Integrin-dependent role of human T cell matrix metalloproteinase activity in chemotaxis through a model basement membrane

Autor: Sunil P. Sreedharan, Edward J. Goetzl, Paul Dazin, Menghang Xia, Caroline H. Damsky
Rok vydání: 1996
Předmět:
Zdroj: Journal of Cellular Biochemistry. 61:452-458
ISSN: 1097-4644
0730-2312
DOI: 10.1002/(sici)1097-4644(19960601)61:3<452::aid-jcb12>3.0.co;2-l
Popis: Human T lymphoblastoma cells of the CD4+ 8+ Tsup-1 line, that express alpha4 and alpha5 but not alpha6 integrins of the beta1 family, and CD4+ human blood T cells bind vasoactive intestinal peptide (VIP) with high affinity, leading to increased adherence, secretion of matrix metalloproteinases (MMPs), and chemotaxis. VIP-enhanced adherence of T cells to fibronectin was inhibited significantly by neutralizing monoclonal antibodies to beta1 > alpha4 >> alpha5, but not to alpha6. Antibodies to beta1 and alpha4 suppressed to a similarly significant extent VIP stimulation of both MMP-dependent T cell chemotaxis through fibronectin-enriched Matrigel and T cell degradation of 3H-type IV collagen in the Matrigel, without affecting VIP-evoked secretion of MMP by suspensions of T cells. The lesser inhibition of VIP-enhanced adherence of T cells to fibronectin by anti-alpha5 antibody, than antibodies to beta1 or alpha4 chains, was associated with lesser or no suppression of MMP-dependent T cell chemotaxis through Matrigel and T cell degradation of type IV collagen in the Matrigel in response to VIP. Specific beta1 integrins thus mediate interactions of stimulated T cells with basement membranes, including adherence, localized digestion by MMPs, and chemotactic passage, that promote entry of T cells into extravascular tissues. © 1996 Wiley-Liss, Inc.
Databáze: OpenAIRE
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