The cutting edge: Membrane-anchored serine protease activities in the pericellular microenvironment

Antalis, Toni M., Buzza, Marguerite S., Hodge, Kathryn M., Hooper, John D. and Netzel-Arnett, Sarah (2010) The cutting edge: Membrane-anchored serine protease activities in the pericellular microenvironment. Biochemical Journal, 428 3: 325-346. doi:10.1042/BJ20100046


Author Antalis, Toni M.
Buzza, Marguerite S.
Hodge, Kathryn M.
Hooper, John D.
Netzel-Arnett, Sarah
Title The cutting edge: Membrane-anchored serine protease activities in the pericellular microenvironment
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 0264-6021
1470-8728
Publication date 2010-06-15
Year available 2010
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1042/BJ20100046
Open Access Status Not yet assessed
Volume 428
Issue 3
Start page 325
End page 346
Total pages 22
Place of publication London, United Kingdom
Publisher Portland Press
Language eng
Subject 1303 Specialist Studies in Education
1307 Cell Biology
1312 Molecular Biology
2700 Medicine
Abstract The serine proteases of the trypsin-like (S1) family play critical roles in many key biological processes including digestion, blood coagulation, and immunity. Members of this family contain N- or C-terminal domains that serve to tether the serine protease catalytic domain directly to the plasma membrane. These membraneanchored serine proteases are proving to be key components of the cell machinery for activation of precursor molecules in the pericellular microenvironment, playing vital functions in the maintenance of homoeostasis. Substrates activated by membraneanchored serine proteases include peptide hormones, growth and differentiation factors, receptors, enzymes, adhesion molecules and viral coat proteins. In addition, new insights into our understanding of the physiological functions of these proteases and their involvement in human pathology have come from animal models and patient studies.The present reviewdiscusses emerging evidence for the diversity of this fascinating group of membrane serine proteases as potent modifiers of the pericellular microenvironment through proteolytic processing of diverse substrates. We also discuss the functional consequences of the activities of these proteases on mammalian physiology and disease.
Keyword Membrane serine protease
Pericellular proteolysis
Serine protease inhibitor
Type II transmembrane serine protease (TTSP)
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID CA098369
075-07
0145-00
384359
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collection: Mater Research Institute-UQ (MRI-UQ)
 
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