Skubitz A P, McCarthy J B, Charonis A S, Furcht L T
Department of Laboratory Medicine and Pathology, University of Minnesota, Minneapolis.
Invasion Metastasis. 1989;9(2):89-101.
A synthetic peptide derived from the B1 chain of laminin, F-9, as well as two peptides derived from the 33-kilodalton fragment of fibronectin, I and II, directly promoted the adhesion of K-1735-M4 metastatic murine melanoma cells. In competition assays, adhesion of these cells to laminin was inhibited by excess soluble peptide F-9. Peptides F-9, I, and II specifically bound 3H-heparin, both by direct binding assays and indirect competition assays. 3H-heparin binding to peptide F-9 was specific as determined by competition with excess unlabeled heparin, dextran sulfate, and dermatan sulfate. These findings suggest that melanoma cell surface associated heparin-like molecules may act as receptors for these domains of laminin and fibronectin.
一种源自层粘连蛋白B1链的合成肽F-9，以及两种源自纤连蛋白33千道尔顿片段的肽I和II，可直接促进K-1735-M4转移性小鼠黑色素瘤细胞的黏附。在竞争试验中，过量的可溶性肽F-9可抑制这些细胞与层粘连蛋白的黏附。通过直接结合试验和间接竞争试验，肽F-9、I和II都能特异性结合3H-肝素。通过与过量未标记的肝素、硫酸葡聚糖和硫酸皮肤素竞争确定，3H-肝素与肽F-9的结合具有特异性。这些发现表明，黑色素瘤细胞表面相关的类肝素分子可能作为层粘连蛋白和纤连蛋白这些结构域的受体。
