J Cell Sci. 1999 Nov;112 ( Pt 21):3603-17.

Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding.

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Cellular Biochemistry and Biophysics Program, Memorial Sloan Kettering Cancer Center, Box 368, Tri-Institutional (Cornell/ Rockefeller University/Sloan-Kettering Institute) MD/PhD Program, New York, NY 10021, USA.

Abstract

Metalloprotease-disintegrins (ADAMs) have captured our attention as key players in fertilization and in the processing of the ectodomains of proteins such as tumor necrosis factor (&agr;) (TNF(&agr;)), and because of their roles in Notch-mediated signaling, neurogenesis and muscle fusion. ADAMs are integral membrane glycoproteins that contain a disintegrin domain, which is related to snake-venom integrin ligands, and a metalloprotease domain (which can contain or lack a catalytic site). Here, we review and critically discuss current topics in the ADAMs field, including the central role of fertilin in fertilization, the role of the TNF(&agr;) convertase in protein ectodomain processing, the role of Kuzbanian in Notch signaling, and links between ADAMs and processing of the amyloid-precursor protein.

PMID:: 10523497; [PubMed - indexed for MEDLINE]

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Metalloendopeptidases

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