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J. Biol. Chem., Vol. 277, Issue 20, 17804-17810, May 17, 2002
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From the ADAMs (a
disintegrin and metalloproteases)
are members of the metzincin superfamily of metalloproteases.
Among integrins binding to disintegrin domains of ADAMs are
Functional Classification of ADAMs Based on a Conserved Motif for
Binding to Integrin
9
1
IMPLICATIONS FOR SPERM-EGG BINDING AND OTHER CELL
INTERACTIONS*
,,,,
Department of Cell Biology, The Scripps
Research Institute, La Jolla, California 92037, § The
Burnham Institute, La Jolla, California 92037, and the ¶ Lung
Biology Center, Center for Occupational and Environmental Health,
Cardiovascular Research Institute, and Department of Medicine,
University of California, San Francisco, California 94143
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
Arg481 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 RX6DLPEF 91
recognition motif (residues 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.
*
This work was supported by National Institutes of Health
Grants GM49899 (to Y. T.) and AR45446 (to E. E.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Cell
Biology, The Scripps Research Inst., VB-6, 10550 N. Torrey Pines Rd.,
La Jolla, CA 92037. Tel.: 858-784-7636; Fax: 858-784-7645; E-mail:
takada@scripps.edu.
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