PTGS 2 ( prostaglandin - endoperoxide synthase 2 ( prostaglandin G / H synthase and cyclooxygenase ) )
نویسندگان
چکیده
COX2 is an enzyme that belongs to the prostaglandin G/H synthase family. It consists of 604 amino acids and has a molecular weight of 68996 Da. COX2 possesses two catalytic activities and respective active sites: a cyclooxygenase (COX) that converts arachidonic acid to a prostaglandin endoperoxide, prostaglandin G2 (PGG2), and; a peroxidase (POX) that reduces PGG2 to PGH2. COX2 functions as homodimer although each subunit has both a POX and a COX active site. Each subunit binds one heme B (iron-protoporphyrin IX) group. Expression
منابع مشابه
PTGS-2–PTGER2/4 Signaling Pathway Partially Protects From Diabetogenic Toxicity of Streptozotocin in Mice
Prostanoids are suggested to participate in diabetes pathology, but their roles are controversially discussed. The purpose of the current study was to examine the role of cyclooxygenase (prostaglandin synthase [PTGS]) enzymes and prostaglandin (PG) E(2) signaling pathways in streptozotocin (STZ)-induced type 1 diabetes. Blood glucose, insulin, and survival rate were studied in mice with targete...
متن کاملLack of Influence of PTGS2/COX2 Polymorphism rs5277 and Risk of Colorectal Cancer in Iran
Inflammation plays a key role in the development of colorectal cancer. Several studies revealed that inflammatory disease of the colon, such as Crohn’s disease and Ulcerative colitis, substantially increase the risk of colorectal cancer (Lennard-Jones et al., 1977; Lashner et al., 1989; Rhodes and Campbell, 2002). Prostaglandins are molecules of particular interest in the inflammatory response....
متن کاملGenetic disruption of Ptgs-1, as well as Ptgs-2, reduces intestinal tumorigenesis in Min mice.
Two isoforms of cyclooxygenase (COX) are known, and to date most studies have implicated COX-2, rather than COX-1, as the isoform involved in colon carcinogenesis. In the present study, we show that homologous disruption of either Ptgs-1 or Ptgs-2 (genes coding for COX-1 or COX-2, respectively) reduced polyp formation in Min/+ mice by approximately 80%. Only COX-1 protein was immunohistochemica...
متن کاملProstaglandin endoperoxide H synthase expression in human thyroid epithelial cells.
KAT-50, an established human thyrocyte cell line, expresses constitutively high levels of prostaglandin endoperoxide H synthase-2 (PGHS-2), the inflammatory cyclooxygenase. Here, we examine primary human thyrocytes. We find that they, too, express PGHS-2 mRNA and protein under control culture conditions. A substantial fraction of the basal prostaglandin E(2) (PGE(2)) produced by these cells can...
متن کاملDifferential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs.
Murine prostaglandin endoperoxide (PGH) synthase-1 and PGH synthase-2 expressed in cos-1 cells were found to be differentially sensitive to inhibition by common nonsteroidal anti-inflammatory drugs (NSAIDs). Aspirin completely inhibited bis-oxygenation of arachidonate by PGH synthase-1; in contrast, aspirin-treated PGH synthase-2 metabolized arachidonate primarily to 15-hydroxyeicosatetraenoic ...
متن کامل