CLINICAL RELEVANCE OF PROTEINASE ACTIVATED RECEPTORS (PARS) IN THE GUT
- Proteinase-Activated Receptor-2: Physiological and Pathophysiological Roles. Coelho, A-M.; Ossovskaya, V.; Bunnett, N.W. // Current Medicinal Chemistry - Cardiovascular & Hematological Age;Mar2003, Vol. 1 Issue 1, p61
Protease-activated receptor 2 (PAR2) is the second member of a new subfamily of G-protein coupled receptors: the protease-activated receptors (PARs). At present, four different PARs have been cloned and all of them share the same basic mechanism of activation. A serine protease cleaves the...
- Non-viral Proteases. Cheronis, John C. // Encyclopedic Reference of Molecular Pharmacology;2004, p672
This encyclopedia entry provides information on non-viral proteases. They are also known as protease, proteinase, endopepetidase, exopeptidase, protein hydrolyase, peptide hydroloase and proteolytic enzymes. Non-viral proteases are enzymes capable of peptide bond cleavage either within a...
- Protease. // Encyclopedic Reference of Cancer;2001, p728
A definition of the term "protease" is presented. Also known as proteinase, it refers to an enzyme that cleaves another protein.
- Proteinase. // Encyclopedic Reference of Cancer;2001, p732
A definition of the term "proteinase" is presented. Also known as protease, it refers to an enzyme that cleaves another protein.
- Proteinase inhibitors and their function in plants: A review. Mosolov, V.; Valueva, T. // Applied Biochemistry & Microbiology;May2005, Vol. 41 Issue 3, p227
The spread, classification, and properties of plant proteins capable of inhibiting proteinases have been reviewed. Data from the literature on the likely physiological functions of these inhibitors in plants are analyzed.
- Zymogen. // Encyclopedic Reference of Cancer;2001, p981
A definition of the term "zymogen" is presented. It refers to the precursor form of a proteinase with absent or limited proteolytic activity. Activities involved in zymogen activation include removal of an auto-inhibitory domain and induction of a conformational change that alters active site...
- Phosphinic peptides as zinc metalloproteinase inhibitors. V. Dive; D. Georgiadis; M. Matziari; A. Makaritis; F. Beau; P. Cuniasse; A. Yiotakis // Cellular & Molecular Life Sciences;Aug2004, Vol. 61 Issue 16, p2010
Solid-phase synthesis of phosphinic peptides was introduced 10 years ago. A major application of this chemistry has been the development of potent synthetic inhibitors of zinc metalloproteases. Specific properties of the inhibitors produced in recent years are reviewed, supporting the notion...
- VASCULAR BIOLOGY: How not to clot. Mitchell, Alison // Nature Reviews Molecular Cell Biology;Oct2001, Vol. 2 Issue 10, p715
Discusses research being done on a small family of G-protein-coupled receptors called the protease-activated receptors (PAR). Reference to a study by Shaun Coughlin and colleagues, published in "Nature" and "Science"; Discussion on the members of the PAR family that have been identified;How...
- Degradation of myofibrillar proteins by a calpain-like proteinase in the arm muscle of Octopus vulgaris. Hatzizisis, D.; Gaitanaki, C.; Beis, I. // Journal of Comparative Physiology B: Biochemical, Systemic & Env;Jul2000, Vol. 170 Issue 5/6, p447
The effects of a calpain-like proteinase (CaDP) isolated from the arm muscle of Octopus vulgaris on the myofibrils and myofibrillar proteins isolated from the same tissue were examined. Our studies clearly showed that treatment of intact myofibrils with CaDP in the presence of 5 mM Ca2+ results...