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Originally published In Press as doi:10.1074/jbc.M007674200 on December 12, 2000

J. Biol. Chem., Vol. 276, Issue 13, 10253-10262, March 30, 2001
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Identification and Enzymatic Characterization of Two Diverging Murine Counterparts of Human Interstitial Collagenase (MMP-1) Expressed at Sites of Embryo Implantation*

Milagros BalbínDagger §, Antonio Fueyo, Vera Knäuper||, José M. López**, Jesús Álvarez**, Luis M. SánchezDagger , Víctor QuesadaDagger Dagger Dagger , Javier BordalloDagger , Gillian Murphy||, and Carlos López-OtínDagger

From the Departamento de Dagger  Bioquímica y Biología Molecular,  Biología Funcional, and ** Morfología y Biología Celular, Facultad de Medicina, Instituto Universitario de Oncología, Universidad de Oviedo, 33006-Oviedo, Spain and the || School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom

Remodeling of fibrillar collagen in mouse tissues has been widely attributed to the activity of collagenase-3 (matrix metalloproteinase-13 (MMP-13)), the main collagenase identified in this species. This proposal has been largely based on the repeatedly unproductive attempts to detect the presence in murine tissues of interstitial collagenase (MMP-1), a major collagenase in many species, including humans. In this work, we have performed an extensive screening of murine genomic and cDNA libraries using as probe the full-length cDNA for human MMP-1. We report the identification of two novel members of the MMP gene family which are contained within the cluster of MMP genes located at murine chromosome 9. The isolated cDNAs contain open reading frames of 464 and 463 amino acids and are 82% identical, displaying all structural features characteristic of archetypal MMPs. Comparison for sequence similarities revealed that the highest percentage of identities was found with human interstitial collagenase (MMP-1). The new proteins were tentatively called Mcol-A and Mcol-B (Murine collagenase-like A and B). Analysis of the enzymatic activity of the recombinant proteins revealed that both are catalytically autoactivable but only Mcol-A is able to degrade synthetic peptides and type I and II fibrillar collagen. Both Mcol-A and Mcol-B genes are located in the A1-A2 region of mouse chromosome 9, Mcol-A occupying a position syntenic to the human MMP-1 locus at 11q22. Analysis of the expression of these novel MMPs in murine tissues revealed their predominant presence during mouse embryogenesis, particularly in mouse trophoblast giant cells. According to their structural and functional characteristics, we propose that at least one of these novel members of the MMP family, Mcol-A, may play roles as interstitial collagenase in murine tissues and could represent a true orthologue of human MMP-1.

* This work was supported in part by grants from the Plan Feder (1FD97-0214), EU-BIOMED II (BMH4-CT96-0017), the Arthritis and Rheumatism Council (to G. M.), and the Wellcome Trust (to V. K.). 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.

Dagger Dagger Recipient of a predoctoral fellowship from Ministerio de Educación, Spain.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AJ278461 and AJ278462.

§ To whom correspondence should be addressed: Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad de Oviedo, 33006 Oviedo, Spain. Tel.: 34-985-104202; Fax: 34-985-103564; E-mail: mbf@sauron.quimica.uniovi.es.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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