Association of the tetraspanin CD151 with the laminin-binding integrinsα3β1, α6β1, α6β4 and α7β1 in cells in culture and in vivo
Author:
Sterk Lotus M. T.12, Geuijen Cecile A. W.1, van den Berg José G.3, Claessen Nike3, Weening Jan J.3, Sonnenberg Arnoud1
Affiliation:
1. Division of Cell Biology, The Netherlands Cancer Institute, Plesmanlaan 121,1066 CX Amsterdam, The Netherlands 2. Division of Pathology, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands 3. Division of Pathology, Academic Medical Center, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands
Abstract
CD151 is a cell surface protein that belongs to the tetraspanin superfamily. It forms complexes with the laminin-binding integrinsα3β1, α6β1 and α6β4 and is codistributed with these integrins in many tissues at sites of cell-matrix interactions. In this study we show that CD151 can also form stable complexes with the laminin-binding integrin α7β1. The strength of this interaction is comparable to that between CD151 and α3β1. Complexes ofα3β1, α6β1 and α7β1 with CD151 are equally well formed with all splice variants of the α3, α6 and α7 subunits, and complex formation is not affected by mutations that prevent the cleavage of the integrin α6 subunit. Like the expression ofα3β1 and α6β1, expression of α7β1 in K562 cells results in increased levels of CD151 at its surface. Two non-integrin laminin receptors, dystroglycan and the polypeptide on which the Lutheran blood group antigens are expressed, are also often colocalized with CD151, but no association with CD151-α3β1 complexes was found with biochemical analysis.The anti-CD151 antibody TS151R detects an epitope at a site at which CD151 interacts with integrins, and therefore it cannot react with CD151 when it is bound to an integrin. Comparison of the straining patterns produced by TS151R with that by of an anti-CD151 antibody recognizing an epitope outside the binding site (P48) revealed that most tissues expressing one or more laminin-binding integrins reacted with P48 but not with TS151R. However,smooth muscle cells that express α7β1 and renal tubular epithelial cells that express α6β1 were stained equally well by TS151R and P48. These results suggest that the interactions between CD151 and laminin-binding integrins are subject to cell-type-specific regulation.
Publisher
The Company of Biologists
Reference69 articles.
1. Angelisova, P., Hilgert, I. and Horejší, V.(1994). Association of four antigens of the tetraspans family(CD37, CD53, TAPA-1, and R2/C33) with MHC class II glycoproteins.Immunogenetics39, 249-256. 2. Ashman L. K., Fitter, S., Sincock, P. M., Nguyen, L. Y. and Cambareri, A. C. (1997). CD151 (PETA-3) workshop summary report. In Leukocyte typing VI. White cell differentiation antigens (ed. T. Kishimoto, H. Kikutani, A. E. G. Kr. von dem Borne, S. M. Goyert, D. Y. Mason, M. Miyasaka, L. Moretta, K. Okumura, S. Shaw, T. A. Springer, K. Sugamura and H. Zola), pp. 681-683. New York: Garland Publishing Inc. 3. Aumailley, M. and Rouselle, P. (1999). Laminins of the dermo-epidermal junction. Matrix Biol.18, 19-28. 4. Berditchevski, F. and Odintsova, E. (1999). Characterization of integrin-tetraspanin adhesion complexes: role of tetraspanins in integrin signaling. J. Cell Biol.146, 477-492. 5. Berditchevski, F., Bazzoni, G. and Hemler, M. E.(1995). Specific association of CD63 with the VLA-3 and VLA-6 integrins. J. Biol. Chem.270, 17784-17790.
Cited by
89 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
|
|