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Published on: January 31, 2014
Collagenase 2 (MMP-8) expression in murine tissue-remodeling processes. Analysis of its potential role in postpartum
1Departamento, Facultad de Medicina, Universidad de Oviedo, Oviedo 33006, Spain.
Abstract:
Neutrophil collagenase or collagenase 2 (MMP-8) is unique among the family of matrix metalloproteinases (MMPs) because of its exclusive pattern of expression in inflammatory conditions. At present, no evidence of the occurrence of this enzyme in tissues other than human has been reported. In this work, we have cloned the murine homologue of human collagenase 2. The isolated cDNA contains an open reading frame coding for a polypeptide of 465 amino acids, which is 74% identical to its human counterpart. The mouse collagenase 2 exhibits the domain structure characteristic of several MMPs, including a signal sequence, a prodomain with the cysteine residue essential for enzyme latency, an activation locus with the Zinc-binding site, and a COOH-terminal fragment with sequence similarity to hemopexin. It also contains the three conserved residues (Tyr-209, Asp-230, and Gly-232) located around the Zinc-binding site and are distinctive of the collagenase subfamily. Northern blot analysis of RNAs isolated from a variety of mouse tissues revealed that collagenase 2 is expressed at late stages during mouse embryogenesis, coinciding with the appearance of hematopoietic cells. In addition, collagenase 2 was highly expressed in the postpartum uterus starting at 1 day postpartum and extending up to 5 days. Enzymatic analysis revealed that matrilysin, another MMP overexpressed in uterine tissue, is able to activate murine procollagenase 2. These data suggest that both enzymes could form an activation cascade resulting in the generation of the collagenolytic activity required during the process of massive connective tissue resumption occurring in the involuting uterus.
Insights
Researchers cloned mouse collagenase 2 (MMP-8), an enzyme typically found in inflammation. This matrix metalloproteinase is expressed during mouse embryogenesis and postpartum uterine involution, where it may activate collagen breakdown.
Area of Science:
- Biochemistry
- Molecular Biology
- Developmental Biology
Background:
- Neutrophil collagenase, or collagenase 2 (MMP-8), is a matrix metalloproteinase (MMP) primarily associated with inflammatory conditions.
- Its presence in tissues outside humans has not been previously documented.
Purpose of the Study:
- To clone and characterize the murine homologue of human collagenase 2.
- To investigate the expression patterns and potential activation mechanisms of mouse collagenase 2.
Main Methods:
- Cloning of the murine collagenase 2 cDNA.
- Sequence analysis to determine protein structure and identity.
- Northern blot analysis to assess tissue-specific RNA expression.
- Enzymatic assays to study activation pathways.
Main Results:
- Successfully cloned mouse collagenase 2 cDNA, encoding a 465-amino acid polypeptide 74% identical to human collagenase 2.
- Mouse collagenase 2 shares characteristic MMP domain structure, including a signal sequence, prodomain, and hemopexin-like domain.
- Northern blot revealed expression during late embryogenesis and high expression in the postpartum uterus (days 1-5).
- Matrilysin was identified as an enzyme capable of activating murine procollagenase 2 in vitro.
Conclusions:
- Murine collagenase 2 is expressed during key developmental and physiological processes, including embryogenesis and postpartum uterine remodeling.
- An activation cascade involving matrilysin and collagenase 2 is proposed for generating collagenolytic activity during uterine involution.
- These findings establish a murine model for studying collagenase 2 function in vivo.
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