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

Robin J. McAnulty , Geoffrey J. Laurent
{"title":"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","authors":"Robin J. McAnulty ,&nbsp;Geoffrey J. Laurent","doi":"10.1016/S0174-173X(87)80001-8","DOIUrl":null,"url":null,"abstract":"<div><p>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 [<sup>14</sup>C] -proline with a large “flooding” dose of unlabelled proline. Incorporation of [<sup>14</sup>C]-proline into lung, heart, skeletal muscle and skin collagen and its appearance as hydroxy [<sup>14</sup>C]-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.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 93-104"},"PeriodicalIF":0.0000,"publicationDate":"1987-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0174-173X(87)80001-8","citationCount":"157","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Collagen and related research","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0174173X87800018","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 157

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.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
体内胶原合成和降解。成年大鼠组织中新合成的胶原蛋白广泛降解导致胶原蛋白快速周转的证据
现在已知胶原蛋白在身体组织中的转化比传统认为的要快,但是降解的动力学和机制仍然知之甚少。在这里,我们测量胶原合成率和新合成的胶原(可能是前胶原)的比例,在成年大鼠的组织中,注射了大剂量的未标记的脯氨酸后,迅速降解。[14C]-脯氨酸在肺、心脏、骨骼肌和皮肤胶原蛋白中的结合,并以羟基[14C]-脯氨酸的形式出现,无论是游离的还是小分子量的,在长达1小时的不同时间内,表明在成年大鼠的某些组织中,[14C]-脯氨酸的合成和降解速度非常快。心脏、肺、骨骼肌和皮肤(其中新合成胶原的降解比例见括号)分别为5.2±0.7%/天(53±5%)、9.0±0.7%/天(37±2%)、2.2±0.3%/天(38±7%)和4.4±1.3% /天(8.8±0.5%)。这些数据提供了体内证据,这与在分离细胞中观察到的一致,即一部分新合成的胶原蛋白在合成后迅速降解,并且可能在细胞内降解。它们还表明,胶原蛋白在正常大鼠组织中可以快速合成和降解,但不同组织间胶原蛋白的平均周转率和细胞内降解的比例差异很大。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
0
期刊最新文献
Increased Collagenase Activity is not Detectable in Cervical Softening in the Ewe Abstracts From The Second International Conference On Molecular Biology And Pathology Of Matrix' Philadelphia, Pennsylvania, June 15-18,1988 Authors Index The Drosophila Homoeotic Gene Spalt is Structurally Related to Collagen αl(IV) Chain Quantitation of Collagen Fragments and Gelatin by Deconvolution of Polarimetry Denaturation Curves
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1