Kleinman H K, Graf J, Iwamoto Y, Sasaki M, Schasteen C S, Yamada Y, Martin G R, Robey F A
Laboratory of Developmental Biology and Anomalies, National Institutes of Health, Bethesda, Maryland 20892.
Arch Biochem Biophys. 1989 Jul;272(1):39-45. doi: 10.1016/0003-9861(89)90192-6.
Previously we reported that a pentapeptide (Tyr-Ile-Gly-Ser-Arg or YIGSR) from domain III of the B1 chain of laminin is a cell attachment site with the ability to stimulate cell adhesion and migration and to block experimental metastases. Here we report studies on the activities of synthetic peptides that cover domain III and report a second biologically active peptide PDSGR from this domain with activities similar to YIGSR. We also show that cyclic YIGSR is more potent in these assays than the linear peptide as expected since this sequence on laminin is bracketed by cysteines. Due to their proximity and similar spectrum of activities, it is possible that these sequences act in concert in the native laminin molecule.
此前我们报道,层粘连蛋白B1链结构域III中的一个五肽(酪氨酸-异亮氨酸-甘氨酸-丝氨酸-精氨酸或YIGSR)是一个细胞附着位点,具有刺激细胞黏附和迁移以及阻断实验性转移的能力。在此我们报告了对覆盖结构域III的合成肽活性的研究,并报道了该结构域中的第二个生物活性肽PDSGR,其活性与YIGSR相似。我们还表明,正如预期的那样,环化YIGSR在这些测定中比线性肽更有效,因为层粘连蛋白上的这个序列被半胱氨酸包围。由于它们位置相近且活性谱相似,这些序列有可能在天然层粘连蛋白分子中协同发挥作用。