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Research Article |
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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