Disease relevance of L-Tyrosine O-sulfate

• In a previous paper, we briefly reported on isolation from the supernatant fraction of rat fibroblasts infected by Fujinami sarcoma virus fibronectin that yielded tyrosine-O-sulfate on Pronase hydrolysis [1].
• Decrease of tyrosine-O-sulfate-containing proteins found in rat fibroblasts infected with Rous sarcoma virus or Fujinami sarcoma virus [2].
• In this study, we examined the possibility of selecting such antibodies from large phage antibody libraries using sulfotyrosine as a test case [3].
• Sulfotyrosine is a post-translational modification important in many extracellular protein-protein interactions, including human immunodeficiency virus infection [3].
• Tyramine-O-sulfate, in addition to tyrosine-O-sulfate, is produced and secreted by HepG2 human hepatoma cells, but not by 3Y1 rat embryo fibroblasts [4].

High impact information on L-Tyrosine O-sulfate

• We propose that this sulfotyrosine-containing segment of PSGL-1, in conjunction with sLex presented on O-linked glycans, constitutes the high affinity P-selectin-binding site [5].
• We found that CCR5 2-18 is sulfated by both TPST isoenzymes leading to a final product with four sulfotyrosine residues [6].
• Isolation of tyrosine-O-sulfate by Pronase hydrolysis from fibronectin secreted by Fujinami sarcoma virus-infected rat fibroblasts [1].
• Aspartic acid residues 72 and 75 and tyrosine-sulfate 73 of heparin cofactor II promote intramolecular interactions during glycosaminoglycan binding and thrombin inhibition [7].
• Thin layer chromatography of a base hydrolysate of [35S]O4-labeled C4 alpha-chains, or C4 isolated from human plasma, revealed the presence of tyrosine-O-sulfate [8].

Biological context of L-Tyrosine O-sulfate

• These results suggest that tyramine-O-sulfate may be derived from the de novo sulfation of tyramine, instead of the decarboxylation of tyrosine-O-sulfate [4].

Anatomical context of L-Tyrosine O-sulfate

• A similar tyrosine-O-sulfate-binding protein was also detected in the choleate extracts of the Golgi-enriched microsomal membrane fractions prepared from bovine pancreas and from both liver and pancreas of dog [9].

Associations of L-Tyrosine O-sulfate with other chemical compounds

• NMR and fluorescence polarization measurements showed that the CXCR4 peptide stabilizes dimeric SDF-1alpha, and that sulfotyrosine 21 binds a specific site on the chemokine that includes arginine 47 [10].
• Sodium chlorate, a potent inhibitor of sulfation reactions, completely inhibits the formation of tyrosine-o-sulfate in type III procollagen in human fibroblasts, when used in concentrations that do not affect the incorporation of radioactive amino acids into protein [11].
• Certain sulfotyrosine peptides derived from casein are known to be good inhibitors of the protein tyrosine phosphatase, PTP1B [12].
• A major tyrosine-O-sulfate (TyrS)-binding protein present in bovine serum was purified to electrophoretic homogeneity using a combination of TyrS-Affi-Gel 10 affinity chromatography, DEAE-Bio-Gel A ion-exchange chromatography, and hydroxylapatite chromatography [13].
• Two tyrosine-O-sulfate containing cholecystokinin-related peptides were synthetized, i.e. the undeca- and the dodecapeptide amide corresponding to the C-terminus of this gut hormone; in the undecapeptide the N-terminal serine was O-substituted with the 2-deoxy-alpha-D-galactosyl group [14].

Gene context of L-Tyrosine O-sulfate

• Amino acid analysis of 35S-sulfate labeled VP1 by enzymatic hydrolysis followed by two-dimensional thin-layer electrophoresis revealed the presence of 35S-sulfate-labeled tyrosine-O-sulfate [15].
• Presence of tyrosine-O-sulfate in sheep pituitary prolactin [16].
• The results show that tyrosine-O-sulfate residues in HCII and in cholecystokinin peptide fragments (as model compounds) do not significantly contribute to the absorbance spectrum from 280 to 300 nm [17].
• Change in binding affinities of 3Y1 secreted fibronectin upon desulfation of tyrosine-O-sulfate [18].
• Structure, modelling, and molecular dynamics studies of the inhibition of protein tyrosine phosphatase 1B by sulfotyrosine peptides [12].

Analytical, diagnostic and therapeutic context of L-Tyrosine O-sulfate

• Quantitation of tyrosine-O-sulfate in human urine by ion-pair reverse-phase high-performance liquid chromatography [19].

References