CD44 variants but not CD44s cooperate with β1-containing integrins to permit cells to bind to osteopontin independently of arginine-glycine- aspartic acid, thereby stimulating cell motility and chemotaxis

Yohko U. Katagiri, Jonathan Sleeman, Hideki Fujii, Peter Herrlich, Hiroshi Hotta, Kumiko Tanaka, Shunsuke Chikuma, Hideo Yagita, Ko Okumura, Masaaki Murakami, Ikuo Saiki, Ann F. Chambers, Toshimitsu Uede

研究成果: Article査読

258 被引用数 (Scopus)

抄録

The expression of osteopontin (OPN), CD44 variants, and integrins has been correlated with tumorigenesis and metastasis. Here we show that these proteins cooperate to enhance cell motility. First, we demonstrate that several different CD44 variants bind to OPN in an arginine-glycine-aspartic acid-independent manner, but that the standard form of CD44 does not. These CD44 variants bind to both the amino- and COOH-terminal portions of OPN independently of the arginine-glycine-aspartic acid sequence, suggesting that multiple domains on OPN can be bound by the CD44 variants. Antibodies directed against the integrin β1 subunit are able to inhibit this binding. The binding of CD44 variants to OPN is significantly augmented by both anti- CD44s and anti-CD44v antibodies. This augmentation by anti-CD44 antibodies is OPN specific and, again, can be blocked by anti-β1 antibodies. Finally, we show that OPN binding by CD44 variants/β1-containing integrins promotes cell spreading, motility, and chemotactic behavior.

本文言語English
ページ(範囲)219-226
ページ数8
ジャーナルCancer Research
59
1
出版ステータスPublished - 1999 1 1
外部発表はい

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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