Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies

Yoshikazu Takada, Wilma Puzon

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183 引文 斯高帕斯(Scopus)

摘要

Members of the β1 integrin subfamily recognize multiple ligands such as fibronectin, laminin, and collagen and mediate cell-cell and cell-extracellular matrix interactions, β1 subunit may play a central role in regulating β1 integrin avidity. Here we have identified a small region of β1 subunit (residues 207-218) that is critical for the binding of both activating (8A2, A1A5, and TS2/16) and inhibiting (4B4, 4B5, 13, AIIB2, and P4C10) monoclonal antibodies against human β1 using interspecies chimeric β1 and site-directed mutagenesis. Chicken β1 that has human sequence within residues 207-218 (CH mutant) is recognized by all the human specific antibodies listed above. The region 207-218 is located between the two putative ligand binding sites (residues 120-182 and 220-231), and the amino acid sequence of the region involves a predicted bend structure. The other anti-β1 antibodies that do not affect cell . attachment to ligands (K20, 102DF5, LM442, and LM534) recognized the carboxyl-terminal regions of extracellular domain of β1 (residues 426-587 for K20 and 588-708 for 102DF5, LM442, and LM534, respectively). Our data suggest a potential mechanism for the avidity regulation of β1 integrin through conformational changes of β1 subunit.

原文英語
頁(從 - 到)17597-17601
頁數5
期刊Journal of Biological Chemistry
268
發行號23
出版狀態已發佈 - 八月 15 1993
對外發佈

ASJC Scopus subject areas

  • 生物化學

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