The potential of laminin-2-biomimetic short peptide to promote cell adhesion, spreading and migration by inducing membrane recruitment and phosphorylation of PKC未

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• 作者：Sung Youn Jung^a ; ¹ ; ^{jsy1618@snu.ac.kr} ; Jin-Man Kim^a ; ¹ ; ^{kjinman75@hotmail.com} ; Seung-Ki Min^b ; ¹ ; ^{snowmanonmars@gmail.com} ; O. Bok Kim^a ; ^{genibok@hanmail.net} ; Da Hyun Jang^a ; ^{jdahyun@naver.com} ; Hyun Ki Kang^a ; ^{kang1978@snu.ac.kr} ; Byung-Moo Min^a ; ^{bmmin@snu.ac.kr}
• 关键词：Laminin-2 ; RNIPPFEGCIWN motif ; Cellular activity ; Integrin 伪3尾1/PKC未/FAK signaling ; Peripheral nerve regeneration
• 刊名：Biomaterials
• 出版年：2012
• 期刊代码：7_01429612
• 类别：ms
• 出版时间：May, 2012
• 卷：33
• 期：15
• 页码：3967-3979
• 文件大小：1431 K

摘要

Laminin 伪2 chain plays an important role in basement membrane assembly and peripheral myelinogenesis; however, the integrin binding motif within human laminin 伪2 chain and the signaling pathways downstream of this ligand-receptor interaction are poorly understood. We identified a motif, RNIPPFEGCIWN (Ln2-LG3-P2), within LG3 domain of human laminin 伪2 chain as a major site for both 伪3尾1 integrin and cellular activities such as cell adhesion, spreading, and migration. Binding of 伪3尾1 integrin with Ln2-LG3-P2 induced the membrane recruitment of protein kinase C未 (PKC未) and stimulated its tyrosine phosphorylation. The cellular activities induced by Ln2-LG3-P2 and the phosphorylation of focal adhesion kinase (FAK) were inhibited by rottlerin, a PKC未 inhibitor, but not by G枚6976, a PKC伪/尾 inhibitor. These results indicate that RNIPPFEGCIWN motif within human laminin 伪2 chain is a major ligand for 伪3尾1 integrin, and that binding of 伪3尾1 integrin mediates cellular activities through membrane recruitment and tyrosine phosphorylation of PKC未 and FAK phosphorylation.