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

被引:109
作者
Antalis, Toni M. [1 ,2 ]
Buzza, Marguerite S. [1 ,2 ]
Hodge, Kathryn M. [1 ,2 ]
Hooper, John D. [3 ]
Netzel-Arnett, Sarah [1 ,2 ]
机构
[1] Univ Maryland, Sch Med, Ctr Vasc & Inflammatory Dis, Baltimore, MD 21201 USA
[2] Univ Maryland, Sch Med, Dept Physiol, Baltimore, MD 21201 USA
[3] Queensland Univ Technol, Inst Hlth & Biomed Innovat, Kelvin Grove, Qld 4059, Australia
基金
英国医学研究理事会; 美国国家卫生研究院;
关键词
membrane serine protease; pericellular proteolysis; serine protease inhibitor; type II transmembrane serine protease (TTSP); HEPATOCYTE GROWTH-FACTOR; EPITHELIAL SODIUM-CHANNEL; IRON-DEFICIENCY ANEMIA; PROATRIAL NATRIURETIC PEPTIDE; TRYPSIN-LIKE PROTEASE; AUTOSOMAL RECESSIVE ICHTHYOSIS; FACTOR ACTIVATOR INHIBITOR-1B; SALT-SENSITIVE HYPERTENSION; PROSTATE-CANCER PROGRESSION; ENTEROPEPTIDASE LIGHT-CHAIN;
D O I
10.1042/BJ20100046
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The serine proteases of the trypsin-like (S 1) 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 membrane-anchored 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 membrane-anchored 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 review discusses 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.
引用
收藏
页码:325 / 346
页数:22
相关论文
共 240 条
[51]   The serine protease Corin is a novel modifier of the agouti pathway [J].
Enshell-Seijffers, David ;
Lindon, Catherine ;
Morgan, Bruce A. .
DEVELOPMENT, 2008, 135 (02) :217-225
[52]   Identification of hepatocyte growth factor activator inhibitor-1B as a potential physiological inhibitor of prostasin [J].
Fan, B ;
Wu, TD ;
Li, W ;
Kirchhofer, D .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (41) :34513-34520
[53]   Mutations in TMPRSS6 cause iron-refractory iron deficiency anemia (IRIDA) [J].
Finberg, Karin E. ;
Heeney, Matthew M. ;
Campagna, Dean R. ;
Aydinok, Yesim ;
Pearson, Howard A. ;
Hartman, Kip R. ;
Mayo, Mary M. ;
Samuel, Stewart M. ;
Strouse, John J. ;
Markianos, Kyriacos ;
Andrews, Nancy C. ;
Fleming, Mark D. .
NATURE GENETICS, 2008, 40 (05) :569-571
[54]   Membrane-bound serine protease matriptase-2 (Tmprss6) is an essential regulator of iron homeostasis [J].
Folgueras, Alicia R. ;
Martin de Lara, Fernando ;
Pendas, Alberto M. ;
Garabaya, Cecilia ;
Rodriguez, Francisco ;
Astudillo, Aurora ;
Bernal, Teresa ;
Cabanillas, Ruben ;
Lopez-Otin, Carlos ;
Velasco, Gloria .
BLOOD, 2008, 112 (06) :2539-2545
[55]  
Förbs D, 2005, INT J ONCOL, V27, P1061
[56]   The methyl group of Nα(Me)Arg-containing peptides disturbs the active-site geometry of thrombin, impairing efficient cleavage [J].
Friedrich, R ;
Steinmetzer, T ;
Huber, R ;
Stürzebecher, J ;
Bode, W .
JOURNAL OF MOLECULAR BIOLOGY, 2002, 316 (04) :869-874
[57]   Catalytic domain structures of MT-SP1/matriptase, a matrix-degrading transmembrane serine proteinase [J].
Friedrich, R ;
Fuentes-Prior, P ;
Ong, E ;
Coombs, G ;
Hunter, M ;
Oehler, R ;
Pierson, D ;
Gonzalez, R ;
Huber, R ;
Bode, W ;
Madison, EL .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (03) :2160-2168
[58]   CVS-3983, a selective matriptase inhibitor, suppresses the growth of androgen independent prostate tumor xenografts [J].
Galkin, AV ;
Mullen, L ;
Fox, WD ;
Brown, J ;
Duncan, D ;
Moreno, O ;
Madison, EL ;
Agus, DB .
PROSTATE, 2004, 61 (03) :228-235
[59]   ENaC Proteolytic Regulation by Channel-activating Protease 2 [J].
Garcia-Caballero, Agustin ;
Dang, Yan ;
He, Hong ;
Stutts, M. Jackson .
JOURNAL OF GENERAL PHYSIOLOGY, 2008, 132 (05) :521-535
[60]   Biochemical characterization of human enteropeptidase light chain [J].
Gasparian, ME ;
Ostapchenko, VG ;
Dolgikh, DA ;
Kirpichnikov, MP .
BIOCHEMISTRY-MOSCOW, 2006, 71 (02) :113-119