Recombinant laminin-8 (α4β1γ1) -: Production, purification, and interactions with integrins

被引:113
作者
Kortesmaa, J
Yurchenco, P
Tryggvason, K [1 ]
机构
[1] Karolinska Inst, Dept Med Biochem & Biopys, Div Matrix Biol, S-17177 Stockholm, Sweden
[2] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Pathol, Piscataway, NJ 08854 USA
关键词
D O I
10.1074/jbc.275.20.14853
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Laminins are a large family of heterotrimeric extracellular matrix glycoproteins that, in addition to having structural roles, take part in the regulation of processes such as cell migration, differentiation, and proliferation. The laminin cu, chain is widely distributed both in adults and during development in tissues such as cardiac, skeletal and smooth muscle fibers, vascular endothelia, lungs, and in peripheral nerves. It can associate with laminin beta(1)/gamma(1) chains to form laminin-8 and with the beta(2)/gamma(1) chains to form laminin-9. Functional studies on these laminins have been hampered by poor availability of the protein in pure and soluble forms. To facilitate studies on laminin-8, recombinant laminin-8 was produced in a mammalian expression system, purified and shown to form native Y-shaped molecules in rotary shadowing electron microscopy. Integrins mediating cell adhesion to laminin-8 were identified using function-blocking mAbs. The integrin specificities were found to differ somewhat from that of laminin-l. Integrin alpha(6)beta(1) was found to be a major mediator of adhesion of HT-1080 and cultured capillary endothelial cells to laminin-8, Considering the expression patterns of laminin-8 and integrin alpha(6)beta(1) it is likely that the former is a ligand for the latter in vivo as well.
引用
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页码:14853 / 14859
页数:7
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