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Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-956

Lin, X; Hengartner, M O; Kolesnick, R N (1998). Caenorhabditis elegans contains two distinct acid sphingomyelinases. Journal of Biological Chemistry, 273(23):14374-14379.

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Mounting evidence supports a role for acid sphingomyelinase (ASM) in cellular stress signaling. Only murine and human sphingomyelinases have been defined at the molecular level. These enzymes are the products of a conserved gene and at the amino acid level share 82% identity. In this study, we show that the nematode Caenorhabditis elegans possesses two ASMs, termed ASM-1 and ASM-2 encoded by two distinct genes, but lacks detectable neutral sphingomyelinase activity. The C. elegans ASMs are about 30% identical with each other and with the human and murine enzymes. The conserved regions include a saposin-like domain, proline-rich domain, and a putative signal peptide. In addition, 16 cysteines distributed throughout the molecules, and selected glycosylation sites, are conserved. The expression of these genes in C. elegans is regulated during development. Asm-1 is preferentially expressed in the embryo, whereas asm-2 is predominantly expressed in postembryonic stages. When transfected as Flag-tagged proteins into COS-7 cells, ASM-1 is found almost entirely in a secreted form whereas only 20% of ASM-2 is secreted. Only the secreted forms display enzymatic activity. Furthermore, ASM-2 requires addition of Zn2+ to be fully active, whereas ASM-1 is active in the absence of cation. C. elegans is the first organism to display two ASMs. This finding suggests the existence of an ASM gene family.


23 citations in Web of Science®
22 citations in Scopus®
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Item Type:Journal Article, refereed
Communities & Collections:07 Faculty of Science > Institute of Molecular Life Sciences
Dewey Decimal Classification:570 Life sciences; biology
Date:5 June 1998
Deposited On:11 Feb 2008 12:19
Last Modified:05 Apr 2016 12:16
Publisher:American Society for Biochemistry and Molecular Biology
Publisher DOI:10.1074/jbc.273.23.14374
Related URLs:http://www.jbc.org/cgi/content/abstract/273/23/14374
PubMed ID:9603947

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