Role of matrix proteases in processing enamel proteins

Authors
Citation
Jf. Woessner, Role of matrix proteases in processing enamel proteins, CONNECT TIS, 39(1-3), 1998, pp. 373-377
Citations number
30
Categorie Soggetti
da verificare
Journal title
CONNECTIVE TISSUE RESEARCH
ISSN journal
03008207 → ACNP
Volume
39
Issue
1-3
Year of publication
1998
Pages
373 - 377
Database
ISI
SICI code
0300-8207(1998)39:1-3<373:ROMPIP>2.0.ZU;2-Y
Abstract
This article reviews the current status of research on proteases of the ena mel layer that are capable of processing and degrading proteins of the enam el matrix. Following a brief survey of the historical development of this d iscipline, a summary is presented of the current status. Two proteases have recently been cloned: EMSP-1 (enamel matrix serine protease-1), a serine p rotease, 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 fea tures of these two families are outlined. The article concludes with some s uggested areas for future research-identifying further proteases and charac terizing those now known.