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Characterization of the astacin family of metalloproteases in <it>C. elegans</it>

By Zapf Richard, Baillie David L, Johnsen Robert, Schupp Marcus-Oliver, Möhrlen Frank, Pan Jie, Park Ja-On, Moerman Donald G and Hutter Harald


<p>Abstract</p> <p>Background</p> <p>Astacins are a large family of zinc metalloproteases found in bacteria and animals. They have diverse roles ranging from digestion of food to processing of extracellular matrix components. The <it>C. elegans </it>genome contains an unusually large number of astacins, of which the majority have not been functionally characterized yet.</p> <p>Results</p> <p>We analyzed the expression pattern of previously uncharacterized members of the astacin family to try and obtain clues to potential functions. Prominent sites of expression for many members of this family are the hypodermis, the alimentary system and several specialized cells including sensory sheath and sockets cells, which are located at openings in the body wall. We isolated mutants affecting representative members of the various subfamilies. Mutants in <it>nas-5</it>, <it>nas-21 </it>and <it>nas-39 </it>(the BMP-1/Tolloid homologue) are viable and have no apparent phenotypic defects. Mutants in <it>nas-6 </it>and <it>nas-6; nas-7 </it>double mutants are slow growing and have defects in the grinder of the pharynx, a cuticular structure important for food processing.</p> <p>Conclusions</p> <p>Expression data and phenotypic characterization of selected family members suggest a diversity of functions for members of the astacin family in nematodes. In part this might be due to extracellular structures unique to nematodes.</p

Topics: Biology (General), QH301-705.5, Science, Q, DOAJ:Biology, DOAJ:Biology and Life Sciences
Publisher: BioMed Central
Year: 2010
DOI identifier: 10.1186/1471-213X-10-14
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