A PENTAPEPTIDE FROM THE LAMININ-B1 CHAIN MEDIATES CELL-ADHESION AND BINDS THE 67000-LAMININ RECEPTOR
A PENTAPEPTIDE FROM THE LAMININ-B1 CHAIN MEDIATES CELL-ADHESION AND BINDS THE 67000-LAMININ RECEPTOR
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DOI：
10.1021/bi00396a004
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发表时间：
1987-11-03
期刊：
影响因子：
2.9
通讯作者：
KLEINMAN, HK
中科院分区：
文献类型：
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作者：
GRAF, J;OGLE, RC;KLEINMAN, HK
层粘连蛋白通过B1链上的9个氨基酸CDPGYIGSR位点促进上皮细胞粘附。使用来自该序列的较小的合成肽以及具有氨基酸取代的各种肽，我们发现有效细胞粘附以及受体结合所需的最小序列是YIGSR。肽中酪氨酸的缺失或精氨酸的取代导致活性的显著损失。在任一肽的末端精氨酸上存在酰胺基团显著增加活性。YIGSR在促进多种上皮细胞的粘附方面具有活性;然而，它对软骨细胞、成纤维细胞和成骨细胞无活性。
Laminin promotes epithelial cell adhesion in part through a site of nine amino acids CDPGYIGSR on the B1 chain. Using smaller synthetic peptides from this sequence as well as various peptides with amino acid substitutions, we find that the minimum sequence necessary for efficient cell adhesion as well as receptor binding is YIGSR. The deletion of tyrosine or the substitution of arginine in the peptides resulted in a significant loss of activity. The presence of an amide group on the terminal arginine of either peptide increases activity significantly. YIGSR is active in promoting the adhesion of a variety of epithelial cells; however, it is inactive with chondrocytes, fibroblasts, and osteoblasts.