Disease relevance of PTGS1

• Gene expression of cytosolic phospholipase A2 (cPLA2) and prostaglandin endoperoxide synthase (PGHS) 1 and 2 was studied in ovine maternal uterine and fetal tissues during glucocorticoid induced premature labor and spontaneous labor and compared with gestational age matched controls not in labor [1].

High impact information on PTGS1

• Changes in gene expression induced in tobacco leaves by the harpin HrpN protein elicitor were examined, and a new cDNA, piox (for pathogen-induced oxygenase), with homology to genes encoding cyclooxygenase or prostaglandin endoperoxide synthase (PGHS), was identified [2].
• Because some intermediate forms of prostaglandin endoperoxide synthase are spectrally indistinguishable, the enzyme and substrate transformations were monitored in parallel to simplify the interpretation of the kinetics [3].
• The importance of cysteine residues in the cyclooxygenase activity of prostaglandin endoperoxide synthase (PGHS) was investigated using cysteine-specific reagents and site-directed mutagenesis [4].
• Prostaglandin endoperoxide synthase substituted with manganese protoporphyrin IX. Formation of a higher oxidation state and its relation to cyclooxygenase reaction [5].
• Tyrosine 385 of prostaglandin endoperoxide synthase is required for cyclooxygenase catalysis [6].

Biological context of PTGS1

• The complete amino acid sequence of prostaglandin endoperoxide synthase from sheep vesicular gland has been deduced by cloning and sequence analysis of DNA complementary to its messenger RNA [7].
• Orientation of the active site and antigenic determinants of prostaglandin endoperoxide synthase in the endoplasmic reticulum [8].
• The expression of cytosolic phospholipase A2 and prostaglandin endoperoxide synthase in ovine maternal uterine and fetal tissues during late gestation and labor [1].
• The expression of prostaglandin endoperoxide synthase 2 messenger RNA and the proportion of smooth muscle and collagen in the sheep cervix during the estrous cycle [9].
• Prostaglandin-endoperoxide synthase (PTGS) (also known as cyclooxygenase) converts arachidonic acid into several prostaglandins, many of which have roles in vasodilation and vasoconstriction under normal and pathological conditions [10].

Anatomical context of PTGS1

• Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase) [11].
• Endothelial cells as well as vascular smooth muscle cells can be a source of PTGS within the artery [10].
• Incubation of 5,8,11-[1-14C]eicosatrienoic acid with prostaglandin endoperoxide synthase of ram vesicular gland microsomes led to formation of a number of polar metabolites [12].
• Ontogeny of immunoreactive prostaglandin endoperoxide synthase isoforms in ovine fetal pituitary, hypothalamus and brainstem [13].

Associations of PTGS1 with chemical compounds

• Prostaglandin endoperoxide synthase (PES, EC 1.14.99.1) catalyse the conversion of arachidonic acid into prostaglandin H2 [14].
• Inactivation of prostaglandin endoperoxide synthase by acylating derivatives of indomethacin [15].
• Oxidation of tetramethylhydrazine by prostaglandin endoperoxide synthase also resulted in the N-demethylation of tetramethylhydrazine leading to the formation of formaldehyde [16].
• Metabolism of hydrazines by prostaglandin endoperoxide synthase may be of importance in tissue containing low mixed-function oxidase activity [16].
• Reaction of manganese-reconstituted prostaglandin endoperoxide synthase (Mn-PGHS) with 15-hydroperoxyeicosatetraenoic acid (15-HPETE) generates two products in nearly equal amounts: 15-hydroxyeicosatetraenoic acid (15-HETE) and 15-ketoeicosatetraenoic acid (15-KETE) [Kulmacz et al. (1994) Biochemistry 33, 5428-5439] [17].

Other interactions of PTGS1

• Prostaglandin endoperoxide synthase activity in brain tissues decreased with the increased levels of immunoreactive PGHS-2 [18].

Analytical, diagnostic and therapeutic context of PTGS1

• In situ hybridization analysis of ovarian prostaglandin endoperoxide synthase mRNA throughout the periovulatory period of the ewe [19].

References