Dahners L E, Lester G E, Caprise P
University of North Carolina School of Medicine, Chapel Hill 27599-7055, USA.
J Orthop Res. 2000 Jul;18(4):532-6. doi: 10.1002/jor.1100180404.
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).
据报道,五肽NKISK可抑制核心蛋白聚糖(一种存在于胶原纤维表面的蛋白聚糖)与纤连蛋白(一种组织粘附分子)的结合。由于我们对与韧带或肌腱长度变化(在生长或挛缩过程中)相关的纤维-纤维结合感兴趣,因此我们研究了这种肽使纤维解离的可能性。该肽能使完整的纤维释放到悬浮液中,以便在电子显微镜下进行检查(这在成熟脊椎动物组织中以前是不可能的)。