Wang Lianzijun, Qiu Zhongqiang, Lee Myeongwoo
Department of Biology, Baylor University, Waco, TX 76798, U.S.A.
MicroPubl Biol. 2021 Oct 11;2021. doi: 10.17912/micropub.biology.000485. eCollection 2021.
The amino acid sequence Arg-Gly-Asp (RGD) is a cell-binding motif for extracellular matrix proteins. Initially found in fibronectin, the RGD motif is also found in LAM-3/laminin α chain in . Laminin, a heterotrimeric glycoprotein, is a significant component of the basement membrane. Mutations in laminin subunits disrupt the extracellular matrix hence inhibit cell adhesion. This study aims to characterize the function of the RGD motif in /laminin α. Two mutations, RGE and ΔRGD, were generated. Our analysis of the mutants revealed that the RGD motif is involved in the motility of animals, suggesting that the cell-laminin interaction plays a role in regulating body contraction.
氨基酸序列精氨酸-甘氨酸-天冬氨酸(RGD)是细胞与细胞外基质蛋白结合的基序。RGD基序最初在纤连蛋白中被发现,在层粘连蛋白3/层粘连蛋白α链中也有发现。层粘连蛋白是一种异源三聚体糖蛋白,是基底膜的重要组成部分。层粘连蛋白亚基的突变会破坏细胞外基质,从而抑制细胞黏附。本研究旨在表征RGD基序在层粘连蛋白α中的功能。产生了两个突变体,即RGE和ΔRGD。我们对这些突变体的分析表明,RGD基序参与动物的运动,这表明细胞与层粘连蛋白的相互作用在调节身体收缩中发挥作用。