The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissue

被引：19

作者：

Dahners, LE ^{[1
]}

Lester, GE ^{[1
]}

Caprise, P ^{[1
]}

机构：

[1] Univ N Carolina, Sch Med, Chapel Hill, NC 27599 USA

来源：

JOURNAL OF ORTHOPAEDIC RESEARCH | 2000年 / 18卷 / 04期

关键词：

D O I：

10.1002/jor.1100180404

中图分类号：

R826.8 [整形外科学]; R782.2 [口腔颌面部整形外科学]; R726.2 [小儿整形外科学]; R62 [整形外科学（修复外科学）];

学科分类号：

摘要：

The pentapeptide NKISK has been reported to inhibit the binding of decorin, a proteoglycan on the surface of collagen fibrils, to fibronectin, a tissue adhesion molecule. Because of our interest in fibril-fibril binding as it relates to changes in length of ligament or tendon (during growth or contracture), we investigated the potential of this peptide to dissociate fibrils. The peptide permitted the release of intact fibrils into suspension for examination under the electron microscope (which has not previously been possible in mature vertebrate tissues).

引用

页码：532 / 536

页数：5

共 18 条

[1]

BINKLEY JM, 1986, CLIN ORTHOP RELAT R, P301

[2] COLLAGEN FIBRILLOGENESIS IN-SITU - FIBRIL SEGMENTS UNDERGO POSTDEPOSITIONAL MODIFICATIONS RESULTING IN LINEAR AND LATERAL GROWTH DURING MATRIX DEVELOPMENT [J].