Literature DB >> 11062989

Role of matrix proteases in processing enamel proteins.

J F Woessner1.   

Abstract

This article reviews the current status of research on proteases of the enamel layer that are capable of processing and degrading proteins of the enamel matrix. Following a brief survey of the historical development of this discipline, a summary is presented of the current status. Two proteases have recently been cloned: EMSP-1 (enamel matrix serine protease-1), a serine protease, and enamelysin, a metalloprotease. These two are placed into their appropriate families: the chymotrypsin family S1 of clan SA of the serine protease class and the matrixin family or matrix metalloproteinase family, M10 of clan MB (the metzincins) of the metalloprotease class. The major features of these two families are outlined. The article concludes with some suggested areas for future research--identifying further proteases and characterizing those now known.

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Year:  1998        PMID: 11062989     DOI: 10.3109/03008209809023913

Source DB:  PubMed          Journal:  Connect Tissue Res        ISSN: 0300-8207            Impact factor:   3.417


  10 in total

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Review 2.  Acute actions and novel targets of matrix metalloproteinases in the heart and vasculature.

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5.  Crystal structure of an active form of human MMP-1.

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7.  Histological, histochemical, and protein changes after induced malocclusion by occlusion alteration of Wistar rats.

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10.  Matrix metalloproteinase inhibitors enhance the efficacy of frontline drugs against Mycobacterium tuberculosis.

Authors:  Yitian Xu; Lihua Wang; Matthew D Zimmerman; Kai-Yuan Chen; Lu Huang; Dah-Jiun Fu; Firat Kaya; Nikolai Rakhilin; Evgeniya V Nazarova; Pengcheng Bu; Veronique Dartois; David G Russell; Xiling Shen
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  10 in total

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