Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cortisol, insulin, somatotropin, thyreotropin, thyroxine, triiodothyronine, testosterone, aldosterone, c-AMP, c-GMP, prostaglandins (PGF1-x, PGF2-x, PGA + E), and renin concentrations in serum or plasma of the venous blood of the third international crew of the scientific orbital complex of "Soyuz 29 - Salyut 6 - Soyuz 31" were determined following the 7-day space flight. The increased activity of the renin-angiotensin-aldosterone system before the flight as well as variations in the pressor/depressor prostaglandin ratios indicate an increased strain during the pre-flight period. During the first stage of the post-flight period some parameters were changed due to the landing process and the returning to earth gravity. The associated physical load and the onset of reactions for enhancement of the orthostatic tolerance resulted in an increase of cyclic nucleotid and thyroxine concentrations. The relatively higher levels of the pressor PGs of group F in comparison with the prostaglandins A + E could be evaluated as a compensatory reaction for enhancement of the orthostatic tolerance. The cortisol and STH concentrations increased with growing motor activity. The variations seen after the 7-day space flight were essentially within the reference areas. It may be assumed that the readaptation was not yet totally accomplished by the 8th day after landing.
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PMID:[Results of endocrinolgic studies of the 3rd international crew of the scientific orbital station complex; Soyuz 29 - Salyut 6 - Soyuz 31 (joint space flight enterprise of the USSR - GDR). 2. Hormones and biologically active substances in blood]. 675

Research has shown that several PGs (prostaglandins) influence the following 3 major functions of the gastrointestinal tract: 1) gastric secretion; 2) motor activity; and 3) intestinal ion transport. The clinical and animal research literature on PG effects on motility and intestinal transport is summarized. PGEs and, to a lesser extent, PGF2a influence gastrointestinal motility. PGE, PGA, and PGF2a are involved in the process of water and electrolyte transport by the intestine. The article concentrates on what is known regarding PG effects on gastric secretion. The effect--inhibition of the gastric secretions--occurs in several species and in man. The inhibition includes all components of gastric juice--volume, acid, pepsin, and mucus. The effect is manifest in the basal state and in all secretogogues tested so far. The following mechanisms of action of this effect are discussed: 1) inhibition through changed gastric blood flow; 2) inhibition through a nervous mechanism; 3) operation through the cyclic AMP system; or 4) inhibition through interference with gastrin release or gastrin activity. Because certain PGs have these inhibitory effect on gastric secretions, it is possible that they can be used clinically in the treatment of peptic ulcers.
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PMID:Prostaglandins and gastric secretion. 1226 11

A particulate preparation (MgP) capable of photosynthetic CO(2) assimilation without the addition of stromal protein was obtained by rupturing whole spinach (Spinacia oleracea var. America) chloroplasts in 15 millimolar MgCl(2) buffered with Tricine at pH 8.5. This CO(2) assimilation was dependent upon light, inorganic phosphate, ferredoxin, ADP, NAD or NADP, and primer. Excepting glycolate, the products of CO(2) fixation by MgP were similar to those found with whole chloroplasts.Glycerate-3-phosphate (PGA), fructose-1, 6-bisphosphate (FBP), and ribose-5-phosphate (R5P) but not fructose-6-P (F6P) functioned as primers. Concentrations of PGA and FBP but not of R5P higher than 2 millimolar were inhibitory to CO(2) fixation. A lag of CO(2) fixation was observed with PGA and FBP but not with R5P. This lag as well as inhibition by NADP, ADP, and ATP in the FBP-primed preparation was eliminated by an equimolar mixture of FBP plus F6P indicating FBPase as the sensitive site. NADP, ADP, and ATP also blocked CO(2) fixation by the PGA-fortified preparation but inhibition was even more sensitive than that observed when FBP was added. Inhibition by AMP in the PGA and FBP-primed preparations was not affected by the addition of F6P. When R5P was the starting primer, inhibition of CO(2) fixation was relatively insensitive to the adenylates and NADP. In contrast to the parent whole chloroplast, CO(2) fixation by MgP was insensitive to high (5 millimolar) inorganic phosphate. Depending upon the ferredoxin concentration, NAD was as effective as NADP in supporting CO(2) fixation.
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PMID:Characterization of a Photosynthesizing Reconstituted Spinach Chloroplast Preparation : REGULATION BY PRIMER, ADENYLATES, FERREDOXIN, AND PYRIDINE NUCLEOTIDES. 1666 54

(14)CO(2) photoassimilation in the presence of MgATP, MgADP, and MgAMP was investigated using intact chloroplasts from Sedum praealtum, a Crassulacean acid metabolism plant, and two C(3) plants: spinach and peas. Inasmuch as free ATP, ADP, AMP, and uncomplexed Mg(2+) were present in the assays, their influence upon CO(2) assimilation was also examined. Free Mg(2+) was inhibitory with all chloroplasts, as were ADP and AMP in chloroplasts from Sedum and peas. With Sedum chloroplasts in the presence of ADP, the time course of assimilation was linear. However, with pea chloroplasts, ADP inhibition became progressively more severe, resulting in a curved time course. ATP stimulated assimilation only in pea chloroplasts. MgATP and MgADP stimulated assimilation in all chloroplasts. ADP inhibition of CO(2) assimilation was maximal at optimum orthophosphate concentrations in Sedum chloroplasts, while MgATP stimulation was maximal at optimum or below optimum concentrations of orthophosphate. MgATP stimulation in peas and Sedum and ADP inhibition in Sedum were not sensitive to the addition of glycerate 3-phosphate (PGA).PGA-supported O(2) evolution by pea chloroplasts was not inhibited immediately by ADP; the rate of O(2) evolution slowed as time passed, corresponding to the effect of ADP on CO(2) assimilation, and indicating that glycerate 3-phosphate kinase was a site of inhibition. Likewise, upon the addition of AMP, inhibition of PGA-dependent O(2) evolution became more severe with time. This did not mirror CO(2) assimilation, which was inhibited immediately by AMP. In Sedum chloroplasts, PGA-dependent O(2) evolution was not inhibited by ADP and AMP. In chloroplasts from peas and Sedum, the magnitude of MgADP and MgATP stimulation of PGA-dependent O(2) evolution was not much larger than that given by ATP, and it was much smaller than MgATP stimulation of CO(2) assimilation. Analysis of stromal metabolite levels by anion exchange chromatography indicated that ribulose 1,5-bisphosphate carboxylase was inhibited by ADP and stimulated by MgADP in Sedum chloroplasts.The appearance of label in the medium was measured when [U-(14)C] ADP-loaded Sedum chloroplasts were challenged with ATP, ADP, or AMP and their Mg(2+) complexes. The rate of back exchange was stimulated by the presence of Mg(2+). This suggests that ATP, ADP, and AMP penetrate the chloroplast slower than their Mg(2+) complexes. A portion of the CO(2) assimilation and O(2) evolution data could be explained by differential penetration rates, and other proposals were made to explain the remainder of the observations.
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PMID:Influence of adenosine phosphates and magnesium on photosynthesis in chloroplasts from peas, sedum, and spinach. 1666 88


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