Literature DB >> 3497767

Collagen synthesis and degradation in vivo. Evidence for rapid rates of collagen turnover with extensive degradation of newly synthesized collagen in tissues of the adult rat.

R J McAnulty, G J Laurent.   

Abstract

Collagen turnover is now known to occur more rapidly in body tissues than traditionally believed, but the kinetics and mechanisms for degradation are still poorly understood. Here we measure collagen synthesis rates and the proportion of newly synthesized collagen (probably procollagen) which is rapidly degraded, in tissues of the adult rat after injection of [14C]-proline with a large "flooding" dose of unlabelled proline. Incorporation of [14C]-proline into lung, heart, skeletal muscle and skin collagen and its appearance as hydroxy [14C]-proline, free or in small molecular weight moieties, at various times up to one hour, suggested extremely rapid synthesis and degradation for some tissues of the adult rat. Values in heart, lung, skeletal muscle and skin (with the proportion of degradation of newly synthesized collagen shown in parentheses) were 5.2 +/- 0.7%/day (53 +/- 5%), 9.0 +/- 0.7%/day (37 +/- 2%), 2.2 +/- 0.3%/day (38 +/- 7%) and 4.4 +/- 1.3%/day (8.8 +/- 0.5%). These data provide in vivo evidence, which are consistent with the observation in isolated cells, that a proportion of newly synthesized collagen is degraded rapidly, and probably intracellularly, after its synthesis. They also indicate that collagen may be synthesized and degraded rapidly in normal rat tissues, but the mean turnover rates and the proportions of collagen degraded intracellularly vary widely between tissues.

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Year:  1987        PMID: 3497767     DOI: 10.1016/s0174-173x(87)80001-8

Source DB:  PubMed          Journal:  Coll Relat Res        ISSN: 0174-173X


  31 in total

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Journal:  Compr Physiol       Date:  2012-01       Impact factor: 9.090

5.  Racemization and isomerization of type I collagen C-telopeptides in human bone and soft tissues: assessment of tissue turnover.

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Review 6.  Matrix biomechanics and dynamics in pulmonary fibrosis.

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7.  Collagen-gelatin mixtures as wound model, and substrates for VEGF-mimetic peptide binding and endothelial cell activation.

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8.  Developmental changes in the type I procollagen processing pathway in chick-embryo cornea.

Authors:  S J Mellor; G L Atkins; D J Hulmes
Journal:  Biochem J       Date:  1991-06-15       Impact factor: 3.857

Review 9.  Extracellular matrix in lung development, homeostasis and disease.

Authors:  Yong Zhou; Jeffrey C Horowitz; Alexandra Naba; Namasivayam Ambalavanan; Kamran Atabai; Jenna Balestrini; Peter B Bitterman; Richard A Corley; Bi-Sen Ding; Adam J Engler; Kirk C Hansen; James S Hagood; Farrah Kheradmand; Qing S Lin; Enid Neptune; Laura Niklason; Luis A Ortiz; William C Parks; Daniel J Tschumperlin; Eric S White; Harold A Chapman; Victor J Thannickal
Journal:  Matrix Biol       Date:  2018-03-08       Impact factor: 11.583

10.  Determination of steady-state protein breakdown rate in vivo by the disappearance of protein-bound tracer-labeled amino acids: a method applicable in humans.

Authors:  Lars Holm; Bruce O'Rourke; David Ebenstein; Michael J Toth; Rasmus Bechshoeft; Niels-Henrik Holstein-Rathlou; Michael Kjaer; Dwight E Matthews
Journal:  Am J Physiol Endocrinol Metab       Date:  2013-02-19       Impact factor: 4.310

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