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Volumn 1419, Issue 2, 1999, Pages 195-206

Amphiphilic and hydrophilic nature of sheep and human platelet phosphotyrosine phosphatase forms

Author keywords

Amphiphilic form; Hydrophilic form; Platelet; Protein tyrosine phosphatase

Indexed keywords

AMPHOPHILE; ISOENZYME; PROTEIN TYROSINE PHOSPHATASE;

EID: 0344849470     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(99)00066-8     Document Type: Article
Times cited : (11)

References (38)
  • 1
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signaling by protein tyrosine phosphatases
    • N.K. Tonks, B.G. Weel, From form to function: signaling by protein tyrosine phosphatases, Cell 87 (1996) 365-368.
    • (1996) Cell , vol.87 , pp. 365-368
    • Tonks, N.K.1    Weel, B.G.2
  • 2
    • 0344297230 scopus 로고
    • Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets
    • A. Golden, J.S. Brugge, Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets, Proc. Natl. Acad. Sci. USA 86 (1986) 901-905.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 901-905
    • Golden, A.1    Brugge, J.S.2
  • 3
    • 3142588838 scopus 로고
    • Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets
    • J.E. Ferrel, J.S. Martin, Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets, Proc. Natl. Acad. Sci. USA 86 (1989) 2234-2238.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2234-2238
    • Ferrel, J.E.1    Martin, J.S.2
  • 5
    • 0025775939 scopus 로고
    • Membrane glycoprotein IV (CD63) is physically associated with the Fyn, and Yes protein-tyrosine kinases in human platelets
    • M.-M. Huang, J.B. Bolen, J.W. Barnwell, S.J. Shatill, J.S. Brugge, Membrane glycoprotein IV (CD63) is physically associated with the Fyn, and Yes protein-tyrosine kinases in human platelets, Proc. Natl. Acad. Sci. USA 8 (1991) 7844-7848.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.8 , pp. 7844-7848
    • Huang, M.-M.1    Bolen, J.B.2    Barnwell, J.W.3    Shatill, S.J.4    Brugge, J.S.5
  • 8
    • 0023766362 scopus 로고
    • Platelet tyrosine-specific protein phosphorylation is regulated by thrombin
    • J.E. Ferrel, G.S. Martin, Platelet tyrosine-specific protein phosphorylation is regulated by thrombin, Proc. Natl. Acad. Sci. USA 8 (1988) 3603-3610.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.8 , pp. 3603-3610
    • Ferrel, J.E.1    Martin, G.S.2
  • 9
    • 0024473908 scopus 로고
    • Protein-tyrosine-phosphatase. The other side of the coin
    • T. Hunter, Protein-tyrosine-phosphatase. The other side of the coin, Cell 58 (1989) 1013-1016.
    • (1989) Cell , vol.58 , pp. 1013-1016
    • Hunter, T.1
  • 10
    • 0024378995 scopus 로고
    • A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila
    • M. Streuli, N.X. Krueger, A.Y.M. Tsai, H. Saito, A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila, Proc. Natl. Acad. Sci. USA 86 (1989) 8698-8702.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8698-8702
    • Streuli, M.1    Krueger, N.X.2    Tsai, A.Y.M.3    Saito, H.4
  • 11
  • 12
    • 0026324171 scopus 로고
    • Protein tyrosine phosphatase: A diverse family of intracellular and transmembrane enzymes
    • E.H. Fischer, U.H. Charboneau, N.K. Tonks, Protein tyrosine phosphatase: a diverse family of intracellular and transmembrane enzymes, Science 253 (1991) 401-406.
    • (1991) Science , vol.253 , pp. 401-406
    • Fischer, E.H.1    Charboneau, U.H.2    Tonks, N.K.3
  • 13
    • 0030953448 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in signal transduction
    • B.G. Neel, N.K. Tonks, Protein tyrosine phosphatases in signal transduction, Curr. Opin. Cell Biol. 9 (1997) 193-204.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 193-204
    • Neel, B.G.1    Tonks, N.K.2
  • 14
    • 0028854163 scopus 로고
    • Regulation of membrane-associated tyrosine phosphatases in UMR 106.06 osteoblast cells
    • M.C. Southey, D.M. Findlay, B.E. Kemp, Regulation of membrane-associated tyrosine phosphatases in UMR 106.06 osteoblast cells, Biochem. J. 305 (1995) 485-490.
    • (1995) Biochem. J. , vol.305 , pp. 485-490
    • Southey, M.C.1    Findlay, D.M.2    Kemp, B.E.3
  • 15
    • 0027494395 scopus 로고
    • Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase IB
    • J.V. Frangioni, A. Oda, M. Smith, E.W. Salzman, B.G. Neel, Calpain-catalyzed cleavage and subcellular relocation of protein phosphotyrosine phosphatase IB, EMBO J. 12 (1993) 4843-4856.
    • (1993) EMBO J. , vol.12 , pp. 4843-4856
    • Frangioni, J.V.1    Oda, A.2    Smith, M.3    Salzman, E.W.4    Neel, B.G.5
  • 16
    • 0029035974 scopus 로고
    • 3 through cytoskeletal reorganization and tyrosine phosphorylation in human platelets
    • 3 through cytoskeletal reorganization and tyrosine phosphorylation in human platelets, J. Biol. Chem. 270 (1995) 11927-11934.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11927-11934
    • Ezumi, Y.1    Takayama, H.2    Okuma, M.3
  • 17
    • 0027291018 scopus 로고
    • Identification of a protein-tyrosine phosphatase from human platelet membranes by an immobilon-based solid phase assay
    • D.D. Dawicki, M. Steiner, Identification of a protein-tyrosine phosphatase from human platelet membranes by an immobilon-based solid phase assay, Anal. Biochem. 213 (1993) 245-255.
    • (1993) Anal. Biochem. , vol.213 , pp. 245-255
    • Dawicki, D.D.1    Steiner, M.2
  • 18
    • 0025992880 scopus 로고
    • Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1
    • M. Gu, J.D. York, I. Warshawsky, P.W. Majerus, Identification, cloning, and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to cytoskeletal protein 4.1, Proc. Natl. Acad. Sci. USA 88 (1991) 5867-5871.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5867-5871
    • Gu, M.1    York, J.D.2    Warshawsky, I.3    Majerus, P.W.4
  • 19
    • 0029958610 scopus 로고    scopus 로고
    • The properties of the protein tyrosine phosphatase PTPMEG
    • P.W. Mejerus, M. Gu, The properties of the protein tyrosine phosphatase PTPMEG, J. Biol. Chem. 271 (1996) 27751-27759.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27751-27759
    • Mejerus, P.W.1    Gu, M.2
  • 20
    • 0025829907 scopus 로고
    • Phosphotyrosine phosphatase activity in human platelets
    • M. Smilowitz, L. Aamli, D. Xu, P.M. Epstein, Phosphotyrosine phosphatase activity in human platelets, Life Sci. 49 (1991) 29-37.
    • (1991) Life Sci. , vol.49 , pp. 29-37
    • Smilowitz, M.1    Aamli, L.2    Xu, D.3    Epstein, P.M.4
  • 22
    • 0024990088 scopus 로고
    • Subcellular distribution and characterization of acetylcholinesterase activities from sheep platelets: Relationship between temperature dependence and environment
    • J. Sánchez-Yagüe, J.A. Cabezas, M. Llanillo, Subcellular distribution and characterization of acetylcholinesterase activities from sheep platelets: relationship between temperature dependence and environment, Blood 76 (1990) 737-744.
    • (1990) Blood , vol.76 , pp. 737-744
    • Sánchez-Yagüe, J.1    Cabezas, J.A.2    Llanillo, M.3
  • 23
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • C. Bordier, Phase separation of integral membrane proteins in Triton X-114 solution, J. Biol. Chem. 256 (1980) 1604-1607.
    • (1980) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 24
    • 0025369665 scopus 로고
    • Amphiphilic and hydrophilic molecular forms of acetylcholinesterase in membranes derived from sarcoplasmic reticulum of skeletal muscle
    • M.D. Cánovas-Muñoz, J. Campoy, E. Muñoz-Delgado, C.J. Vidal, Amphiphilic and hydrophilic molecular forms of acetylcholinesterase in membranes derived from sarcoplasmic reticulum of skeletal muscle, Biochim. Biophys. Acta 1039 (1990) 323-330.
    • (1990) Biochim. Biophys. Acta , vol.1039 , pp. 323-330
    • Cánovas-Muñoz, M.D.1    Campoy, J.2    Muñoz-Delgado, E.3    Vidal, C.J.4
  • 25
    • 73049130725 scopus 로고
    • A method for determining the sedimentation behavior of enzymes. Applications to protein mixtures
    • R.G. Martin, B.N. Ames, A method for determining the sedimentation behavior of enzymes. Applications to protein mixtures, J. Biol. Chem. 236 (1961) 1372-1379.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1372-1379
    • Martin, R.G.1    Ames, B.N.2
  • 26
    • 0014779155 scopus 로고
    • Two-dimensional thin-layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • G. Rousser, S. Flischer, A. Yamamoto, Two-dimensional thin-layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots, Lipids 5 (1970) 494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rousser, G.1    Flischer, S.2    Yamamoto, A.3
  • 27
    • 0017184389 scopus 로고
    • A rapid sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding, Anal. Biochem. 53 (1976) 304-308.
    • (1976) Anal. Biochem. , vol.53 , pp. 304-308
    • Bradford, M.M.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0022644189 scopus 로고
    • Triton X-114. A detergent that has come in from the cold
    • J.G. Pryde, Triton X-114. A detergent that has come in from the cold, Trends Biochem. Sci. 11 (1986) 160-163.
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 160-163
    • Pryde, J.G.1
  • 30
    • 0021735544 scopus 로고
    • Distribution of platelet glycoproteins and phosphoproteins in hydrophobic and hydrophilic phases in Triton X-114 phase partitioning
    • K.J. Clemetson, D. Bienz, M.L. Zahno, E.F. Lüscher, Distribution of platelet glycoproteins and phosphoproteins in hydrophobic and hydrophilic phases in Triton X-114 phase partitioning, Biochim. Biophys. Acta 778 (1984) 463-469.
    • (1984) Biochim. Biophys. Acta , vol.778 , pp. 463-469
    • Clemetson, K.J.1    Bienz, D.2    Zahno, M.L.3    Lüscher, E.F.4
  • 31
    • 0027295333 scopus 로고
    • Engineered deletion of the unique N-terminal domain of the cyclic AMP-specific phosphodiesterase RD1 prevents plasma membrane association and the attainment of enhanced thermostability without altering its sensitivity to inhibition by rolipram
    • Y. Shakur, J.G. Pryde, M.D. Houslay, Engineered deletion of the unique N-terminal domain of the cyclic AMP-specific phosphodiesterase RD1 prevents plasma membrane association and the attainment of enhanced thermostability without altering its sensitivity to inhibition by rolipram, Biochem. J. 292 (1993) 677-695.
    • (1993) Biochem. J. , vol.292 , pp. 677-695
    • Shakur, Y.1    Pryde, J.G.2    Houslay, M.D.3
  • 32
    • 0001869569 scopus 로고
    • A.J. Kenny, A.J. Turner, (Eds.), Elsevier, Amsterdam
    • J.P. Toutant, J. Massoulié, in: A.J. Kenny, A.J. Turner, (Eds.), Mammalian Ectoenzymes, Elsevier, Amsterdam, 1987, pp. 289-328.
    • (1987) Mammalian Ectoenzymes , pp. 289-328
    • Toutant, J.P.1    Massoulié, J.2
  • 33
    • 0027262361 scopus 로고
    • Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains
    • Z. Zhao, S.-H. Shen, E.H. Fischer, Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains, Proc. Natl. Acad. Sci. USA 90 (1993) 4251-4255.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 4251-4255
    • Zhao, Z.1    Shen, S.-H.2    Fischer, E.H.3
  • 34
    • 0028205463 scopus 로고
    • Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets
    • R.Y. Li, F. Gaits, A. Ragab, J.M.F. Ragab-Thomas, H. Chap, Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets, FEBS Lett. 343 (1994) 89-93.
    • (1994) FEBS Lett. , vol.343 , pp. 89-93
    • Li, R.Y.1    Gaits, F.2    Ragab, A.3    Ragab-Thomas, J.M.F.4    Chap, H.5
  • 35
    • 0023949969 scopus 로고
    • Flow cytometric analysis of human bone marrow. IV. Differential quantitative expression of T-200 common leucocyte antigen
    • V.O. Shah, C.J. Civin, M.R. Loken, Flow cytometric analysis of human bone marrow. IV. Differential quantitative expression of T-200 common leucocyte antigen, J. Immunol. 140 (1988) 1861-1867.
    • (1988) J. Immunol. , vol.140 , pp. 1861-1867
    • Shah, V.O.1    Civin, C.J.2    Loken, M.R.3
  • 36
    • 0026576176 scopus 로고
    • Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC 14P
    • W. Gu, I. Warshawsky, P.W. Majerus, Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC 14P, Proc. Natl. Acad. Sci. USA 89 (1992) 2980-2984.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2980-2984
    • Gu, W.1    Warshawsky, I.2    Majerus, P.W.3
  • 37
    • 0027352902 scopus 로고
    • Sphingolipid-like molecule linked to CD45, a protein tyrosine phosphatase
    • A. Takeda, Sphingolipid-like molecule linked to CD45, a protein tyrosine phosphatase, Adv. Lipid Res. 26 (1993) 293-317.
    • (1993) Adv. Lipid Res. , vol.26 , pp. 293-317
    • Takeda, A.1
  • 38
    • 0027979052 scopus 로고
    • Characterization of two structurally related Xenopus laevis protein tyrosine phosphatases with homology to lipid-binding proteins
    • R.L. Del Vecchio, N.K. Tonks, Characterization of two structurally related Xenopus laevis protein tyrosine phosphatases with homology to lipid-binding proteins, J. Biol. Chem. 269 (1994) 19639-19645.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19639-19645
    • Del Vecchio, R.L.1    Tonks, N.K.2


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