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Papers In Press, published online ahead of print March 6, 2002
Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
Corresponding Author: takada{at}scripps.edu
ADAMs (A Disintegrin And Metalloproteases) are members of the mezisin superfamily of metalloproteases. Among integrins binding to disintegrin domains of ADAMs are
J. Biol. Chem, 10.1074/jbc.M200086200
Submitted on January 4, 2002
Revised on March 6, 2002
Accepted on March 6, 2002
Functional classification of ADAMs based on a conserved motif for binding to integrin
9
1; implications for sperm-egg binding and other cell interactions
9
1 and v3, and they bind in an RGD-independent and an RGD-dependent manner, respectively. Human ADAM15 is the only ADAM with the RGD motif in the disintegrin domain. Thus, both integrin 91 and v3 recognize the ADAM15 disintegrin domain. We determined how these integrins recognize the ADAM15 disintegrin domain by mutational analysis. We found that the Arg-481 and the Asp-Leu-Pro-Glu-Phe residues (residues 488-492) were critical for 91 binding, but the RGD motif (residues 484-486) was not. In contrast, the RGD motif was critical for v3 binding, but the other residues flanking the RGD motif were not. As the R(X6)DLPEF 91-recognition motif (residue 481-492) is conserved among ADAMs, except for ADAM10 and 17, we hypothesized that 91 may recognize disintegrin domains in all ADAMs except ADAM10 and 17. Indeed, we found that 91 bound avidly to the disintegrin domains of ADAM1, 2, 3, and 9 but not to the disintegrin domains of ADAM10 and 17. As several ADAMs have been implicated in sperm-oocyte interaction, we tested whether the functional classification of ADAMs, based on specificity for integrin 91, applies to sperm-egg binding. We found that the ADAM2 and 15 disintegrin domains bound to oocytes, but the ADAM17 disintegrin domain did not. Furthermore, the ADAM2 and 15 disintegrin domains effectively blocked binding of sperm to oocytes, but the ADAM17 disintegrin domain did not. These results suggest that oocytes and 91 have similar binding specificities for ADAMs, and that 91, or a receptor with similar specificity, may be involved in sperm-egg interaction during fertilization. As 91 is a receptor for many ADAM disintegrins, and 91 and ADAMs are widely expressed, 91-ADAM interaction may be of a broad biological importance.
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