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Open Access Research article

Characterization of the astacin family of metalloproteases in C. elegans

Ja-On Park1, Jie Pan1, Frank Möhrlen2, Marcus-Oliver Schupp2, Robert Johnsen3, David L Baillie3, Richard Zapf4, Donald G Moerman4 and Harald Hutter1*

Author Affiliations

1 Department of Biological Sciences, Simon Fraser University, Burnaby, BC, Canada

2 Department of Zoology, University of Heidelberg, Heidelberg, Germany

3 Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, Canada

4 Department of Zoology, University of British Columbia, Vancouver, BC, Canada

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BMC Developmental Biology 2010, 10:14  doi:10.1186/1471-213X-10-14

Published: 28 January 2010

Abstract

Background

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 C. elegans genome contains an unusually large number of astacins, of which the majority have not been functionally characterized yet.

Results

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 nas-5, nas-21 and nas-39 (the BMP-1/Tolloid homologue) are viable and have no apparent phenotypic defects. Mutants in nas-6 and nas-6; nas-7 double mutants are slow growing and have defects in the grinder of the pharynx, a cuticular structure important for food processing.

Conclusions

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.