Enhancement of cell adhesion and spreading by a cartilage-specific noncollagenous protein, cartilage matrix protein (CMP/matrilin-1), via integrin

Seicho Makihira, Weiqun Yan, Shigeru Ohno, Takeshi Kawamoto, Katsumi Fujimoto, Akinobu Okimura, Eri Yoshida, Mitsuhide Noshiro, Taizo Hamada, Yukio Kato

研究成果: Contribution to journalArticle査読

66 被引用数 (Scopus)

抄録

Cartilage matrix protein (CMP; also known as matrilin-1), one of the major noncollagenous proteins in most cartilages, binds to aggrecan and type II collagen. We examined the effect of CMP on the adhesion of chondrocytes and fibroblasts using CMP-coated dishes. The CMP coating at 10-20 μg/ml enhanced the adhesion and spreading of rabbit growth plate, resting and articular chondrocytes, and fibroblasts and human epiphyseal chondrocytes and MRC5 fibroblasts. The effect of CMP on the spreading of chondrocytes was synergistically increased by native, but not heated, type II collagen (gelatin). The monoclonal antibody to integrin α1 or β1 abolished CMP- induced cell adhesion and spreading, whereas the antibody to integrin α2, α3, α5, β2, α5β1, or α(v)β5 had little effect on cell adhesion or spreading. The antibody to integrin α1, but not to other subunits, coprecipitated 125I-CMP that was added to MRC5 cell lysates, indicating the association of CMP with the integrin α1 subunit. Unlabeled CMP competed for the binding to integrin α1 with 125I-CMP. These findings suggest that CMP is a potent adhesion factor for chondrocytes, particularly in the presence of type II collagen, and that integrin α1β1 is involved in CMP- mediated cell adhesion and spreading. Since CMP is expressed almost exclusively in cartilage, this adhesion factor, unlike fibronectin or laminin, may play a special role in the development and remodeling of cartilage.

本文言語英語
ページ(範囲)11417-11423
ページ数7
ジャーナルJournal of Biological Chemistry
274
16
DOI
出版ステータス出版済み - 4 16 1999

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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