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Start Over Author "Shimomura R" Journal biochemical and biophysical research communications
4 results on '"Shimomura R"'

2. Phosphorylation Sites of Myelin Basic Protein by A Catalytic Fragment of Non-receptor Type Protein-Tyrosine Kinase P72sykand Comparison with Those by Insulin Receptor Kinase

Author

Shimomura, R., Sakai, K., Tanaka, Y., Yonezawa, K., Hashimoto, E., Kasuga, M., and Yamamura, H.

Abstract

Myelin basic protein has been used as a model substrate for determination of substrate recognition motif of various protein kinases. In this report phosphorylated sites of bovine brain myelin basic protein were studied with a catalytic fragment of protein-tyrosine kinase p72syk. Three of four tyrosine residues in myelin basic protein were phosphorylated by this kinase. Major phosphorylated site was 134Y and minor phosphorylated sites were 68Y and 127Y. As the phosphorylation site by p56lckwas only 68Y, the recognition motif of p72sykwas quite different from that of p56lck. Furthermore, the fact that elution pattern on HPLC of the phosphopeptides obtained by insulin receptor kinase was different from that by p72syksuggested that the recognition motif of p72sykwas also different from that of insulin receptor kinase. These results may suggest that each protein-tyrosine kinase has a specific substrate recognition motif.

Published
1993
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3. Phospholipids differently modulate the activity of cytosolic protein-tyrosine kinase from porcine spleen.

Author

Sakai K, Taniguchi T, Shimomura R, Asahi M, Kobayashi T, Inazu T, Nakamura S, and Yamamura H

Subjects
Animals, Cytosol enzymology, Kinetics, Lipid Bilayers, Phosphorylation, Swine, Phospholipids pharmacology, Protein-Tyrosine Kinases metabolism, Spleen enzymology
Abstract

Effect of membrane phospholipids on the activity of cytosolic protein-tyrosine kinase from porcine spleen (CPTK-40) has been studied. Using poly(Glu Na, Tyr)4:1 as a substrate, phosphatidylethanolamine, phosphatidylcholine and phosphatidylserine had stimulatory effects on that phosphorylation activity, however phosphatidic acid had inhibitory and phosphatidylinositol had no effects. Similar results were obtained using[Val5]angiotensin II as a substrate. On the other hand using basic protein (H2B histone and myelin basic protein) as substrates, phosphatidic acid stimulated the activity of CPTK-40, while phosphatidylinositol inhibited the activity. Phosphatidylethanolamine, phosphatidylcholine and phosphatidylserine caused different effect on the activity of CPTK-40 depending on the substrate employed. However using acidic protein (tubulin and casein) as substrates, the activity of CPTK-40 was neither stimulated nor inhibited by any phospholipids. These results suggest that phospholipids may modulate the activity of CPTK-40.

Published
1989
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4. Similarity and pleiotropic actions of adenosine 3',5'-monophosphate-dependent protein kinases from mammalian tissues.

Author

Yamamura H, Inoue Y, Shimomura R, and Nishizuka Y

Subjects
Adenosine Triphosphate, Adrenal Glands enzymology, Animals, Autoradiography, Cattle, Electrophoresis, Paper, Enzyme Activation, Glucosyltransferases, Glycogen, Histones, Kinetics, Lipase, Nucleoside Diphosphate Sugars, Phosphorus Isotopes, Phosphorylases, Proteins, Rabbits, Rats, Ribosomes, Trypsin, Uracil Nucleotides, Brain enzymology, Cyclic AMP, Liver enzymology, Muscles enzymology, Phosphotransferases
Published
1972
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