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Article: A calcium-binding protein in bile and gallstones

TitleA calcium-binding protein in bile and gallstones
Authors
Issue Date1992
PublisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.hepatology.org/
Citation
Hepatology, 1992, v. 16 n. 6, p. 1315-1321 How to Cite?
AbstractCalcium salts are often present in the center of all types of gallstones. Matrix proteins are known to be essential for biomineralization and may therefore also be important in the formation and growth of gallstones. Other researchers have described an anionic peptide fraction of a biliary lipoprotein complex in bile and a low-molecular weight acidic glycoprotein present in gallstones. Our goal was to determine whether such a protein was present in bile and whether this protein has any calcium-binding properties. We identified a pigment-associated, highly acidic protein that precipitates from bile on addition of CaCl2 0.5 mol/L. In addition, the protein is selectively concentrated in cholesterol and pigment stones. We have, therefore, confirmed the findings of these other researchers, and we have extended the study of this protein's interactions with calcium. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrates a single band (molecular weight ≤ 14 kD) that reacts positively with cationic stains. The protein was shown to inhibit the precipitation of CaCO3 from a supersaturated solution. The capacity to bind calcium was further confirmed by autoradiography with 45Ca++ and by a membrane adsorption-binding assay. Calcium-induced aggregation was demonstrated by equilibrium dialysis and by quasielastic light scattering studies. Protein measured by Lowry's assay method and amino acid analysis constitutes only 2% to 4% of the harvested material. We speculate that a substantial lipid component may also be present. The presence of this material in bile, its ability to bind pigment and calcium, its presumed lipid content, its self-aggregation in the presence of calcium and its selective incorporation into gallstones suggest that it may play a functional role in the pathogenesis of gallstones.
Persistent Identifierhttp://hdl.handle.net/10722/175671
ISSN
2015 Impact Factor: 11.711
2015 SCImago Journal Rankings: 4.752
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorKestell, MFen_US
dc.contributor.authorSekijima, Jen_US
dc.contributor.authorLee, SPen_US
dc.contributor.authorPark, HZen_US
dc.contributor.authorLong, Men_US
dc.contributor.authorKaler, EWen_US
dc.date.accessioned2012-11-26T09:00:24Z-
dc.date.available2012-11-26T09:00:24Z-
dc.date.issued1992en_US
dc.identifier.citationHepatology, 1992, v. 16 n. 6, p. 1315-1321en_US
dc.identifier.issn0270-9139en_US
dc.identifier.urihttp://hdl.handle.net/10722/175671-
dc.description.abstractCalcium salts are often present in the center of all types of gallstones. Matrix proteins are known to be essential for biomineralization and may therefore also be important in the formation and growth of gallstones. Other researchers have described an anionic peptide fraction of a biliary lipoprotein complex in bile and a low-molecular weight acidic glycoprotein present in gallstones. Our goal was to determine whether such a protein was present in bile and whether this protein has any calcium-binding properties. We identified a pigment-associated, highly acidic protein that precipitates from bile on addition of CaCl2 0.5 mol/L. In addition, the protein is selectively concentrated in cholesterol and pigment stones. We have, therefore, confirmed the findings of these other researchers, and we have extended the study of this protein's interactions with calcium. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis demonstrates a single band (molecular weight ≤ 14 kD) that reacts positively with cationic stains. The protein was shown to inhibit the precipitation of CaCO3 from a supersaturated solution. The capacity to bind calcium was further confirmed by autoradiography with 45Ca++ and by a membrane adsorption-binding assay. Calcium-induced aggregation was demonstrated by equilibrium dialysis and by quasielastic light scattering studies. Protein measured by Lowry's assay method and amino acid analysis constitutes only 2% to 4% of the harvested material. We speculate that a substantial lipid component may also be present. The presence of this material in bile, its ability to bind pigment and calcium, its presumed lipid content, its self-aggregation in the presence of calcium and its selective incorporation into gallstones suggest that it may play a functional role in the pathogenesis of gallstones.en_US
dc.languageengen_US
dc.publisherJohn Wiley & Sons, Inc. The Journal's web site is located at http://www.hepatology.org/en_US
dc.relation.ispartofHepatologyen_US
dc.subject.meshAmino Acids - Analysisen_US
dc.subject.meshAutoradiographyen_US
dc.subject.meshBile - Metabolismen_US
dc.subject.meshCalcium - Metabolismen_US
dc.subject.meshCalcium Carbonate - Pharmacologyen_US
dc.subject.meshCalcium Radioisotopesen_US
dc.subject.meshCalcium-Binding Proteins - Isolation & Purification - Metabolismen_US
dc.subject.meshCholelithiasis - Metabolismen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshHumansen_US
dc.subject.meshKineticsen_US
dc.subject.meshMolecular Weighten_US
dc.titleA calcium-binding protein in bile and gallstonesen_US
dc.typeArticleen_US
dc.identifier.emailLee, SP: sumlee@hku.hken_US
dc.identifier.authorityLee, SP=rp01351en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1002/hep.1840160602en_US
dc.identifier.pmid1446888-
dc.identifier.scopuseid_2-s2.0-0026439238en_US
dc.identifier.volume16en_US
dc.identifier.issue6en_US
dc.identifier.spage1315en_US
dc.identifier.epage1321en_US
dc.identifier.isiWOS:A1992KB34600001-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridKestell, MF=7801543836en_US
dc.identifier.scopusauthoridSekijima, J=6506103215en_US
dc.identifier.scopusauthoridLee, SP=7601417497en_US
dc.identifier.scopusauthoridPark, HZ=7601570519en_US
dc.identifier.scopusauthoridLong, M=7203019679en_US
dc.identifier.scopusauthoridKaler, EW=7007157989en_US

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