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J. Biol. Chem., Vol. 277, Issue 26, 23321-23329, June 28, 2002
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From the We report the isolation and
characterization of a cDNA encoding Dm2-MMP, the second
matrix metalloproteinase (MMP) identified in the Drosophila
melanogaster genome. The cloned cDNA codes for a polypeptide
of 758 residues that displays a domain organization similar to that of
other MMPs, including signal peptide, propeptide, catalytic, and
hemopexin domains. However, the structure of Dm2-MMP is
unique because of the presence of an insertion of 214 amino acids
between the catalytic and hemopexin domains that is not present in any
of the previously described MMPs. Dm2-MMP also contains a
C-terminal extension predicted to form a cleavable glycosylphosphatidylinositol anchor site. Western blot and
immunofluorescence analysis of S2 cells transfected with the isolated
cDNA confirmed that Dm2-MMP is localized at the cell
surface. Production of the catalytic domain of Dm2-MMP in
Escherichia coli and analysis of its enzymatic activity
revealed that this proteinase cleaves several synthetic peptides used
for analysis of vertebrate MMPs. This proteolytic activity was
abolished by MMP inhibitors such as BB-94, confirming that the isolated
cDNA codes for an enzymatically active metalloproteinase.
Reverse transcription-PCR analysis showed that Dm2-MMP is expressed at low levels in all of the
developmental stages of Drosophila as well as in adult
flies. However, detailed in situ hybridization at the
larval stage revealed a strong tissue-specific expression in discrete
regions of the brain and eye imaginal discs. According to these
results, we propose that Dm2-MMP plays both general
proteolytic functions during Drosophila development and in
adult tissues and specific roles in eye development and neural tissues
through the degradation and remodeling of the extracellular matrix.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AJ289232.
Structural and Enzymatic Characterization of Drosophila
Dm2-MMP, a Membrane-bound Matrix Metalloproteinase with
Tissue-specific Expression*
§,,,,,
Departamento de Bioquímica y
Biología Molecular, Facultad de Medicina, Instituto
Universitario de Oncología, Universidad de Oviedo,
33006-Oviedo, Spain and the ¶ Institut de Recherches
Signalisation, Développement et Cancer, Centre de Biochimie-UMR
6543-CNRS, Parc Valrose, 06108 Nice Cedex 2, France
*
This work was supported by Comisión Interministerial
de Ciencia y Tecnología Grant SAF00-0217, Plan Fondos Europeos
para el Desarrollo Regional Grant 1FD97-0214, a CNRS grant
(ATIPE), l'Association pour la Recherche sur le Cancer Grants
5550 and 7594, and a Fondation pour la Recherche Medicale grant. The
Instituto Universitario de Oncología is supported by Obra
Social Cajastur-Asturias.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.
To whom correspondence should be addressed: Dept. de
Bioquímica y Biología Molecular, Facultad de Medicina,
Universidad de Oviedo, 33006 Oviedo-Spain. Tel.: 34985104201;
Fax: 34985103564; E-mail: CLO@correo.uniovi.es.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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