Assessment of Pharmacological Inhibition of PGH-Synthases in Man
Autor: | M. di Giamberardino, Francesco Cipollone, Giovanna Santini, Roberto Padovano, Maria G. Sciulli, M. T. Rotondo, M. R. Panara, Carlo Patrono, Paola Patrignani |
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Rok vydání: | 1996 |
Předmět: |
chemistry.chemical_classification
medicine.medical_specialty biology Chemistry Prostaglandin Prostanoid Prostacyclin Isozyme chemistry.chemical_compound Thromboxane A2 Endocrinology Enzyme Internal medicine medicine biology.protein lipids (amino acids peptides and proteins) Arachidonic acid Cyclooxygenase medicine.drug |
Zdroj: | Eicosanoids ISBN: 9781489902023 |
DOI: | 10.1007/978-1-4899-0200-9_4 |
Popis: | The conversion of arachidonic acid to prostaglandin(PG)H2 is catalyzed by PG-endoperoxide synthase (PGHS) which exhibits both cyclooxygenase and peroxidase activities (DeWitt, 1991). PGH2 is further metabolized by other enzymes to various prostanoids (PGs, prostacyclin and thromboxane A2). Two isozymes of PGHS are known, referred to as PGHS-1 and PGHS-2 (Smith, 1992). PGHS-1 is a constitutive enzyme present in almost all cell types (Simmons et al., 1991). Thus, PGHS-1 is the major isoform of gastrointestinal tissue (DeWitt & Smith, 1988). Prostanoid production by PGHS-1 is involved in physiological functions such as vascular homeostasis, control of kidney function and gastric cytoprotection (Smith, 1992). PGHS-2 is induced in a more restricted cell-specific fashion by mitogenic and inflammatory stimuli (Kujubu et al., 1991; Fletcher et al., 1992; O’Banion et al., 1992; Lee et al., 1992; O’Sullivan et al., 1992a; O’Sullivan et al., 1992b; Hempel et al., 1994; Patrignani et al., 1994). |
Databáze: | OpenAIRE |
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