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Association of the tetraspanin CD151 with the laminin-binding integrins 3ß1, 6ß1, 6ß4 and 7ß1 in cells in culture and in vivo

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

Author of correspondence (e-mail: asonn{at}nki.nl )

Accepted 21 December 2001

CD151 is a cell surface protein that belongs to the tetraspanin superfamily. It forms complexes with the laminin-binding integrins 3ß1, 6ß1 and 6ß4 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 7ß1. The strength of this interaction is comparable to that between CD151 and 3ß1. Complexes of 3ß1, 6ß1 and 7ß1 with CD151 are equally well formed with all splice variants of the 3, 6 and 7 subunits, and complex formation is not affected by mutations that prevent the cleavage of the integrin 6 subunit. Like the expression of 3ß1 and 6ß1, expression of 7ß1 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 CD151-3ß1 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 7ß1 and renal tubular epithelial cells that express 6ß1 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.

Key words: Tetraspanin, Laminin receptor, Integrin, Dystroglycan, Lutheran blood group antigens

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