; Cysteine|*

MeSH Heading

Buffers; Cations, Monovalent; Chemistry; Hydrogen-Ion Concentration; Hydrolysis; Phosphates; Sodium Chloride; Solutions; Support, Non-U.S. Gov't; Tetraethylammonium Compounds|PD; Water

Publication Type

JOURNAL ARTICLE

ISSN

0269-3879

Country of Publication

ENGLAND

Record 10 from database: MEDLINE
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Title

Labeling of the beta gamma subunit complex of transducin with an environmentally sensitive cysteine reagent. Use of fluorescence spectroscopy to monitor transducin subunit interactions.

Author

Phillips WJ; Cerione RA

Address

Department of Pharmacology, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853.

Source

J Biol Chem, 1991 Jun, 266:17, 11017-24

Abstract

In this study, we have examined the interactions of the beta gamma subunit complex of the retinal GTP-binding protein transducin (beta gamma T) with its alpha subunit (alpha T) using fluorescence spectroscopic approaches. The beta gamma T subunit complex was covalently labeled with 2-(4'-maleimidylanilino)napthalene-6-sulfonic acid (MIANS), an environmentally sensitive fluorescent cysteine reagent. The formation of the MIANS beta gamma T complexes (two to five MIANS adducts per beta gamma T) resulted in 2-3-fold enhancements in the MIANS fluorescence, and 20-25-nm blue shifts in the fluorescence emission maxima, relative to the emission for identical concentrations of MIANS-labeled MIANS complexes. The addition of alpha T.GDP to these MIANS beta gamma T complexes resulted in an additional enhancement in the MIANS fluorescence (typically ranging from 20 to 40%) and a 5-10-nm blue shift in the wavelength for maximum emission. These fluorescence changes were specifically elicited by the GDP-bound form of alpha T and were not observed upon the addition of purified alpha T.guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S) complexes to the MIANS beta gamma T species. Conditions which resulted in the activation of the alpha T.GDP subunit (i.e. the addition of AlF4- or the addition of rhodopsin-containing vesicles and GTP gamma S) resulted in a reversal of the alpha T.GDP-induced enhancement of the MIANS beta gamma T fluorescence. Thus the MIANS beta gamma T fluorescence provided a spectroscopic monitor for transducin-subunit association and transducin-activation. Based on the results from studies using this spectroscopic read-out, it appears that the association of the alpha T.GDP species with the beta gamma T subunit complex to form the holotransducin molecule is rapid and does not limit the rate of the rhodopsin-stimulated activation of holotransducin. However, either the dissociation of the activated alpha T subunit from the beta gamma T complex, or a conformational change in beta gamma T which occurs as a result of the subunit dissociation event, appears to be slow relative to the G protein-subunit association event.

Language of Publication

English

Unique Identifier

91250406

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MeSH Heading (Major)

Anilino Naphthalenesulfonates|*PD; Cysteine|*; GTP Phosphohydrolases|*ME; Rod Outer Segments|*ME; Sulfhydryl Reagents|*PD; Transducin|IP/*ME

MeSH Heading

Aluminum|PD; Animal; Cattle; Fluorine|PD; Guanosine Diphosphate|ME; Guanosine 5'-O-(3-Thiotriphosphate)|PD; Kinetics; Macromolecular Systems; Rhodopsin|ME; Spectrometry, Fluorescence; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0021-9258

Country of Publication

UNITED STATES

Record 11 from database: MEDLINE
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Title

Mutations in the nucleotide binding domain of the alpha subunits of the F1-ATPase from thermophilic Bacillus PS3 that affect cross-talk between nucleotide binding sites.

Author

Grodsky NB; Dou C; Allison WS

Address

Department of Chemistry and Biochemistry, School of Medicine, University of California, San Diego, La Jolla 92093-0601, USA.

Source

Biochemistry, 1998 Jan, 37:4, 1007-14

Abstract

Inactivation of MF1 (bovine mitochondrial F1-ATPase) with 5'-p-fluorosulfonylbenzoylethenoadenosine is caused by labeling alpha Y244 [Verburg, J. G., and Allison, W. S. (1990) J. Biol. Chem. 265, 8065-8074]. In the crystal structure [Abrahams, J.P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628], alpha Y244 is hydrogen bonded to alpha R304 which is also hydrogen bonded to alpha Y300. The catalytic properties of mutant alpha 3 beta 3 gamma subcomplexes of the TF1-ATPase from the thermophilic Bacillus PS3 containing the alpha F244C, alpha R304C, and alpha Y300C substitutions have been examined. Each has unique features for hydrolyzing ATP and forming inhibitory ADP-fluoroaluminate complexes in catalytic sites. Unlike wild-type, the (alpha R304C)3 beta 3 gamma and (alpha Y300C)3 beta 3 gamma subcomplexes entrap inhibitory MgADP in a catalytic site during turnover which fails to dissociate when ATP binds to noncatalytic sites. Although the hydrolytic properties of the (alpha F244C)3 beta 3 gamma subcomplex and wild-type are similar, the mutant forms ADP-fluoroaluminate complexes 7 times faster than wild-type when Al3+ and F- are added to it in the presence of excess ADP and Mg2+. It also resists inhibition by high Mg2+ concentrations in the assay medium. At least one noncatalytic site of the (alpha F244C)3 beta 3 gamma subcomplex has increased affinity for ADP, indicating that the enhanced rate of formation of the ADP-fluoroaluminate complex reflects augmented cooperativity between noncatalytic and catalytic sites. The rate of formation of the ADP-fluoroaluminate complex in (alpha Y300C)3 beta 3 gamma increases only 40% when MgADP in bound to two catalytic sites rather than one, compared to a 9-fold increase exhibited by wild type. When Al3+ and F- are added to the (alpha Y300C)3 beta 3 gamma subcomplex after incubation with excess ADP and Mg2+, ADP-fluoroaluminate complexes are formed in three catalytic sites rather than two observed with the other subcomplexes. Reconciliation of the catalytic properties of the mutant subcomplexes in terms of the crystal structure suggests that alpha F244, alpha R304, and alpha Y300 of TF1 are part of a pathway that propagates conformational signals from one catalytic site to another.

Language of Publication

English

Unique Identifier

98128578

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MeSH Heading (Major)

Adenosine Diphosphate|AA/*ME; Adenosine Triphosphate|*ME; Bacterial Proteins|GE/*ME; H(+)-Transporting ATP Synthase|GE/*ME

MeSH Heading

Aluminum; Arginine|GE; Bacillus|EN; Binding Sites; Comparative Study; Cysteine|GE; Fluorine; Hydrolysis; Models, Molecular; Mutagenesis, Site-Directed; Phenylalanine|GE; Structure-Activity Relationship; Support, U.S. Gov't, P.H.S.; Tyrosine|GE

Publication Type

JOURNAL ARTICLE

ISSN

0006-2960

Country of Publication

UNITED STATES

Record 12 from database: MEDLINE
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Title

Abiotic factors affecting the toxicity of lead to fungi.

Author

Babich H; Stotzky G

Address

 

Source

Appl Environ Microbiol, 1979 Sep, 38:3, 506-13

Abstract

The toxicity of lead (Pb) to fungi in pure culture was influenced by several abiotic factors: pH, inorganic anions, clay minerals, and particulate (humic acid) and soluble organic matter. The toxicity of Pb was potentiated under acidic conditions (pH 5 and 6), and phosphate or carbonate anions reduced the toxicity, apparently as a result of the formation of sparingly soluble Pb salts. Clay minerals (montmorillonite greater than attapulgite greater than kaolinite) and particulate humic acid protected against the toxicity of Pb, presumably as the result of sorption, by cation exchange of the Pb to the exchange complexes, which reduced its availability for uptake by the fungi. Soluble organics, such as tryptone, yeast extract, cysteine, succinic acid, and increasing concentrations of neopeptone, also reduced the toxicity of Pb.

Language of Publication

English

Unique Identifier

80128953

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MeSH Heading (Major)

Fungi|*DE/GD; Lead|*PD; Soil Microbiology|*

MeSH Heading

Aluminum Silicates|PD; Carbonates|PD; Culture Media; Humic Acids|PD; Hydrogen-Ion Concentration; Phosphates|PD; Species Specificity

Publication Type

JOURNAL ARTICLE

ISSN

0099-2240

Country of Publication

UNITED STATES

Record 13 from database: MEDLINE
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Title

Comparative inhibition of hepatic hydroxymethylbilane synthase by both hard and soft metal cations.

Author

Farmer DJ; Hollebone BR

Address

 

Source

Can J Biochem Cell Biol, 1984 Jan, 62:1, 49-54

Abstract

The in vitro inhibition of hydroxymethylbilane synthase (EC 4.3.1.8, uroporphyrinogen I synthetase) obtained from livers of Sprague-Dawley rats has been studied with a wide range of di- and tri-valent metal ions. After purification by cell lysis, heat treatment, and centrifugation, the stable, soluble enzyme yielded sigmoidal inhibition curves with increasing concentrations of each of the 16 test ions. Using the negative logarithm of metal concentration for 50% inhibition (the pM50 value), the metal ions could be classified according to their Klopman hardness values. Very soft ions including Hg2+, intermediate ions including Cr3+, and very hard ions including Al3+ all yielded large pM50 values indicating strong inhibition. In comparison to known metal-ion chemical behaviour, these three ions could indicate three different types of inhibitory binding sites at or near the active site: Hg2+ corresponding to sulfur in cysteine, Cr3+ corresponding to nitrogen in histidine, and Al3+ corresponding to oxygen in carboxyl groups. The presence of the first two sites is also indicated by the pH dependence of activity.

Language of Publication

English

Unique Identifier

84180087

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MeSH Heading (Major)

Ammonia-Lyases|*AI; Hydroxymethylbilane Synthase|*AI; Liver|*EN

MeSH Heading

Aluminum|PD; Animal; Cations; Chromium|PD; Kinetics; Male; Mercury|PD; Rats; Rats, Inbred Strains

Publication Type

JOURNAL ARTICLE

ISSN

0714-7511

Country of Publication

CANADA

Record 14 from database: MEDLINE
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Title

Acute toxicity studies of aluminium compounds: antidotal efficacy of several chelating agents.

Author

Llobet JM; Domingo JL; Gómez M; Tomás JM; Corbella J

Address

 

Source

Pharmacol Toxicol, 1987 Apr, 60:4, 280-3

Abstract

Four aluminum compounds--nitrate, chloride, sulphate and bromide--were administered orally and intraperitoneally to rats and mice. The LD50-values (14 days) were determined. The majority of deaths occurring during the first four days. The clinical and physical signs appearing after intoxication include among other lethargy, decreased locomotor activity, piloerection, weight loss and perorbital bleeding. After 14 days no alterations in liver and renal functions were detected in the animals which received intraperitoneally the LD50-values of aluminum nitrate as a single dose. Aluminum concentrations were highest in liver and spleen. No histopathological lesions could be observed. To compare the efficacies of nine chelating agents on the toxicity of aluminum in mice, the therapeutic index and the therapeutic effectiveness of each chelating agent have been calculated. Malic, succinic, oxalic and malonic acids showed the best results with malic and succinic acids being the most effective. Deferoxamine mesylate (DFOA), sodium salicylate, L-cysteine and citric acid were not so effective as antidotes for acute aluminum toxicity. Aurin tricarboxylic acid (ATCA) should not be used due to its high toxicity.

Language of Publication

English

Unique Identifier

87231583

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MeSH Heading (Major)

Aluminum|AI/*TO; Chelating Agents|*TU

MeSH Heading

Animal; Antidotes; Bromides|TO; Chlorides|TO; Comparative Study; Female; Lethal Dose 50; Male; Mice; Nitrates|TO; Rats; Rats, Inbred Strains; Sulfates|TO

Publication Type

JOURNAL ARTICLE

ISSN

0901-9928

Country of Publication

DENMARK

Record 15 from database: MEDLINE
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Title

Five genes induced by aluminum in wheat (Triticum aestivum L.) roots.

Author

Snowden KC; Gardner RC

Address

Centre for Gene Technology, School of Biological Sciences, University of Auckland, New Zealand.

Source

Plant Physiol, 1993 Nov, 103:3, 855-61

Abstract

Five different cDNAs (termed wali1 to wali5 for Wheat Aluminum Induced) whose expression was induced by Al stress have been isolated from the root tips of Al-treated wheat (Triticum aestivum L.) plants. Four of these genes were induced 24 to 96 h after Al treatment, and their expression is reduced when the Al is removed. Each of these four genes was induced by inhibitory levels of Al in two wheat cultivars--Warigal, an Al-sensitive cultivar, and Waalt, an Al-tolerant cultivar. The fifth gene (wali2) showed a complex bimodal pattern of induction and was induced by Al only in the sensitive cultivar. Comparison of the nucleotide sequences of these clones to those in the sequence data bases showed that wali4 is homologous to phenylalanine ammonia-lyase and wali1 is homologous to a group of plant proteins that are cysteine-rich and have homology to metallothioneins. wali2 encodes a novel protein with a repeating motif of cysteine amino acids. The remaining two wali clones (wali3 and wali5) encode related, cysteine-rich proteins that show no significant homology to any known sequences.

Language of Publication

English

Unique Identifier

94294563

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MeSH Heading (Major)

Aluminum|*PD; Gene Expression|*DE; Genes, Plant|*DE; Wheat|DE/*GE/*ME

MeSH Heading

Amino Acid Sequence; Base Sequence; Blotting, Northern; Comparative Study; Consensus Sequence; Conserved Sequence; DNA|CH/GE; Gene Library; Molecular Sequence Data; Plants|GE/ME; RNA, Messenger|AN/BI; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0032-0889

Country of Publication

UNITED STATES

Record 16 from database: MEDLINE
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Title

Effect of salts and other agents on foot-and-mouth disease virus poly (U) polymerase activity.

Author

Polatnick J

Address

 

Source

Arch Virol, 1985, 84:3-4, 269-75

Abstract

The activity of the purified poly(U) polymerase replication complex of foot-and-mouth disease virus was optimized when 100 mM NH4+ and either 0.75 mM Al3+ or 1.0 mM Fe3+ was added to the standard assay reaction mixture. Zn2+ at concentrations of 10(-5) mM to 5 mM inhibited enzyme activity although all polymerases examined to date have contained zinc. Mercaptoethanol and dithiothreitol inhibited polymerase activity despite the presence of cysteine residues in the viral induced polypeptide of the replication complex, possibly because of their action as metal chelators rather than as reducing agents.

Language of Publication

English

Unique Identifier

85198398

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MeSH Heading (Major)

Aphthovirus|*EN; Nucleotidyltransferases|AI/*ME

MeSH Heading

Aluminum|PD; Ammonium Chloride|PD; Dithiothreitol|PD; Ethylmaleimide|PD; Ferric Compounds|PD; Mercaptoethanol|PD; Metals|PD; Oxidation-Reduction; Zinc|PD

Publication Type

JOURNAL ARTICLE

ISSN

0304-8608

Country of Publication

AUSTRIA

Record 17 from database: MEDLINE
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Title

Oxidation of the alpha(3)(betaD311C/R333C)(3)gamma subcomplex of the thermophilic Bacillus PS3 F(1)-ATPase indicates that only two beta subunits can exist in the closed conformation simultaneously.

Author

Ren H; Dou C; Stelzer MS; Allison WS

Address

Department of Chemistry, University of California at San Diego, La Jolla, California 92093-0506, USA.

Source

J Biol Chem, 1999 Oct, 274:44, 31366-72

Abstract

In the crystal structure of the bovine heart mitochondrial F(1)-ATPase (Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E. (1994) Nature 370, 621-628), the two liganded beta subunits, one with MgAMP-PNP bound to the catalytic site (beta(T)) and the other with MgADP bound (beta(D)) have closed conformations. The empty beta subunit (beta(E)) has an open conformation. In beta(T) and beta(D), the distance between the carboxylate of beta-Asp(315) and the guanidinium of beta-Arg(337) is 3.0-4.0 A. These side chains are at least 10 A apart in beta(E). The alpha(3)(betaD311C/R333C)(3)gamma subcomplex of TF(1) with the corresponding residues substituted with cysteine has very low ATPase activity unless it is reduced prior to assay or assayed in the presence of dithiothreitol. The reduced subcomplex hydrolyzes ATP at 50% the rate of wild-type and is rapidly inactivated by oxidation by CuCl(2) with or without magnesium nucleotides bound to catalytic sites. Titration of the subcomplex with iodo[(14)C]acetamide after prolonged treatment with CuCl(2) in the presence or absence of 1 mM MgADP revealed nearly two free sulfhydryl groups/mol of enzyme. Therefore, one pair of introduced cysteines is located on a beta subunit that exists in the open or partially open conformation even when catalytic sites are saturated with MgADP. Since V(max) of ATP hydrolysis is attained when three catalytic sites of F(1) are saturated, the catalytic site that binds ATP must be closing as the catalytic site that releases products is opening.

Language of Publication

English

Unique Identifier

20002663

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MeSH Heading (Major)

Bacillus|*EN; H(+)-Transporting ATP Synthase|*CH/GE/ME

MeSH Heading

Adenosine Triphosphate|ME; Adenylyl Imidodiphosphate|ME; Aluminum|PD; Copper|PD; Dithiothreitol|PD; Edetic Acid|PD; Fluorine|PD; Heat; Hydrolysis; Iodoacetamide|PD; Iodoacetates|PD; Models, Molecular; Mutagenesis; Oxidation-Reduction; Protein Conformation; Protein Structure, Quaternary; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0021-9258

Country of Publication

UNITED STATES

Record 18 from database: MEDLINE
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Title

Five genes induced by aluminum in wheat (Triticum aestivum L.) roots.

Author

Snowden KC; Gardner RC

Address

Centre for Gene Technology, School of Biological Sciences, University of Auckland, New Zealand.

Source

Plant Physiol, 1993 Nov, 103:3, 855-61

Abstract

Five different cDNAs (termed wali1 to wali5 for Wheat Aluminum Induced) whose expression was induced by Al stress have been isolated from the root tips of Al-treated wheat (Triticum aestivum L.) plants. Four of these genes were induced 24 to 96 h after Al treatment, and their expression is reduced when the Al is removed. Each of these four genes was induced by inhibitory levels of Al in two wheat cultivars--Warigal, an Al-sensitive cultivar, and Waalt, an Al-tolerant cultivar. The fifth gene (wali2) showed a complex bimodal pattern of induction and was induced by Al only in the sensitive cultivar. Comparison of the nucleotide sequences of these clones to those in the sequence data bases showed that wali4 is homologous to phenylalanine ammonia-lyase and wali1 is homologous to a group of plant proteins that are cysteine-rich and have homology to metallothioneins. wali2 encodes a novel protein with a repeating motif of cysteine amino acids. The remaining two wali clones (wali3 and wali5) encode related, cysteine-rich proteins that show no significant homology to any known sequences.

Language of Publication

English

Unique Identifier

94294563

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MeSH Heading (Major)

Aluminum|*PD; Gene Expression|*DE; Genes, Plant|*DE; Wheat|DE/*GE/*ME

MeSH Heading

Amino Acid Sequence; Base Sequence; Blotting, Northern; Comparative Study; Consensus Sequence; Conserved Sequence; DNA|CH/GE; Gene Library; Molecular Sequence Data; Plants|GE/ME; RNA, Messenger|AN/BI; Sequence Homology, Amino Acid; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0032-0889

Country of Publication

UNITED STATES

Record 19 from database: MEDLINE
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Title

Regulation of blood glucose by sustained delivery of insulin via ALCAP ceramics in rats.

Author

Muzina DJ; Snow KR; Bajpai PK

Address

 

Source

Biomed Sci Instrum, 1989, 25:, 191-202

Abstract

Years of research at the University of Dayton has resulted in the development of a porous, resorbable, alumino-calcium-phosphorous oxide ceramic (ALCAP) which is capable of delivering substances of different molecular weights and chemical structures. In vitro delivery of insulin has been accomplished by means of ALCAP ceramics and ALCAP ceramic reservoir systems. Insulin delivered by implanted ALCAP ceramic systems was capable of lowering blood glucose levels in streptozotocin induced diabetic rats up to 21 days. Ceramics containing a solid composite of insulin, ALCAP powder (particle size to 38 um), and cysteine (ACI delivery system) were implanted in diabetic rats. Insulin delivered from the ACI systems reduced the hyperglycemia of diabetic rats for 14 days. ALCAP ceramics with 1.0 ml glass reservoirs (GRCS) were filled with a solution of insulin in vegetable oil to slow the delivery of hormone in vivo. The hormone delivered in oil by the GRCS device effectively regulated blood sugar in diabetic rats for 21 days.

Language of Publication

English

Unique Identifier

89303182

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MeSH Heading (Major)

Aluminum|*; Blood Glucose|*ME; Calcium|*; Ceramics|*; Diabetes Mellitus, Experimental|BL/*DT; Drug Implants|*; Insulin|*AD; Phosphorus|*

MeSH Heading

Animal; Delayed-Action Preparations; Oxides; Rats; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0067-8856

Country of Publication

UNITED STATES

Record 20 from database: MEDLINE
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Title

Elasticity of mutant myosin subfragment-1 arranged on a functional silver surface.

Author

Suda H; Sasaki YC; Oishi N; Hiraoka N; Sutoh K

Address

Department of Biological Science and Technology, Tokai University, 317 Nishino, Numazu, Shizuoka, 410-0321, Japan. suda@fb.u-tokai.ac.jp

Source

Biochem Biophys Res Commun, 1999 Aug, 261:2, 276-82

Abstract

Elasticity of a two-dimensionally arranged myosin subfragment-1 (S1) was measured by using a surface forces apparatus. To prepare a two-dimensionally arranged S1-monolayer on a functionalized silver surface, we used genetically engineered Dictyostelium S1 molecules. A highly reactive cysteine residue was fused to the COOH-terminus using the recombinant DNA method. On the other hand, the maleimide groups was self-assembled onto a silver surface. Then the mutant S1 molecules were chemically bound to the functionalized silver surface at its COOH-terminus. This arrangement technique was necessary in order to create a stable S1-monolayer by chemical bond formation onto the silver surface. The occupied area of the single S1 on the silver surface was about 110 nm(2). In the interaction between the S1-monolayer and mica surfaces in aqueous solution, a long-range attractive force was observed. The elastic constants (stiffness and Young's modulus) of myosin S1 were evaluated from force-distance profiles in aqueous solution, using the Hertz theory. We found that the stiffness (or spring constant) and Young's modulus of S1 in the absence of nucleotide are 4.4 +/- 1.0 pN/nm and 0.71 +/- 0.16 GPa, respectively. Copyright 1999 Academic Press.

Language of Publication

English

Unique Identifier

99355564

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MeSH Heading (Major)

Mutation|*; Myosin Subfragments|*CH/*GE

MeSH Heading

Aluminum Silicates; Amino Acid Sequence; Animal; Biophysics|IS; Dictyostelium|GE; Elasticity; Muscle Contraction|PH; Protein Engineering; Rabbits; Recombinant Proteins|CH/GE; Silver; Support, Non-U.S. Gov't; Surface Properties

Publication Type

JOURNAL ARTICLE

ISSN

0006-291X

Country of Publication

UNITED STATES

Record 21 from database: MEDLINE
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Title

Conjugation to preadsorbed preactivated proteins and efficient generation of anti peptide antibodies.

Author

Houen G; Jakobsen MH; Svaerke C; Koch C; Barkholt V

Address

Department of Autoimmunology, Statens Serum Institut, Copenhagen, Denmark.

Source

J Immunol Methods, 1997 Aug, 206:1-2, 125-34

Abstract

A solid phase conjugation method is described based on the preadsorption of proteins to aluminium hydroxide adjuvant followed by activation of the adsorbed carrier proteins with iodoacetic acid N-hydroxysuccinimidester or other conjugation reagents. Cysteine-containing peptides were coupled to the iodoacetic acid-activated carrier-adjuvant particles through their SH groups. No dialysis is required since the reaction product is isolated at each step of the procedure by a simple centrifugation and can easily be extensively washed between individual manipulations. The method generates peptide-carrier-adjuvant particles with sterically defined presentation of the peptides at the surface of the particles. When used for immunization of mice and rabbits the conjugates elicited high-titered specific anti-peptide sera, which reacted well with the parent protein in ELISA. The strongest reactions were with the denatured form of the parent protein. On immunoblots antisera to the N- and C-terminus of calreticulin recognized the same M, 52,000 protein.

Language of Publication

English

Unique Identifier

97469103

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MeSH Heading (Major)

Carrier Proteins|AD/*IM/*ME; Peptide Fragments|AD/*IM

MeSH Heading

Adsorption; Aluminum Hydroxide; Amino Acid Sequence; Animal; Antibody Formation; Calcium-Binding Proteins|AD/IM/ME; Immunoblotting; Mice; Molecular Sequence Data; Ovalbumin|AD/IM/ME; Rabbits; Ribonucleoproteins|AD/IM/ME; Support, Non-U.S. Gov't; Tuberculin|AD/IM/ME; Vaccines, Synthetic|AD/IM/ME

Publication Type

JOURNAL ARTICLE

ISSN

0022-1759

Country of Publication

NETHERLANDS

Record 22 from database: MEDLINE
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Title

Use of resonance energy transfer to determine the proximity of the guanine nucleotide binding site of transducin relative to a conformationally-sensitive site on the gamma subunit of the cyclic GMP phosphodiesterase.

Author

Erickson JW; Mittal R; Cerione RA

Address

Department of Pharmacology, New York State College of Veterinary Medicine, Cornell University, Ithaca 14853-6401, USA.

Source

Biochemistry, 1995 Jul, 34:27, 8693-700

Abstract

In this work, we have used resonance energy transfer to determine the relative positions of a reactive cysteine residue on the gamma subunit of the retinal cyclic GMP phosphodiesterase (gamma PDE) and a reactive lysine residue on the alpha subunit of transducin (alpha T). The single cysteine residue on gamma PDE (residue 68) is located at a site that is sensitive to the binding of both the inactive and active forms of alpha T. This is demonstrated by the finding that the addition of an alpha T-GDP complex to a gamma PDE subunit labeled with the environmentally-sensitive probe 2-(4-maleimidoanilino)naphthalene-6-sulfonate (MIANS) results in an enhancement in the MIANS fluorescence. The alpha TGDP-induced fluorescence enhancement is dose-dependent and yields an apparent Kd value of approximately 3 microM. Activation of alpha TGDP by aluminum fluoride, when bound to the MIANS-labeled gamma PDE (M-gamma PDE), then results in a quenching of the MIANS fluorescence. The aluminum fluoride-induced change in M-gamma PDE fluorescence occurs on a time scale identical to that observed for changes in the intrinsic alpha T fluorescence that correspond to activating conformational changes in the alpha T "switch II" region. These results suggest that the induction of the activated state of the alpha T subunit results in a change in conformation close to cysteine 68 in gamma PDE.(ABSTRACT TRUNCATED AT 250 WORDS)

Language of Publication

English

Unique Identifier

95337088

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MeSH Heading (Major)

Guanine Nucleotides|*ME; Transducin|*ME; 3',5'-Cyclic-GMP Phosphodiesterase|CH/*ME

MeSH Heading

Amino Acid Sequence; Anilino Naphthalenesulfonates; Animal; Binding Sites; Cattle; Cysteine|CH; Energy Transfer; Eosine Yellowish-(YS)|AA/CH; Fluorescent Dyes; Lysine|CH; Molecular Sequence Data; Sulfhydryl Reagents|CH; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0006-2960

Country of Publication

UNITED STATES

Record 23 from database: MEDLINE
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Title

Cancer procoagulant in serum of rats during development of experimental epithelioma.

Author

Mielicki W; Wierzbicki R

Address

Medical Academy of Lodz, Department of Biochemistry, Poland.

Source

Int J Cancer, 1990 Jan, 45:1, 125-6

Abstract

The activity of cancer procoagulant (CP) during the development of Guérin epithelioma was studied in the blood of Wistar rats. Blood was collected from the carotid artery and, after clotting, proteins adsorbing on aluminum hydroxide were removed from the serum. Then procoagulant activity was determined in the test system without factor VII by means of substrate S-2222 specific for factor Xa. A statistically significant increase in the activity of CP in serum was detected, coinciding with the period of intensive tumor growth (15th-25th day of disease).

Language of Publication

English

Unique Identifier

90129407

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MeSH Heading (Major)

Blood Coagulation Factors|*AN; Carcinoma|*BL; Cysteine Endopeptidases|*BL; Tumor Markers, Biological|*BL

MeSH Heading

Animal; Female; Methods; Neoplasm Transplantation; Rats; Rats, Inbred Strains; Time Factors

Publication Type

JOURNAL ARTICLE

ISSN

0020-7136

Country of Publication

UNITED STATES

Record 24 from database: MEDLINE
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Title

Proteolysis in human lens epithelium determined by a cell-permeable substrate.

Author

Karlsson JO; Andersson M; Kling Petersen A; Sjöstrand J

Address

Institute of Anatomy and Cell Biology, GÂoteborg University, Sweden.

Source

Invest Ophthalmol Vis Sci, 1999 Jan, 40:1, 261-4

Abstract

PURPOSE: To develop a system for continuous evaluation of proteolytic activity in human lens epithelium and to characterize factors of importance for the regulation of proteolytic activity in lens epithelial cells. METHODS: Human lens epithelial cells were obtained during cataract surgery. Capsule epithelium specimens consisted of the central parts of the anterior capsule and the underlying lens epithelium. The sample, with the cell-permeable substrate Suc-Leu-Leu-Val-Tyr-7-amino-4-methylcoumarin, was placed in a chamber, which was placed in a thermostat-controlled aluminum block. Fluorescence changes were continuously measured by the fiber optics of the luminometer, which was placed 5 mm above the buffer surface. RESULTS: After administration of substrate to the medium overlying the cells, the substrate was degraded at a relatively slow rate. Approximately 10 picomoles of amino-4-methylcoumarin were formed per minute. A significant increase of proteolytic activity could be observed after application of 1 microM ionomycin or 2 microM thapsigargin. No leakage of lactate dehydrogenase from the cells was observed during these procedures. Basal proteolytic activity was totally inhibited by the proteasome inhibitor lactacystin. Lactacystin also attenuated the response to ionomycin and thapsigargin. CONCLUSIONS: Human lens epithelium responds to increased Ca levels from external or internal stores with an increased proteolytic activity that may be mediated by calpain, by the proteasome, or by both. This calcium-dependent change in proteolytic activity may be of importance in the development of cataract.

Language of Publication

English

Unique Identifier

99103530

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MeSH Heading (Major)

Calpain|*ME; Cell Membrane Permeability|*; Coumarins|*ME; Cysteine Endopeptidases|*ME; Lens, Crystalline|DE/*EN; Multienzyme Complexes|*ME; Oligopeptides|*ME

MeSH Heading

Acetylcysteine|AA/PD; Calcium|ME; Cell Survival; Enzyme Inhibitors|PD; Epithelium|DE/EN; Human; Ionomycin|PD; Lactate Dehydrogenase|ME; Substrate Specificity; Support, Non-U.S. Gov't; Thapsigargin|PD

Publication Type

JOURNAL ARTICLE

ISSN

0146-0404

Country of Publication

UNITED STATES

Record 25 from database: MEDLINE
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Title

ADP-ribosylation factor-1 is sensitive to N-ethylmaleimide.

Author

Yamaguchi T; Nakayama K; Hatsuzawa K; Tani K; Himeno M; Tagaya M

Address

School of Life Science, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji, Tokyo, 192-0392, Japan.

Source

J Biochem (Tokyo), 1998 Dec, 124:6, 1229-36

Abstract

The treatment of normal rat kidney cells with N-ethylmaleimide caused the release of beta-COP, a component of coatomer, from the Golgi apparatus without causing disassembly of the organelle. The release of beta-COP, which was not due to depolymerization of microtubules, was markedly blocked by the activation of GTP-binding proteins by aluminum fluoride or a nonhydrolyzable analogue of GTP. To determine which component is N-ethylmaleimide-sensitive, we reconstituted the recruitment of coatomer from the bovine brain cytosol onto the Golgi apparatus in digitonin-permeabilized cells. In cells treated with N-ethylmaleimide before permeabilization, beta-COP was still recruited onto the Golgi apparatus. In contrast, beta-COP was not recruited when N-ethylmaleimide-treated bovine brain cytosol was used. These results suggest that the N-ethylmaleimide-sensitive factor(s) are present in the cytosol. It is known that coatomer and ADP-ribosylation factor-1 (ARF1) are the only cytoplasmic proteins needed for the assembly of Golgi-derived coated vesicles. N-Ethylmaleimide treatment of a coatomer-rich fraction did not affect the binding of beta-COP to the Golgi apparatus, whereas the same treatment of an ARF-rich fraction abolished beta-COP binding. Similar results were obtained using purified recombinant ARF1. Concomitant with inactivation, 0.85 mol of N-ethylmaleimide was incorporated into 1 mol of ARF1. ARF1 contains only one cysteine residue (Cys-159), which is located near the base moiety of the bound guanine nucleotide.

Language of Publication

English

Unique Identifier

99054741

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MeSH Heading (Major)

Ethylmaleimide|CH/*PD; Golgi Apparatus|DE/*ME/UL; GTP-Binding Proteins|CH/*DE/ME

MeSH Heading

Animal; Cattle; Cells, Cultured; Cysteine; Cytosol|CH; Guanosine 5'-O-(3-Thiotriphosphate)|PD; Intracellular Membranes|ME; Kidney|CY; Membrane Proteins|DE/ME; Microtubule-Associated Proteins|ME; Paclitaxel|PD; Rats; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0021-924X

Country of Publication

JAPAN

Record 26 from database: MEDLINE
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Title

Conformational changes at the highly reactive cystein and lysine regions of skeletal muscle myosin induced by formation of transition state analogues.

Author

Maruta S; Homma K; Ohki T

Address

Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo, 192-8577, Japan. shinsaku@t.soka.ac.jp

Source

J Biochem (Tokyo), 1998 Sep, 124:3, 578-84

Abstract

Myosin forms stable ternary complexes with Mg2+-ADP and phosphate analogues of aluminum fluoride (AlF4-), beryllium fluoride (BeFn), and scandium fluoride (ScFn). These complexes are distinct from each other and may mimic different transient states in the ATPase cycle [Maruta et al. (1993) J. Biol. Chem. 268, 7093-7100]. Regions of skeletal muscle myosin containing the highly reactive residues Cys 707 (SH1), Cys 697 (SH2), and lysine 83 (RLR) dramatically alter their local conformation when myosin hydrolyzes ATP, and these changes may reflect formation of a series of transient intermediates during ATP hydrolysis. We used the fluorescent probes 4-fluoro-7-sulfamoylbezofurazan, 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid, and trinitrobenzene-sulfonate, which bind to SH1, SH2, and RLR, respectively, to examine differences in local conformations within myosin.ADP.phosphate analogue (BeFn, Vi, AlF4-, and ScFn) complexes. It was observed that the ternary complexes had SH1 conformations similar to those seen on S-1 in the presence of ATP. In contrast, local conformations in the SH2 and RLR regions of S-1.ADP.BeFn were different from those in corresponding regions of S-1.ADP.AlF4- or ScFn. These results suggest that SH1 and SH2 move distinctly during ATP hydrolysis and that the local conformations of the SH2 and RLR regions more sensitively reflect different transient states.

Language of Publication

English

Unique Identifier

98391831

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MeSH Heading (Major)

Cysteine|*CH; Lysine|*CH; Muscle, Skeletal|*CH/EN; Myosin|*CH

MeSH Heading

Adenosinetriphosphatase|ME; Anilino Naphthalenesulfonates; Animal; Chickens; Picrates|CH; Protein Conformation; Spectrometry, Fluorescence; Sulfhydryl Reagents

Publication Type

JOURNAL ARTICLE

ISSN

0021-924X

Country of Publication

JAPAN

Record 27 from database: MEDLINE
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Title

Elevation of cerebral proteases after systemic administration of aluminum.

Author

Guo Ross S; Yang E; Bondy SC

Address

Center for Occupational and Environmental Health, Department of Community and Environmental Medicine, University of California, Irvine 92697-1825, USA. sxguo@uci.edu

Source

Neurochem Int, 1998 Sep, 33:3, 277-82

Abstract

The levels of three proteases in the cerebral cortex of rats following a three week exposure to aluminum, were measured. The activity of apopain (CPP32), an interleukin 1beta converting enzyme (ICE)-like cysteine protease specifically associated with apoptosis, was increased following dosing with aluminum. The activity of calcium-activated neutral protease, calpain, was also increased. However, the enzyme activity of trypsin-like serine protease, known to be elevated by oxidative events, was unchanged. Since aluminum is suspected as a possible factor in the pathogenesis of Alzheimer's disease and other neurological diseases, it is speculated that changed levels in proteolytic enzymes may relate to the neurotoxicity of aluminum.

Language of Publication

English

Unique Identifier

98430724

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MeSH Heading (Major)

Alum Compounds|*PD; Cerebral Cortex|*DE/*EN; Endopeptidases|*ME

MeSH Heading

Animal; Apoptosis; Calpain|ME; Caspase 1|ME; Caspases|ME; DNA Fragmentation; Male; Rats; Rats, Sprague-Dawley; Support, U.S. Gov't, P.H.S.; Trypsin|ME

Publication Type

JOURNAL ARTICLE

ISSN

0197-0186

Country of Publication

ENGLAND

Record 28 from database: MEDLINE
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Title

Sucralfate and soluble sucrose octasulfate bind and stabilize acidic fibroblast growth factor.

Author

Volkin DB; Verticelli AM; Marfia KE; Burke CJ; Mach H; Middaugh CR

Address

Department of Pharmaceutical Research, Merck Research Laboratories, West Point, PA 19486.

Source

Biochim Biophys Acta, 1993 Nov, 1203:1, 18-26

Abstract

The actions of the anti-ulcer drug sucralfate have been proposed to be mediated through interaction with fibroblast growth factors (Folkman, J., Szabo, S., Strovroff, M., McNeil, P., Li, W. and Shing, Y. (1991) Ann. Surg. 214, 414-427). We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. In addition, SOS also enhances the mitogenic activity of aFGF and partially protects the protein's three cysteine residues from copper-catalyzed oxidation. SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays. Front-face fluorescence measurements show that the native, folded form of aFGF binds to the insoluble aluminum salt of sucrose octasulfate (sucralfate). Moreover, sucralfate stabilizes aFGF against thermal and acidic pH-induced unfolding to the same extent as observed with SOS. Thus, due to their high charge density, SOS and sucralfate bind and stabilize aFGF via interaction with the aFGF polyanion binding site.

Language of Publication

English

Unique Identifier

94032454

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MeSH Heading (Major)

Fibroblast Growth Factor, Acidic|*CH; Sucralfate|*PD; Sucrose|*AA/PD

MeSH Heading

Binding, Competitive|DE; Calorimetry, Differential Scanning; Circular Dichroism; Heat; Heparin; Hydrogen-Ion Concentration; Recombinant Proteins|CH; Spectrometry, Fluorescence; Suramin; Urea

Publication Type

JOURNAL ARTICLE

ISSN

0006-3002

Country of Publication

NETHERLANDS

Record 29 from database: MEDLINE
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Title

Inhibition of transcription factor IIIA-DNA interactions by xenobiotic metal ions.

Author

Hanas JS; Gunn CG

Address

Department of Biochemistry and Molecular Biology, University of Oklahoma College of Medicine, Oklahoma City 73190, USA.

Source

Nucleic Acids Res, 1996 Mar, 24:5, 924-30

Abstract

Transcription factor IIIA (TFIIIA), a cysteine-rich regulatory protein, is the prototype for the largest known superfamily of eukaryotic transcription factors. Members of the TFIIIA superfamily contain Cys2His2 zinc finger domains responsible for nucleic acid binding. Xenobiotic metal ions, which lack known biological function, were previously used as probes for the structure and function of steroid hormone receptors which contain Cys2Cys2 zinc finger domains. Structural alterations in cysteine-rich regulatory proteins by such ions in vivo might potentiate carcinogenesis and other disease processes. In the present study cadmium and other xenobiotic metal ions were used to probe the structure and function of TFIIIA. The specific interaction of TFIIIA with the internal control region (ICR) of the 5S RNA gene, as assayed by DNase I protection, was inhibited by Cd2+ ion concentrations of > or = 0.1 microM. Aluminum ions were also found to inhibit the TFIIIA-5S RNA gene interaction, albeit at higher concentrations (> or = 5 microM). Inhibition by either metal ion was not readily reversible. Other xenobiotic metal ions, such as mercury or cesium, were not found to be inhibitory under these conditions. None of these ions at the concentrations used in this study affected the ability of DNase I to digest DNA or restriction enzymes to specifically cleave DNA. Preincubation of TFIIIA bound to 5S RNA with either Cd2+ or Al3+ resulted in subsequent DNA binding upon dilution and RNA removal, whereas preincubation of free TFIIIA with the metal ions resulted in inhibition of subsequent DNA binding. Because 5S rRNA also binds the TFIIIA zinc finger domains, these results indicate that the 5S RNA bound to TFIIIA protects the protein from metal inhibition and implicates the zinc fingers in the inhibition mechanism. The nature of the footprint inhibition indicates that the N-terminal fingers of TFIIIA are affected by the metal ions. Cd2+ and Al3+ ions also inhibited the ability of TFIIIA to bind complementary single-stranded DNA and promote renaturation, as measured by Tris-phosphate agarose gel electrophoresis. This gel assay is sensitive to DNA conformation and Al3+ ions were found to alter the conformation of single- and double-stranded DNA in this assay. The inhibition of TFIIIA function in vitro by xenobiotic metals offers new insights into the structure and function of TFIIIA and TFIIIA-type zinc finger proteins. Inhibition by Cd2+ occurs at much lower concentrations than previously observed with steroid hormone receptors and suggests that Cys2His2 zinc finger proteins may be especially sensitive to such agents in vivo.

Language of Publication

English

Unique Identifier

96174660

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MeSH Heading (Major)

DNA|*ME; DNA-Binding Proteins|*ME; Transcription Factors|*ME; Xenobiotics|*PD; Xenopus laevis|GE/*ME

MeSH Heading

Animal; Metals|PD; Protein Binding|DE; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0305-1048

Country of Publication

ENGLAND

Record 30 from database: MEDLINE
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Title

Sucralfate and soluble sucrose octasulfate bind and stabilize acidic fibroblast growth factor.

Author

Volkin DB; Verticelli AM; Marfia KE; Burke CJ; Mach H; Middaugh CR

Address

Department of Pharmaceutical Research, Merck Research Laboratories, West Point, PA 19486.

Source

Biochim Biophys Acta, 1993 Nov, 1203:1, 18-26

Abstract

The actions of the anti-ulcer drug sucralfate have been proposed to be mediated through interaction with fibroblast growth factors (Folkman, J., Szabo, S., Strovroff, M., McNeil, P., Li, W. and Shing, Y. (1991) Ann. Surg. 214, 414-427). We show here that acidic fibroblast growth factor (aFGF; FGF-1) binds in vitro to both the soluble potassium salt and the insoluble aluminum salt of sucrose octasulfate, as demonstrated by a variety of biophysical techniques. Similar to the well-described interaction and stabilization of aFGF by heparin, soluble sucrose octasulfate (SOS) stabilizes aFGF against thermal, urea and acidic pH-induced unfolding as determined by a combination of circular dichroism, fluorescence spectroscopy and differential scanning calorimetry. In addition, SOS also enhances the mitogenic activity of aFGF and partially protects the protein's three cysteine residues from copper-catalyzed oxidation. SOS competes with heparin and suramin for the aFGF polyanion binding site as measured by both fluorescence and light scattering based competitive binding assays. Front-face fluorescence measurements show that the native, folded form of aFGF binds to the insoluble aluminum salt of sucrose octasulfate (sucralfate). Moreover, sucralfate stabilizes aFGF against thermal and acidic pH-induced unfolding to the same extent as observed with SOS. Thus, due to their high charge density, SOS and sucralfate bind and stabilize aFGF via interaction with the aFGF polyanion binding site.

Language of Publication

English

Unique Identifier

94032454

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MeSH Heading (Major)

Fibroblast Growth Factor, Acidic|*CH; Sucralfate|*PD; Sucrose|*AA/PD

MeSH Heading

Binding, Competitive|DE; Calorimetry, Differential Scanning; Circular Dichroism; Heat; Heparin; Hydrogen-Ion Concentration; Recombinant Proteins|CH; Spectrometry, Fluorescence; Suramin; Urea

Publication Type

JOURNAL ARTICLE

ISSN

0006-3002

Country of Publication

NETHERLANDS

Record 31 from database: MEDLINE
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Title

Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C.

Author

Morishita R; Nakayama H; Isobe T; Matsuda T; Hashimoto Y; Okano T; Fukada Y; Mizuno K; Ohno S; Kozawa O; et al

Address

Department of Biochemistry, Aichi Human Service Center, Japan.

Source

J Biol Chem, 1995 Dec, 270:49, 29469-75

Abstract

We have determined the primary structure of a novel gamma subunit (gamma 12, previously designated gamma S1) of G protein purified from bovine spleen. The mature gamma 12 protein composed of 68 amino acids had acetylated serine at the N terminus and geranylgeranylated/carboxylmethylated cysteine at the C terminus. This was consistent with the C-terminal prenylation signal in the amino acid sequence, which was predicted from gamma 12 cDNA isolated from a bovine spleen cDNA library. Western blots with the specific antibody against gamma 12 showed that gamma 12 is present in all tissues examined. Among various gamma subunits (gamma 1, gamma 2, gamma 3, gamma 7, and gamma 12), gamma 12 has a unique property to be phosphorylated by protein kinase C. The phosphorylated amino acid residue was Ser1 (or Ser2). The phosphorylated beta gamma 12 associated with Go alpha more tightly than the unphosphorylated form. Exposure of Swiss 3T3 and aortic smooth muscle cells to phorbol 12-myristate 13-acetate and NaF induced phosphorylation of gamma 12. Stimulation of aortic smooth muscle cells with natural vasoactive agents such as angiotensin II and vasopressin also induced phosphorylation of gamma 12. The extent of phosphorylation of beta gamma 12 in vitro was suppressed by a complex formation with Go alpha, which was relieved by the addition of guanosine 5'-O-(3-thiotriphosphate) or aluminum fluoride. These results strongly suggest that gamma 12 is phosphorylated by protein kinase C during activation of receptor(s) and G protein(s) in living cells.

Language of Publication

English

Unique Identifier

96094347

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MeSH Heading (Major)

G-Proteins|*CH/PH; Protein Kinase C|*PH

MeSH Heading

Amino Acid Sequence; Animal; Base Sequence; Calcium|PH; Cattle; Cells, Cultured; Molecular Sequence Data; Phosphorylation; Support, Non-U.S. Gov't; Tetradecanoylphorbol Acetate|PD

Publication Type

JOURNAL ARTICLE

ISSN

0021-9258

Country of Publication

UNITED STATES

Record 32 from database: MEDLINE
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Title

Antibody and cytotoxic T-lymphocyte responses to a single liposome-associated peptide antigen.

Author

White WI; Cassatt DR; Madsen J; Burke SJ; Woods RM; Wassef NM; Alving CR; Koenig S

Address

Department of Immunology, MedImmune Incorporated, Gaithersburg, MD 20878, USA.

Source

Vaccine, 1995 Aug, 13:12, 1111-22

Abstract

The development of peptide-based vaccines that elicit antibody (Ab) and cellular immune responses has been hampered by the lack of highly immunogenic formulations. In this study, we compared the induction of Ab and cytotoxic T-lymphocyte (CTL) responses to a peptide derived from the V3 loop of HIV-1 gp120 (P18 and its cysteine-glycine derivative (CG-P18)) when incorporated into liposomes with lipid A (LA) or mixed with aluminum hydroxide. P18-specific CTL were only observed with liposomes with LA. P18-specific Ab responses were found with liposomes containing CG-P18 but not P18. Increased surface expression of the former, resulted in enhancement of the Ab response without loss of CTL induction. Thus, the manner in which a peptide is localized can influence the outcome of the response induced by highly immunogenic liposome formulations.

Language of Publication

English

Unique Identifier

96088067

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MeSH Heading (Major)

HIV Envelope Protein gp120|AD/*IM; Peptide Fragments|AD/*IM; T-Lymphocytes, Cytotoxic|*IM

MeSH Heading

Amino Acid Sequence; Animal; Antibody Formation; Female; IgG|BL/CL; Lipid A|AD; Liposomes|AD; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type

JOURNAL ARTICLE

ISSN

0264-410X

Country of Publication

ENGLAND

Record 33 from database: MEDLINE
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Title

Influence of calcium and amino acids on the osmium impregnation of the endoplasmic reticulum.

Author

Thiery G; Bergeron M

Address

Department of Physiology, University of Montreal, QuÆebec, Canada.

Source

J Electron Microsc Tech, 1991 Mar, 17:3, 361-8

Abstract

The aim of this study was to define further the interaction between osmium and organelle content in cells prefixed with glutaraldehyde. We have studied the reaction of osmium with divalent or trivalent cations (calcium, barium, zinc, aluminum, and iron) and various amino acids in the same conditions prevalent in histological techniques, in particular with Thiéry's technique of metal impregnation. Experiments were carried out in vitro in test tubes, on cellulose acetate discs, or with an immunodiffusion apparatus. Some experiments were also carried out with tissue extracts (kidney and intestine). Our studies suggest that calcium is in general essential for the formation of osmium black, but also that lysine is reactive even in the absence of calcium and that a few amino acids--such as tryptophan, ornithine, cysteine, and aspartic acid--are only slightly reactive in the absence of calcium. Other amino acids do not seem to participate in the endoplasmic reticulum osmium impregnation even in the presence of calcium ions. Our studies also suggest that osmium reactivity reflects calcium binding sites and not only calcium content.

Language of Publication

English

Unique Identifier

91259322

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MeSH Heading (Major)

Amino Acids|*ME; Calcium|*ME; Endoplasmic Reticulum|ME/*UL; Osmium|*

MeSH Heading

Animal; Binding Sites; Diffusion; Fixatives; Glutaral; In Vitro; Kidney|CY; Rats; Support, Non-U.S. Gov't

Publication Type

JOURNAL ARTICLE

ISSN

0741-0581

Country of Publication

UNITED STATES