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Identification, sequence analysis and expression of transcripts encoding a putative metalloproteinase, eMDC II, in
1Department of Biochemistry, University of Bristol, School of Medical Sciences, Bristol, BS8 1TD, UK.
Molecular Human Reproduction
|December 10, 1999
Summary
Researchers identified a novel metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) protein, eMDC II, in the male reproductive tract. This protein, abundant in the epididymis, shows characteristics suggesting it possesses proteolytic activity.
Area of Science:
- Biochemistry
- Molecular Biology
- Reproductive Biology
Background:
- The metalloproteinase-like, disintegrin-like, cysteine-rich (MDC) family comprises sequence-related proteins found in both reproductive and non-reproductive tissues.
- MDC proteins share domains homologous to reprolysins and snake venom hemorrhagic factors, suggesting potential enzymatic functions.
- Several MDC proteins are highly expressed in the male reproductive tract, implying roles in fertility.
Purpose of the Study:
- To clone, sequence, and characterize the human and macaque orthologues of a novel MDC family member, designated eMDC II.
- To investigate the potential proteolytic activity of eMDC II based on its conserved domains.
Main Methods:
- Cloning and sequence determination of eMDC II transcripts from human and macaque (Macaca fascicularis).
- Bioinformatic analysis of the deduced protein sequence, focusing on conserved domains and catalytic sites.
- Comparison of eMDC II sequence features with known metalloproteinases and reprolysins.
Main Results:
- The novel eMDC II gene and its transcripts were successfully cloned and sequenced in humans and macaques.
- eMDC II is abundantly expressed in the epididymis, a key site for sperm maturation.
- eMDC II exhibits an extended 'catalytic centre' consensus sequence, characteristic of active reprolysin-like metalloproteinases.
Conclusions:
- eMDC II represents a newly identified member of the MDC protein family with significant expression in the epididymis.
- The structural characteristics of eMDC II strongly suggest it possesses metalloproteinase activity.
- Further research into eMDC II's function could elucidate its role in male reproductive processes.