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Assignment1 of the ADAM15 gene to human chromosome band 1q21.3 by in situ hybridization

ADAM proteins (a disintegrin and metalloprotease) share the potential to mediate proteolytic, adhesion, fusion, and/or signaling reactions (Wolfsberg et al., 1995; Huovila et al., 1996; Schlöndorff and Blobel, 1999). ADAM15 contains the consensus catalytic site, indicating that it may function as an active metallo-protease (Krätzschmar et al., 1996). Also, its disintegrin domain has been shown to bind specifically to integrins ·Vß3 and ·5ß1 (Zhang et al., 1998; Nath et al., 1999). Further, ADAM15 may participate in cellular signaling or cytoskeletal interactions via its putative SH3-ligand motifs (Krätzschmar, 1996). Consistent with its potential to participate in such diverse interactions, ADAM15 has been proposed to play a role in malignancy (Wu et al., 1997). Hence we decided to determine whether the ADAM15 gene is located in a known disease susceptibility region. Indeed, the gene was localized to a region that is amplified in several cancers.