scholarly journals Prostanoid biosynthesis and mechanisms of action

1992 ◽  
Vol 263 (2) ◽  
pp. F181-F191 ◽  
Author(s):  
W. L. Smith
Keyword(s):  
Mechanisms Of Action ◽  
Regulatory Proteins ◽  
Guanine Nucleotide ◽  
Water Reabsorption ◽  
Prostanoid Receptors ◽  
Cytosolic Phospholipase ◽  
Biological Studies ◽  
Collecting Tubule ◽  
Guanine Nucleotide Regulatory Proteins ◽  
Pg E2

Prostanoids are local hormones formed from arachidonic acid that coordinate responses to circulating hormones which elicit prostanoid synthesis. For example, in the kidney, prostaglandin (PG) E2 synthesized by collecting tubule epithelia in response to arginine vasopressin (AVP) acts on the parent collecting tubule as well as the neighboring thick limb to modulate NaCl and water reabsorption occurring in response to AVP. Studies performed over the last 15 years have defined the major cellular and subcellular sites of PG synthesis in the kidney. In addition, it is now recognized that the multiple cellular actions of prostanoids in the kidney are mediated through receptors coupled to guanine nucleotide regulatory proteins. The goal of this review is to summarize recent biochemical and molecular biological studies on prostanoid biosynthetic enzymes and on prostanoid receptors. The major topics to be addressed are 1) phospholipid precursors of arachidonate, 2) membrane-associated and cytosolic phospholipase A2s, 3) PG endoperoxide (PGH) synthase isozymes, 4) thromboxane A (TxA) synthase, and 5) TxA/PGH and PGE receptors.

scholarly journals Platelet activating factor and U44069 stimulate a GTPase activity in human platelets which is distinct from the guanine nucleotide regulatory proteins, Ns and Ni

1986 ◽  
Vol 234 (3) ◽  
pp. 737-740 ◽  
Author(s):  
M D Houslay ◽  
D Bojanic ◽  
A Wilson
Keyword(s):  
Regulatory Protein ◽  
Platelet Activating Factor ◽  
Phospholipid Metabolism ◽  
Human Platelets ◽  
Regulatory Proteins ◽  
Guanine Nucleotide ◽  
Gtpase Activity ◽  
Guanine Nucleotide Regulatory Proteins ◽  
Gtpase Activation ◽  
Guanine Nucleotide Regulatory Protein

Platelet-activating factor (PAF, 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine) and the stable thromboxane-receptor agonist U44069 (9 alpha, 11 beta-epoxymethanoprostaglandin H2) stimulated GTPase activity in platelet membranes in a dose-dependent fashion, yielding Ka values of 12 nM and 27 nM respectively. The degree of GTPase activation elicited by these agents was found to be additive with the GTPase activation due to either the stimulatory (Ns) or inhibitory (Ni) guanine nucleotide regulatory proteins when activated by prostaglandin E1 and adrenaline (+propranolol) respectively. Treatment of membranes with either cholera or pertussis toxins, which inhibited markedly the receptor-mediated stimulation of the GTPase activities of Ns and Ni respectively, had no or only a small effect, respectively, on the GTPase activity stimulated by PAF and U44069. It is suggested that PAF and U44069, which stimulate inositol phospholipid metabolism in platelets, exert actions through a guanine nucleotide regulatory protein which is distinct from Ns and Ni.

Thrombin-induced prostacyclin biosynthesis in human endothelium: Role of guanine nucleotide regulatory proteins in stimulus/coupling responses

1990 ◽  
Vol 142 (1) ◽  
pp. 186-193 ◽  
Author(s):  
Joe G. N. Garcia ◽  
Richard G. Painter ◽  
John W. Fenton ◽  
Denis English ◽  
Karleen S. Callahan
Keyword(s):  
Regulatory Proteins ◽  
Guanine Nucleotide ◽  
Guanine Nucleotide Regulatory Proteins ◽  
Human Endothelium

An intronless gene encoding a potential member of the family of receptors coupled to guanine nucleotide regulatory proteins

Nature ◽  
1987 ◽  
Vol 329 (6134) ◽  
pp. 75-79 ◽  
Author(s):  
Brian K. Kobilka ◽  
Thomas Frielle ◽  
Sheila Collins ◽  
Theresa Yang-Feng ◽  
Tong Sun Kobilka ◽  
...  
Keyword(s):  
Regulatory Proteins ◽  
Guanine Nucleotide ◽  
Gene Encoding ◽  
Intronless Gene ◽  
The Family ◽  
Guanine Nucleotide Regulatory Proteins ◽  
Potential Member

scholarly journals Evidence that adhesion of electrically permeabilized platelets to collagen is mediated by guanine nucleotide regulatory proteins

1992 ◽  
Vol 286 (3) ◽  
pp. 701-705 ◽  
Author(s):  
J L Daniel ◽  
C Dangelmaier ◽  
J B Smith
Keyword(s):  
Monoclonal Antibodies ◽  
Cytochalasin D ◽  
Regulatory Proteins ◽  
Guanine Nucleotide ◽  
Permeabilized Cells ◽  
Collagen Receptors ◽  
Kinase C ◽  
Protein Kinase C Inhibitor ◽  
Guanine Nucleotide Regulatory Proteins ◽  
Collagen Receptor

Adhesion of electrically permeabilized platelets to collagen was found to be essentially independent of free Ca2+ concentration in the medium. Addition of stable GTP analogues increased the proportion of adhering cells about 5-fold. This effect was inhibited by guanosine 5′-[beta-thio]diphosphate, cytochalasin D or monoclonal antibodies to glycoprotein Ia. In contrast, the protein kinase C inhibitor staurosporine had only a small effect on the GTP-analogue-enhanced adhesion of the permeabilized cells to collagen. These results suggest that a guanine nucleotide regulatory (G)-protein is directly linked to the collagen receptor and is involved in the actin-dependent recruitment of additional collagen receptors.

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