Hemicentins Assemble on Diverse Epithelia in the Mouse

Xuehong Xu ¹, Chun Dong ¹ and Bruce E. Vogel ^1*

¹ Program in Cell Structure and Development, Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, Maryland

^* To whom correspondence should be addressed. E-mail: vogel{at}umbi.umd.edu .

Submitted on March 17, 2006
Accepted on 9 September 2006

	Abstract

Hemicentins are recently described extracellular matrix proteins with a single ortholog in C.elegans that assembles into discrete tracks that constrict broad regions of epithelial cell contact into adhesive and flexible line-shaped junctions. There are two highly conserved hemicentin genes in most vertebrate species, however, there is nothing known about the function or distribution of vertebrate hemicentins. To determine the distribution of vertebrate hemicentins, we use a polyclonal antibody to stain mouse tissue and show that hemicentins are found in the pericellular extracellular matrix of epithelial cells in a number of tissues, including embryonic trophectoderm and adult skin and tongue, in addition to the extracellular matrix of some, but not all blood vessels. Hemicentins also assemble on multiple epithelia in the eye, including cornea, lens and retina. The pericellular localization of vertebrate hemicentins on epithelia and other cell surfaces suggests that vertebrate hemicentins, like their nematode counterpart, are secreted extracellular matrix proteins likely to have a role in the architecture of adhesive and flexible cell junctions, particularly in tissues subject to significant amounts of mechanical stress.

Key Words: extracellular matrix, basement membrane, hemidesmosome, cell adhesion

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