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Article: Regulation of procollagen synthesis and processing during ascorbate-induced extracellular matrix accumulation in vitro

TitleRegulation of procollagen synthesis and processing during ascorbate-induced extracellular matrix accumulation in vitro
Authors
Issue Date1990
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1990, v. 269 n. 1, p. 175-181 How to Cite?
AbstractProcollagen biosynthesis and matrix deposition were studied in long-term human skin fibroblast cultures exposed to ascorbic acid. Ascorbic acid specifically stimulated types I and III collagen synthesis, reaching a maximum at day 2 and maintaining a specific high rate of production until day 10 of ascorbate exposure, after which collagen production declined. The increased level of collagen synthesis after different exposure times could also be achieved by only brief treatment (10 h) of parallel scorbutic (ascorbic-acid-deficient) cultures with ascorbic acid. This brief exposure did not result in increased collagen mRNA, thus demonstrating that the ascorbate-induced increase in collagen synthesis at all stages of ascorbic acid exposure was due to post-transcriptional mechanisms, most likely a rapid increase in type 1 collagen mRNA translational efficiency. This mechanism, rather than the transcriptional activation, was the primary response and is adequate to explain the ascorbate-induced increase in collagen synthesis. These data also demonstrate that the presence of a collagenous extracellular matrix was not involved in this collagen biosynthetic regulation. During long-term exposure (18 days) to ascorbic acid, a substantial cross-linked collagenous matrix formed, following an approximately sigmoidal time course. The most rapid matrix deposition occurred during the later days of exposure when the rate of collagen synthesis was decreasing, suggesting that the presence of a pre-existing matrix is important for further collagen accumulation. Procollagen was also efficiently processed to collagen during this phase, demonstrating that efficient procollagen processing is an important regulatory event in collagen matrix deposition.
Persistent Identifierhttp://hdl.handle.net/10722/147352
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, Den_US
dc.contributor.authorLamande, SRen_US
dc.contributor.authorCole, WGen_US
dc.contributor.authorBateman, JFen_US
dc.date.accessioned2012-05-29T06:03:07Z-
dc.date.available2012-05-29T06:03:07Z-
dc.date.issued1990en_US
dc.identifier.citationBiochemical Journal, 1990, v. 269 n. 1, p. 175-181en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/147352-
dc.description.abstractProcollagen biosynthesis and matrix deposition were studied in long-term human skin fibroblast cultures exposed to ascorbic acid. Ascorbic acid specifically stimulated types I and III collagen synthesis, reaching a maximum at day 2 and maintaining a specific high rate of production until day 10 of ascorbate exposure, after which collagen production declined. The increased level of collagen synthesis after different exposure times could also be achieved by only brief treatment (10 h) of parallel scorbutic (ascorbic-acid-deficient) cultures with ascorbic acid. This brief exposure did not result in increased collagen mRNA, thus demonstrating that the ascorbate-induced increase in collagen synthesis at all stages of ascorbic acid exposure was due to post-transcriptional mechanisms, most likely a rapid increase in type 1 collagen mRNA translational efficiency. This mechanism, rather than the transcriptional activation, was the primary response and is adequate to explain the ascorbate-induced increase in collagen synthesis. These data also demonstrate that the presence of a collagenous extracellular matrix was not involved in this collagen biosynthetic regulation. During long-term exposure (18 days) to ascorbic acid, a substantial cross-linked collagenous matrix formed, following an approximately sigmoidal time course. The most rapid matrix deposition occurred during the later days of exposure when the rate of collagen synthesis was decreasing, suggesting that the presence of a pre-existing matrix is important for further collagen accumulation. Procollagen was also efficiently processed to collagen during this phase, demonstrating that efficient procollagen processing is an important regulatory event in collagen matrix deposition.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_US
dc.relation.ispartofBiochemical Journalen_US
dc.subject.meshAscorbic Acid - Pharmacologyen_US
dc.subject.meshCell Division - Drug Effectsen_US
dc.subject.meshChild, Preschoolen_US
dc.subject.meshCollagen - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshExtracellular Matrix - Metabolismen_US
dc.subject.meshFibroblasts - Drug Effects - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshKineticsen_US
dc.subject.meshProcollagen - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshProtein Biosynthesisen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.titleRegulation of procollagen synthesis and processing during ascorbate-induced extracellular matrix accumulation in vitroen_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.pmid2375750-
dc.identifier.scopuseid_2-s2.0-0025335666en_US
dc.identifier.volume269en_US
dc.identifier.issue1en_US
dc.identifier.spage175en_US
dc.identifier.epage181en_US
dc.identifier.isiWOS:A1990DN26800027-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridChan, D=7402216545en_US
dc.identifier.scopusauthoridLamande, SR=7004500719en_US
dc.identifier.scopusauthoridCole, WG=7201518727en_US
dc.identifier.scopusauthoridBateman, JF=16135557700en_US

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