Disease relevance of phosphoserine

• The tissue content of L-phosphoserine was also sensitive to anoxia, falling almost fivefold within 5 min after the liver was removed [1].
• CONCLUSIONS: After a total ischemia duration of 3 h there were signs of damage to the phospholipid membrane of the rat skeletal muscle, as demonstrated by the elevation of OPS and the few or no oxidative changes in the cell [2].

Psychiatry related information on phosphoserine

• This may indicate a physiologically relevant action of L-phosphoserine in Alzheimer's disease brain because whole brain concentrations may reach over 1 mM [3].

High impact information on phosphoserine

• This inhibition can also be brought about by aspartate, 2-amino-4-phosphonobutanoate, and L-phosphoserine, a product of endogenous phosphatidylserine hydrolysis [4].
• Cysteine biosynthesis in trichomonas vaginalis involves cysteine synthase utilizing O-phosphoserine [5].
• The sites identified corresponded to major sites of phosphorylation as determined by direct quantitation of O-phosphoserine [6].
• Measurements of the weights of the explants, their mineral and protein components, and the EDTA-extractable proteins established that bone tissue synthesizes O-phosphoserine- and O-phosphothreonine-containing phosphoproteins which are similar to those present in embryonic and postnatal chicken bone matrix [7].
• Phosphorus-31 nuclear magnetic resonance chemical shielding tensors of L-O-serine phosphate and 3'-cytidine monophosphate [8].

Chemical compound and disease context of phosphoserine

• Even when there were major changes in the individual components of, such as a fivefold drop in L-phosphoserine and a sevenfold fall in alpha-ketoglutarate following 5 min of anoxia, remained relatively unchanged (2.7 X 10(-4) [1].
• The skeletal muscle of rats submitted to total ischemia of 3 h duration showed increased OPS release (2.69 +/- 4.52 vs 8.03 +/- 7.20; n = 10; P = 0.024) and no change in reduced and oxidized glutathione, glutamine synthetase, protein carbonyl, or malondialdehyde [2].
• Muscle biopsies were taken after ischemia and reperfusion and the parameters indicating oxidative stress (reduced and oxidized glutathione, malondialdehyde, glutamine synthetase, protein carbonyl) and O-phosphoserine (OPS) alterations were analyzed [2].

Biological context of phosphoserine

• Hydrolysis of the nucleotidyl-peptide with 5.8 M HCl at 110 degrees C for 90 min yielded O-phosphoserine [9].
• The IC50 of L-phosphoserine in these studies varies from 373 to 721 microM [3].
• The objective of the present study was to investigate oxidative stress based on indicators of oxygen free radical activity and on the changes in behavior of the lipoprotein membrane (O-phosphoserine) in the skeletal muscle of rats [2].
• The authors studied the relative bioequivalence and bioavailability of two oral polyamino-acid formulations (packet and flacon), based on 4 amino acids (L-glutamine, L-phosphoserine, L-phosphothreonine and L-arginine) in association with vitamin B12 (Bio-logos, Sigma Tau Pharma S.A) [10].

Anatomical context of phosphoserine

• O-phosphoserine content of intermediate filament subunits [11].
• The coreceptor was inhibited by phospho-l-serine and to a lesser extent by phospho-d-serine but not by phospho-l-threonine, which is consistent with the coreceptor functioning in the adherence and ingestion of erythrocytes via recognition of PS [12].
• Inhibition of cytosolic human forebrain choline acetyltransferase activity by phospho-L-serine: a phosphomonoester that accumulates during early stages of Alzheimer's disease [13].
• We have performed a series of experiments which demonstrate that (a) an inhibitor of cytosolic human brain choline acetyltransferase is present in the cytosol of Alzheimer brain tissue, (b) human brain cytosolic choline acetyltransferase activity is inhibited by phospho-L-serine in a competitive manner [13].
• Phosphoproteins containing O-phosphoserine and O-phosphothreonine have been isolated from bone matrix and characterized [14].

Associations of phosphoserine with other chemical compounds

• 0. Their serine residues show enhanced susceptibility to beta-elimination, and partial acid hydrolysis of the proteins releases O-phosphoserine [15].
• Phosphoserine aminotransferase (PSAT; EC 2.6.1.52), a member of subgroup IV of the aminotransferases, catalyses the conversion of 3-phosphohydroxypyruvate to l-phosphoserine [16].
• O-Phosphotyrosine prevented 125I-GH-receptor complexes from binding to the antibody column, whereas O-phosphoserine and O-phosphothreonine did not [17].
• The L-isomers of serine-O-phosphate and alpha-aminoadipate were selective inhibitors of IBO-stimulated phosphoinositide hydrolysis, but were less potent than L-AP4 or D,L-AP3 [18].
• Uncalcified samples of turkey tendon obtained prior to calcification, and other samples from areas of tendon that never calcify, contain little or no O-phosphoserine [Ser(P)], O-phosphothreonine [Thr(P)] and gamma-carboxyglutamic acid (Gla) [19].

Gene context of phosphoserine

• 1. Phosphoserine phosphatase (PSP), specific for D- and L-phosphoserine, has been identified in all human tissues [20].
• Induction of rat L-phosphoserine phosphatase by amyloid-beta (1-42) is inhibited by interleukin-11 [21].
• The O-phosphoserine contents of keratin subunits purified from the viable and stratum corneum layers were the same [11].
• In whole bone, a twofold increase in the content of the characteristic amino acid O-phosphoserine for osteopontin occurred in op and tl mutant long bone, but a smaller (15%) and more variable increase was observed in ia mutant rat long bone [22].
• Identification and quantitation of O-phosphoserine in human plasma fibronectin [23].

Analytical, diagnostic and therapeutic context of phosphoserine

• The resulting decrease in mineralization of whole bone and of fractions separated by density centrifugation was accompanied by a very significant decrease in the contents of O-phosphoserine and O-phosphothreonine [24].
• High-performance liquid chromatography of amino acids, peptides and proteins. CXXXI. O-phosphoserine as a new chelating ligand for use with hard Lewis metal ions in the immobilized-metal affinity chromatography of proteins [25].
• Conditions for the immobilization of O-phosphoserine (OPS) to epoxy-activated Sepharose CL-4B are described [25].
• L-Phosphoserine aminotransferase was purified from bovine liver to apparent homogeneity as judged by nondenaturing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, analytical ultracentrifugation, and immunochemical analysis [26].
• Feeding the rat a low protein diet, however, induced the activity of D-3-phosphoglycerate dehydrogenase 12-fold, that of L-phosphoserine aminotransferase 20-fold, and that of L-phosphoserine phosphatase 2-fold [27].

References