2000年11月
Isolation and activity of proteolytic fragment of laminin-5 alpha 3 chain
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- 巻
- 278
- 号
- 3
- 開始ページ
- 614
- 終了ページ
- 620
- 記述言語
- 英語
- 掲載種別
- DOI
- 10.1006/bbrc.2000.3851
- 出版者・発行元
- ACADEMIC PRESS INC
Laminin-5 (alpha3 beta3 gamma2) is an important component of epithelial basement membranes. The 190-kDa alpha3 chain undergoes extracellular cleavage within the carboxyl (C) terminus consisting of five globular domains (G1 to G5), producing the mature laminin-5 with the 160-kDa alpha3 chain. To understand the physiological meaning of this processing, we isolated the C-terminal fragments of the alpha3 chain from the conditioned media of two kinds of human cell lines. The amino-terminal sequence of the fragments suggested that the cleavage occurs at Gln(1337)-Asp(1338) in the spacer region between the G3 and G4 domains. The G4-G5 fragment itself did not show significant activity, but it stimulated cell migration in the presence of a low concentration of the mature laminin-5, suggesting its regulatory role in cell migration. (C) 2000 Academic Press.
- リンク情報
- ID情報
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- DOI : 10.1006/bbrc.2000.3851
- ISSN : 0006-291X
- Web of Science ID : WOS:000165701900019