title: Hemicentins: what have we learned from worms?
abstract: Hemicentins are conserved extracellular matrix proteins discovered in Caenorhabditis elegans, with orthologs in all vertebrate species including human and mouse. Hemicentins share a single, highly conserved amino-terminal von Willebrand A domain, followed by a long (>40) stretch of immunoglobulin repeats, multiple tandem epidermal growth factors and a fibulin-like carboxy-terminal module. C. elegans has a single hemicentin gene that has pleiotropic functions in transient cell contacts that are required for cell migration and basement membrane invasion and in stable contacts at hemidesmosome-mediated cell junctions and elastic fiber-like structures. Here, we summarize what is known about the function of hemicentin in C. elegans and discuss implications for hemicentin function in other species.
authors.affiliation: Program in Cell Structure and Development, Medical Biotechnology Center, University of Maryland Biotechnology Institute, 725 W. Lombard St., Baltimore, MD 21201, USA. vogel@umbi.umd.edu
authors.forename: Bruce E
authors.initials: BE
authors.lastname: Vogel
authors.forename: Joaquin M
authors.initials: JM
authors.lastname: Muriel
authors.forename: Chun
authors.initials: C
authors.lastname: Dong
authors.forename: Xuehong
authors.initials: X
authors.lastname: Xu
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000166:cytology / Q000235:genetics / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D002135:Calcium-Binding Proteins / Q000378:metabolism; D002448:Cell Adhesion / Q000502:physiology; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D009154:Mutation / Q000235:genetics
chemical_list: D029742:Caenorhabditis elegans Proteins; D002135:Calcium-Binding Proteins; D016326:Extracellular Matrix Proteins; C060820:fibulin