Influence of Fibronectin on the Fibrillogenesis of Type I and Type III Collagen

Maria Luisa Speranza , Giovanna Valentini , Alberto Calligaro
{"title":"Influence of Fibronectin on the Fibrillogenesis of Type I and Type III Collagen","authors":"Maria Luisa Speranza ,&nbsp;Giovanna Valentini ,&nbsp;Alberto Calligaro","doi":"10.1016/S0174-173X(87)80003-1","DOIUrl":null,"url":null,"abstract":"<div><p>The <em>in vitro</em> self-assembly of type I and type III calf skin collagen in the presence of fibronectin was studied turbidimetrically. Fibronectin delayed the fibrillogenesis of type III collagen but accelerated that of type I collagen. The effect of fibronectin was concentration-dependent.</p><p>The lag phase was more altered than the growth phase in the presence of fibronectin while the final turbidity and the amount of fibrils formed were unmodified.</p><p>Fibrils obtained in the presence of fibronectin all showed native banding pattern. Fibronectin bound partly to collagen fibrils; the amount of bound fibronectin was similar for the two types of collagen and tended to be constant at increasing fibronectin concentrations. It is suggested that the antithetic effect of fibronectin on type I and type III collagen fibrillogenesis may arise both from the different affinity of fibronectin to the two types of collagen and the different aggregation properties of each collagen type.</p></div>","PeriodicalId":77694,"journal":{"name":"Collagen and related research","volume":"7 2","pages":"Pages 115-123"},"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)80003-1","citationCount":"29","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Collagen and related research","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0174173X87800031","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 29

Abstract

The in vitro self-assembly of type I and type III calf skin collagen in the presence of fibronectin was studied turbidimetrically. Fibronectin delayed the fibrillogenesis of type III collagen but accelerated that of type I collagen. The effect of fibronectin was concentration-dependent.

The lag phase was more altered than the growth phase in the presence of fibronectin while the final turbidity and the amount of fibrils formed were unmodified.

Fibrils obtained in the presence of fibronectin all showed native banding pattern. Fibronectin bound partly to collagen fibrils; the amount of bound fibronectin was similar for the two types of collagen and tended to be constant at increasing fibronectin concentrations. It is suggested that the antithetic effect of fibronectin on type I and type III collagen fibrillogenesis may arise both from the different affinity of fibronectin to the two types of collagen and the different aggregation properties of each collagen type.

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
纤维连接蛋白对I型和III型胶原纤维形成的影响
用浊度法研究了ⅰ型和ⅲ型小牛皮肤胶原蛋白在纤维连接蛋白存在下的体外自组装。纤维连接蛋白延缓了III型胶原的纤维形成,而加速了I型胶原的纤维形成。纤维连接蛋白的作用呈浓度依赖性。在纤维连接蛋白存在的情况下,滞后期比生长期发生了更大的变化,而最终浊度和形成的原纤维数量没有改变。在纤维连接蛋白存在的情况下获得的原纤维均显示天然带型。纤维连接蛋白部分与胶原原纤维结合;两种胶原蛋白结合的纤维连接蛋白的数量相似,并且随着纤维连接蛋白浓度的增加趋于恒定。提示纤维连接蛋白对I型和III型胶原纤维形成的拮抗作用可能是由于纤维连接蛋白对两种胶原的不同亲和力以及每种胶原的不同聚集特性所致。
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