Research OverviewExtracellular Matrix and Hemicentins
Extracellular matrix (ECM), as the name implies, is the part of a tissue that is not part of any cell, but is located outside of the cell membrane. Extracellular matrix is the defining feature of connective tissue. The ECM's main components are various proteins which often contain carbohydrate chains (glycoproteins and proteoglycans) and hyaluronic acid. Collagen, which is the most abundant protein in the body, is also the most abundant ECM protein. Other proteins include fibrin, elastin, fibronectins, laminins, and nidogens. ECM is involved in rapid and local activation of cellular functions, including intercellular communication, in addition to its function in providing anchorage, structure, or cellular support. Hemicentins are extracellular matrix proteins first discovered in the roundworm Caenorhabditis elegans, where they play a variety of roles in cell migration. Closely related proteins are found in vertebrate species, including mice and humans.
| Research DescriptionResearch Specialties: extracellular matrix protein, hemicentins The extracellular matrix (ECM) is an elaborate network of macromolecules that not only keeps cells together to form tissues, but has been demonstrated to be involved in a variety of cellular functions including proliferation, migration, differentiation and survival. While the ECM plays an irreplaceable role in the maintenance of tissue function and structure, ECM proteins have the potential to influence the life of vertebrate animals from embryogenesis and postnatal development to senescence. However, excessive acumulation or reduced activity of ECM may lead to functional abnormalities in humans. Hemicentin is a novel extracellular matrix protein newly identified in C. elegans. The functions of its two vertebrate orthologs (hemicentin-1 and hemicentin-2) are still largely unidentified. Their function in vertebrates is my major research interest, as investigation of these proteins may broaden our comprehension of human diseases such as age-related macular degeneration (ARMD). To understand the function of hemicentins in mammals, we must know their distribution. To date, we have demonstrated that the proteins are located in the periphery of the basal keratinocytes (skin cells) and in the developing hair follicle epithelial cells, including highly differentiated dermal appendix such as sebaceous glands and sweat glands. The pericellular localization of vertebrate hemicentins on epithelial cell surfaces suggests that vertebrate hemicentins have a role in tissue architecture... Complete Information...
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Representative PublicationsXuehong Xu, Chun Dong and Bruce E. Vogel, Hemicentin assemblies on diverse epithelia in the mouse, Journal of Histochemistry and Cytochemistry, 55(2):119-126 (2007) Vogel E. Bruce, Joaquin M. Muriel, Chun Dong and Xuehong Xu. Hemicentins: what have we learned from worms? Cell Research, 16(11):872-878 (2006)
Joaquin M. Muriel, Xuehong Xu, James M. Kramer and Bruce E. Vogel, Selective assembly of fibulin-1 splice variants reveals distinct extracellular matrix networks and potential functions for Perlecan/UNC-52 splice variants, Dev Dyn, 235(10): 2632-2640 (2006)
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