Biochemical and immunological demonstration of prostaglandin D2, E2, and F2α formation from prostaglandin H2 by various rat glutathione S-transferase isozymes

Ujihara, Mayumi; Tsuchida, Shigeki; Satoh, Keisuke; Sato, Kei; Urade, Yoshihiro

doi:10.1016/0003-9861(88)90308-6

Cited by 100 publications

(38 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The reason for the existence of such a large gene family in tobacco, and probably other species encoding proteins with similar functions, is unknown. GSTs are involved in a variety of processes, such as detoxification reactions, protection against oxidative tissue damage, and intracellular chitinase pCNT6 transport but also in the production of secondary messengers such as prostaglandins and leukotrienes (Soderstrom et al, 1985;Ujihara et al, 1988). A role for these secondary messengers in higher plants remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Further Characterization of Expression of Auxin-Induced Genes in Tobacco (Nicotiana tabacum) Cell-Suspension Cultures

et al. 1993

View full text Add to dashboard Cite

Plant hormones are known to have pleiotropic effects on growth and development. For example, the naturally occurring auxin, IAA, influences cell division, cell elongation, and differentiation. A variety of early events (time scale: seconds to hours) preceding the biological response to auxin has been described (Brummell and Hall, 1987). However, the specificity of these early responses and their significance for the occurrence of the biological response are in general far from clear. For instance, the stimulation of proton extrusion and the hyperpolarization of the plasma membrane potential are well-described rapid auxin effects. Recently, however, it was shown that both growth-promoting auxins and growth-inactive structural analogs were capable of inducing these processes (Felle et al., 1991; Peters and Felle, 1991), demonstrating that stimulation of the proton pump is a rather unspecific effect of auxin, although the activation of the H+-ATPase is indispensable for the occurrence of cell elongation.During the past few years, a number of research groups, including our own, have studied early effects of auxins on the induction of specific proteins and mRNAs (for recent reviews, see Guilfoyle, 1986;Theologis, 1986; Key, 1989).

show abstract

Section: Discussionmentioning

confidence: 99%

Further Characterization of Expression of Auxin-Induced Genes in Tobacco (Nicotiana tabacum) Cell-Suspension Cultures

et al. 1993

View full text Add to dashboard Cite

show abstract

“…The recent addition of a second membrane-associated form of PGE synthase (mPGES-2) that is linked to both COX-1 and COX-2 (Murakami et al, 2003) emphasises the potential complexity of the relationship between PGE synthases and COX-1 and COX-2. Various cytosolic glutathione S-transferases also have the ability to convert PGH 2 to PGE 2 and other PGs (Ujihara et al, 1988). Finally, TxA and PGI synthases are distinct members of the diverse cytochrome P 450 superfamily (Hara et al, 1994;Ullrich et al, 2001;Wang and Kulmacz, 2002).…”

Section: Prostanoid Biosynthetic Pathways In Mammalsmentioning

confidence: 99%

Prostaglandins in non-insectan invertebrates: recent insights and unsolved problems

Rowley

Vogan

Taylor

et al. 2005

Journal of Experimental Biology

122

View full text Add to dashboard Cite

Prostaglandins, together with thromboxanes (collectively termed prostanoids), are fatty acid derivatives of significant importance in many physiological processes. These compounds are formed following the action of cyclooxygenases (COX) and associated enzymes on C20 polyunsaturated fatty acid precursors released from phospholipids in membranes. Nearly all mammalian cell types have the biosynthetic machinery to produce at least one type of prostanoid. The same C20 fatty acid substrates can also be acted upon by lipoxygenases to produce mono-di-and trihydroxy derivatives such as leukotrienes, lipoxins and resolvins. The final route is the cytochrome P 450 pathway that can convert C20 fatty acids to hydroxylated derivatives.Collectively these compounds are called eicosanoids; the term derived from the Greek eikosi that refers to the C20 backbone in the parent fatty acid.Prostaglandins (PGs) were first discovered in the 1930s by von Euler and colleagues, who found a substance produced by the prostate gland that caused smooth muscle contraction. They christened the active substance 'prostaglandin', but it was over 30 years until the structure and mode of biosynthesis of these fatty acid derivatives became fully understood. PGs have many basic physiological functions where they act as 'local' hormones. For example, thromboxane (Tx) A 2 and prostacyclin (PGI 2 ) generated by platelets and endothelial cells, respectively, regulate the aggregatory behaviour of

show abstract

“…The deduced amino acid sequence and the tertiary structure of hematopoietic PGDS classified the enzyme as a member of the Sigma class of GSTs. The enzyme isomerizes PGH 2 to PGD 2 selectively and effectively, whereas other GST isozymes catalyze the conversion of PGH 2 nonselectively to produce PGD 2 , PGE 2 , and PGF 2␣ (23). The high specificity of PGDS for the production of PGD 2 is attributed to the unique architecture of the catalytic pocket.…”

Section: Prostaglandin (Pg)mentioning

confidence: 99%

Structural Basis of Hematopoietic Prostaglandin D Synthase Activity Elucidated by Site-directed Mutagenesis

Pinzar¹,

Miyano²,

Kanaoka³

et al. 2000

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Hematopoietic prostaglandin (PG) D synthase (PGDS)is the first identified vertebrate ortholog in the Sigma class of the glutathione S-transferase (GST) family and catalyzes both isomerization of PGH 2 to PGD 2 and conjugation of glutathione to 1-chloro-2,4-dinitrobenzene. We introduced site-directed mutations of 199, which are presumed to participate in catalysis or PGH 2 substrate binding based on the crystallographic structure. Mutants were analyzed in terms of structure, GST and PGDS activities, and activation of the glutathione thiol group. Of all the mutants, only Y8F, W104I, K112E, and L199F showed minor but substantial differences in their far-UV circular dichroism spectra from the wild-type enzyme. Y8F, R14K/E, and W104I were completely inactive. C156L/Y selectively lost only PGDS activity. K112E reduced GST activity slightly and PGDS activity markedly, whereas K198E caused a selective decrease in PGDS activity and K m for glutathione and PGH 2 in the PGDS reaction. No significant changes were observed in the catalytic activities of Y152F and L199F, although their K m for glutathione was increased. Using 5,5-dithiobis(2-nitrobenzoic acid) as an SH-selective agent, we found that only Y8F and R14E/K did not accelerate the reactivity of the glutathione thiol group under the low reactivity condition of pH 5.0. Prostaglandin (PG)1 D synthase (PGDS) is the key enzyme responsible for the formation of PGD 2 and its additional metabolites, the J series of PGs; and these prostanoids exhibit a variety of pharmacological activities and are involved in a number of physiological processes (1). For example, PGD 2 induces vasodilation and bronchoconstriction (2, 3); inhibits platelet aggregation (4); regulates body temperature (5, 6), hormone release (7), and nociception (8); and promotes sleep (9). Furthermore, ⌬ 12 -PGJ 2 inhibits the growth of various tumor cell lines (10), and 15-deoxy-⌬ 12,14 -PGJ 2 is an endogenous ligand for a nuclear receptor, peroxisome proliferator-activated receptor ␥ (11, 12).Two distinct types of PGDS have been isolated and characterized biochemically and immunologically; one is GSHdependent or hematopoietic PGDS (13,14), and the other is GSH-independent or lipocalin-type PGDS (15). Hematopoietic PGDS expressed in antigen-presenting, Kupffer, dendritic, Langerhans (16), megakaryoblastic (17), and mast (18, 19) cells of various organs is involved in the production of PGD 2 as an allergic and inflammatory mediator. In addition, it was characterized as a member of the glutathione S-transferase (GST) gene family (20), whose members are known to catalyze the conjugation of GSH to an electrophilic substrate (21).Recently, we cloned the cDNA for rat hematopoietic PGDS, crystallized the recombinant enzyme, and determined by x-ray crystallography the three-dimensional structure of the enzyme complexed with GSH (22). The deduced amino acid sequence and the tertiary structure of hematopoietic PGDS classified the enzyme as a member of the Sigma class of GSTs. The enzyme isomerizes PGH 2 to PGD 2 sele...

show abstract

Biochemical and immunological demonstration of prostaglandin D2, E2, and F2α formation from prostaglandin H2 by various rat glutathione S-transferase isozymes

Cited by 100 publications

References 28 publications

Further Characterization of Expression of Auxin-Induced Genes in Tobacco (Nicotiana tabacum) Cell-Suspension Cultures

Further Characterization of Expression of Auxin-Induced Genes in Tobacco (Nicotiana tabacum) Cell-Suspension Cultures

Prostaglandins in non-insectan invertebrates: recent insights and unsolved problems

Structural Basis of Hematopoietic Prostaglandin D Synthase Activity Elucidated by Site-directed Mutagenesis

Contact Info

Product

Resources

About