ADM-1, a protein with metalloprotease- and disintegrin-like domains, is expressed in syncytial organs, sperm, and sheath cells of sensory organs in Caenorhabditis elegans

B Podbilewicz

Department of Biology, Technion-Israel Institute of Technology, Haifa, Israel.

A search was carried out for homologues of possible fusogenic proteins to study their function in a genetically tractable animal. The isolation, molecular, and cellular characterization of the Caenorhabditis elegans adm-1 gene (a disintegrin and metalloprotease domain) are described. A glycoprotein analogous to viral fusion proteins has been identified on the surface of guinea pig sperm (PH- 30/fertilin) and is implicated in sperm-egg fusion. adm-1 is the first reported invertebrate gene related to PH-30 and a family of proteins containing snake venom disintegrin- and metalloprotease-like domains. ADM-1 shows a domain organization identical to PH-30. It contains prepro, metalloprotease, disintegrin, cysteine rich with putative fusion peptide, epidermal growth factor-like repeat, transmembrane, and cytoplasmic domains. Antibodies which recognize ADM-1 protein in immunoblots were generated. Using immunofluorescence and in situ hybridization, the products of adm-1 have been detected in specific cells during different stages of development. The localization of ADM-1 to the plasma membrane of embryonic cells and to the sheath cells of sensory organs suggests a function in cell adhesion. ADM-1 expression in the hypodermis, pharynx, vulva, and mature sperm is consistent with a putative role in somatic and gamete cell fusions.

Volume 7, Issue 12, pp. 1877-1893, 12/01/1996
Copyright © 1996 by The American Society for Cell Biology

This article has been cited by other articles:

				D. R. Brooks, N. M. Hooper, and R. E. Isaac The Caenorhabditis elegans Orthologue of Mammalian Puromycin-sensitive Aminopeptidase Has Roles in Embryogenesis and Reproduction J. Biol. Chem., October 31, 2003; 278(44): 42795 - 42801. [Abstract] [Full Text] [PDF]

				X. Huang, P. Huang, M. K. Robinson, M. J. Stern, and Y. Jin UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates motor axon guidance and sex myoblast migration in C. elegans Development, July 15, 2003; 130(14): 3147 - 3161. [Abstract] [Full Text] [PDF]

				K. Kuno, C. Baba, A. Asaka, C. Matsushima, K. Matsushima, and R. Hosono The Caenorhabditis elegans ADAMTS Family Gene adt-1 Is Necessary for Morphogenesis of the Male Copulatory Organs J. Biol. Chem., March 29, 2002; 277(14): 12228 - 12236. [Abstract] [Full Text] [PDF]

				J. P. Evans Getting Sperm and Egg Together: Things Conserved and Things Diverged Biol Reprod, August 1, 2000; 63(2): 355b - 360. [Abstract] [Full Text]

				S. Cal, J. M.P. Freije, J. M. López, Y. Takada, and C. López-Otín ADAM 23/MDC3, a Human Disintegrin That Promotes Cell Adhesion via Interaction with the alpha vbeta 3 Integrin through an RGD-independent Mechanism Mol. Biol. Cell, April 1, 2000; 11(4): 1457 - 1469. [Abstract] [Full Text]

				R Sharma-Kishore, J. White, E Southgate, and B Podbilewicz Formation of the vulva in Caenorhabditis elegans: a paradigm for organogenesis Development, January 2, 1999; 126(4): 691 - 699. [Abstract] [PDF]

				D. Inoue, M. Reid, L. Lum, J. Kratzschmar, G. Weskamp, Y. M. Myung, R. Baron, and C. P. Blobel Cloning and Initial Characterization of Mouse Meltrin beta  and Analysis of the Expression of Four MetalloproteaseDisintegrins in Bone Cells J. Biol. Chem., February 13, 1998; 273(7): 4180 - 4187. [Abstract] [Full Text] [PDF]

				R. Yuan, P. Primakoff, and D. G. Myles A Role for the Disintegrin Domain of Cyritestin, a Sperm Surface Protein Belonging to the ADAM Family, in Mouse Sperm-Egg Plasma Membrane Adhesion and Fusion J. Cell Biol., April 7, 1997; 137(1): 105 - 112. [Abstract] [Full Text] [PDF]

				C Wen, M. Metzstein, and I Greenwald SUP-17, a Caenorhabditis elegans ADAM protein related to Drosophila KUZBANIAN, and its role in LIN-12/NOTCH signalling Development, January 12, 1997; 124(23): 4759 - 4767. [Abstract] [PDF]