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J. Biol. Chem., Vol. 275, Issue 46, 35978-35985, November 17, 2000
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From the Departamento de Bioquímica y Biología
Molecular, Facultad de Medicina, Instituto Universitario de
Oncología, Universidad de Oviedo, 33006-Oviedo, Spain and the
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 involved in the extracellular matrix remodeling taking place during the development of
the central nervous system in Drosophila.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF271666.
Dm1-MMP, a Matrix Metalloproteinase from
Drosophila with a Potential Role in Extracellular Matrix
Remodeling during Neural Development*
,, and Department of Biochemistry and Biophysics, University of
California, San Francisco, California 94143
*
This work was supported by Comisión Interministerial
de Ciencia y Tecnología Spain Grant SAF97-0258, and Plan Fondos
Europeos para el Desarrollo Regional 1FD97-0214.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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