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Novel metalloprotease–disintegrin, meltrin ϵ (ADAM35), expressed in epithelial tissues during chick embryogenesis
Author(s) -
WatabeUchida Mitsuko,
Masuda Aki,
Shimada Naoko,
Endo Masateru,
Shimamura Kenji,
Yasuda Kunio,
SeharaFujisawa Atsuko
Publication year - 2004
Publication title -
developmental dynamics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.634
H-Index - 141
eISSN - 1097-0177
pISSN - 1058-8388
DOI - 10.1002/dvdy.20052
Subject(s) - biology , disintegrin , microbiology and biotechnology , ectodomain , metalloproteinase , morphogenesis , embryogenesis , embryo , receptor , matrix metalloproteinase , genetics , gene
Members of the ADAM ( a d isintegrin a nd m etalloprotease) family are involved in fertilization, morphogenesis, and pathogenesis. Their metalloprotease domains mediate limited proteolysis, including ectodomain shedding of membrane‐anchored growth factors and intercellular‐signaling proteins, and their disintegrin domains play regulatory roles in cell adhesion and migration. In screening for cDNAs encoding chicken ADAM proteins expressed during muscle development, we identified Meltrin ϵ as a novel member of this family. To elucidate its functions, we investigated its expression during development by using antibodies raised against its protease domain. In the somites, Meltrin ϵ protein was specifically expressed in the myotomal cells, which delaminate from the dermomyotome to form epithelial sheets. It was also found in the surface ectoderm, lens placodes, otic vesicles, and the gut epithelia. Basolateral localization of Meltrin ϵ in these epithelial cells suggests its unique roles in the organization of the epithelial tissues and development of the sensory organs and the gut. Developmental Dynamics 230:557–568, 2004. © 2004 Wiley‐Liss, Inc.