Literature DB >> 1111595

Proline recycling during collagen metabolism as determined by concurrent 18O2-and 3H-labeling.

S H Jackson, J A Heininger.   

Abstract

In a previous study where rat skin collagen was labeled with 180 in the hydroxyl group of the collagen hydroxyproline we noticed that the decat rate of this label was much faster than had been observed when the skin collagen hydroxyproline was labeled with oH in the prolyl ring. In this study a ratwas labeled concurrently with [1802] and [3H] proline and the rate of decline of both labels was determined in rat skin collagen hydroxyproline. After correction for growth dilution of the skin collagen the [180] hydroxyproline was found to have a half-life of 27 days while the [3H] hydroxyproline had a half-life of 53 days. The decay rate of the [180] hydroxyproline represents the true turnover rate of collagen since there is no possibility of recycling this label. Hence, the difference between this and the [3H] hydroxyproline decay rate is due to recycling of L-[3H] proline into new collagen. The efficiency of recycling of proline from catabolized collagen into new collagen was about 93%.

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Year:  1975        PMID: 1111595     DOI: 10.1016/0304-4165(75)90241-x

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  12 in total

1.  In vitro phagocytosis of exogenous collagen by fibroblasts from the periodontal ligament: an electron microscopic study.

Authors:  E L Svoboda; D M Brunette; A H Melcher
Journal:  J Anat       Date:  1979-03       Impact factor: 2.610

2.  Year of birth determination using radiocarbon dating of dental enamel.

Authors:  B A Buchholz; K L Spalding
Journal:  Surf Interface Anal       Date:  2010-05-01       Impact factor: 1.607

3.  Protein turnover in the smooth muscle cell of the aortic tunica media as visualized by radioautography.

Authors:  A Terquem; J P Dadoune
Journal:  Cell Tissue Res       Date:  1977-09-14       Impact factor: 5.249

4.  Synthesis and degradation of collagens in skin of healthy and protein-malnourished rats in vivo, studied by 18O2 labelling.

Authors:  J A Molnar; N M Alpert; D A Wagner; S Miyatani; J F Burke; V R Young
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

5.  Rates of collagen synthesis in lung, skin and muscle obtained in vivo by a simplified method using [3H]proline.

Authors:  G J Laurent
Journal:  Biochem J       Date:  1982-09-15       Impact factor: 3.857

6.  Age-related changes in collagen synthesis and degradation in rat tissues. Importance of degradation of newly synthesized collagen in regulating collagen production.

Authors:  P K Mays; R J McAnulty; J S Campa; G J Laurent
Journal:  Biochem J       Date:  1991-06-01       Impact factor: 3.857

7.  Prolyl-tRNA-based rates of protein and collagen synthesis in human lung fibroblasts.

Authors:  J N Hildebran; J Airhart; W S Stirewalt; R B Low
Journal:  Biochem J       Date:  1981-08-15       Impact factor: 3.857

8.  Synthesis and degradation rates of collagens in vivo in whole skin of rats, studied with 1802 labelling.

Authors:  J A Molnar; N Alpert; J F Burke; V R Young
Journal:  Biochem J       Date:  1986-12-01       Impact factor: 3.857

9.  Prolinase activity in prolidase-deficient fibroblasts.

Authors:  G Miech; I Myara; M Mangeot; V Voigtlander; A Lemonnier
Journal:  J Inherit Metab Dis       Date:  1988       Impact factor: 4.982

10.  Characterization of a new PEPD allele causing prolidase deficiency in two unrelated patients: natural-occurrent mutations as a tool to investigate structure-function relationship.

Authors:  Anna Lupi; Antonio De Riso; Sara Della Torre; Antonio Rossi; Elena Campari; Laura Vilarinho; Giuseppe Cetta; Antonella Forlino
Journal:  J Hum Genet       Date:  2004-08-11       Impact factor: 3.172

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