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Article: Comprehensive analysis of collagen metabolism in vitro using [43H]/[14C]proline dual-labeling and polyacrylamide gel electrophoresis

TitleComprehensive analysis of collagen metabolism in vitro using [43H]/[14C]proline dual-labeling and polyacrylamide gel electrophoresis
Authors
Bateman, JFHarley, VChan, DCole, WG
Keywordscell culture
collagen metabolism
electrophoresis
proline hydroxylation
Issue Date1988
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabio
Citation
Analytical Biochemistry, 1988, v. 168 n. 1, p. 171-175 How to Cite?
DOI: http://dx.doi.org/10.1016/0003-2697(88)90025-5
AbstractA method to simultaneously quantify the production, secretion, and prolyl hydroxylation of individual types of collagen in cell culture samples has been developed. Collagens were biosynthetically labeled with a mixture of [14C]proline and [4-3H]proline. The labeled collagens were isolated and their component α-chains were resolved by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Migration of the collagen α-chains was determined by fluorography, and radioactivity in excised bands was quantified by scintillation counting. [14C]proline labeling of collagen chains was used to determine the production and secretion of the different types of collagen. The ratios of the component α1(I) and α2(I) chains of type I collagen were also determined in this way. Prolyl hydroxylation of collagen α-chains was readily determined by measurement of their 3H:14C ratios. Following 4-hydroxylation, 3H was lost from the [4-3H]proline with alteration of this ratio. This dual-labeling method is suitable for the comprehensive analysis of collagen metabolism in multiple samples.
Persistent Identifierhttp://hdl.handle.net/10722/147329
ISSN
0003-2697
2023 Impact Factor: 2.6
2023 SCImago Journal Rankings: 0.493
ISI Accession Number ID
WOS:A1988L731600024

 

DC FieldValueLanguage
dc.contributor.authorBateman, JFen_US
dc.contributor.authorHarley, Ven_US
dc.contributor.authorChan, Den_US
dc.contributor.authorCole, WGen_US
dc.date.accessioned2012-05-29T06:02:57Z-
dc.date.available2012-05-29T06:02:57Z-
dc.date.issued1988en_US
dc.identifier.citationAnalytical Biochemistry, 1988, v. 168 n. 1, p. 171-175en_US
dc.identifier.issn0003-2697en_US
dc.identifier.urihttp://hdl.handle.net/10722/147329-
dc.description.abstractA method to simultaneously quantify the production, secretion, and prolyl hydroxylation of individual types of collagen in cell culture samples has been developed. Collagens were biosynthetically labeled with a mixture of [14C]proline and [4-3H]proline. The labeled collagens were isolated and their component α-chains were resolved by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. Migration of the collagen α-chains was determined by fluorography, and radioactivity in excised bands was quantified by scintillation counting. [14C]proline labeling of collagen chains was used to determine the production and secretion of the different types of collagen. The ratios of the component α1(I) and α2(I) chains of type I collagen were also determined in this way. Prolyl hydroxylation of collagen α-chains was readily determined by measurement of their 3H:14C ratios. Following 4-hydroxylation, 3H was lost from the [4-3H]proline with alteration of this ratio. This dual-labeling method is suitable for the comprehensive analysis of collagen metabolism in multiple samples.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabioen_US
dc.relation.ispartofAnalytical Biochemistryen_US
dc.subjectcell culture-
dc.subjectcollagen metabolism-
dc.subjectelectrophoresis-
dc.subjectproline hydroxylation-
dc.subject.meshCarbon Radioisotopes - Diagnostic Useen_US
dc.subject.meshCells, Cultureden_US
dc.subject.meshCollagen - Analysis - Biosynthesis - Secretionen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshFibroblasts - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydroxylationen_US
dc.subject.meshIsotope Labelingen_US
dc.subject.meshMethylationen_US
dc.subject.meshProline - Diagnostic Use - Metabolismen_US
dc.subject.meshTritium - Diagnostic Useen_US
dc.titleComprehensive analysis of collagen metabolism in vitro using [43H]/[14C]proline dual-labeling and polyacrylamide gel electrophoresisen_US
dc.typeArticleen_US
dc.identifier.emailChan, D:chand@hkucc.hku.hken_US
dc.identifier.authorityChan, D=rp00540en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/0003-2697(88)90025-5-
dc.identifier.pmid3364711en_US
dc.identifier.scopuseid_2-s2.0-0023848205en_US
dc.identifier.volume168en_US
dc.identifier.issue1en_US
dc.identifier.spage171en_US
dc.identifier.epage175en_US
dc.identifier.isiWOS:A1988L731600024-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US
dc.identifier.scopusauthoridHarley, V=35465928300en_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.issnl0003-2697-

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