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Dm1-MMP, a Matrix Metalloproteinase fromDrosophila with a Potential Role in Extracellular Matrix Remodeling during Neural Development

Llano, Elena, Pendás, Alberto M., Aza-Blanc, Pedro, Kornberg, Thomas B., López-Otı́n, Carlos·2000·Journal of Biological Chemistry
DOI 10.1074/jbc.m006045200
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Abstract

We have cloned and characterized a cDNA encoding Dm1-MMP, the first matrix metalloproteinase (MMP) identified in Drosophila melanogaster. The isolated cDNA encodes a protein of 541 residues that has a domain organization identical to that of most vertebrate MMPs including a signal sequence, a prodomain with the activation locus, a catalytic domain with a zinc-binding site, and a COOH-terminal hemopexin domain. Northern blot analysis of Dm1-MMP expression in embryonic and larval adult tissues revealed a strong expression level in the developing embryo at 10-22 h, declining thereafter and being undetectable in adults. Western blot analysis confirmed the presence of pro- and active forms of Dm1-MMP in vivo during larval development. In situ hybridization experiments demonstrated that Dm1-MMP is expressed in a segmented pattern in cell clusters at the midline during embryonic stage 12-13, when neurons of the central nervous system start to arise. Recombinant Dm1-MMP produced in Escherichia coli exhibits a potent proteolytic activity against synthetic peptides used for analysis of vertebrate MMPs. This activity is inhibited by tissue inhibitors of metalloproteinases and by synthetic MMP inhibitors such as BB-94. Furthermore, Dm1-MMP is able to degrade the extracellular matrix and basement membrane proteins fibronectin and type IV collagen. On the basis of these data, together with the predominant expression of Dm1-MMP in embryonic neural cells, we propose that this enzyme may be i…

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Metadata

Authors
Llano, E., Pendás, A. M., Aza-Blanc, P., Kornberg, T. B., & López-Otı́n, C.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2000-11
Volume
275
Issue
46
Pages
35978-35985
ISSN
0021-9258
DOI
10.1074/jbc.m006045200
Cited by
104
References
0
Language
en
Status
Retracted
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