RSS-Feed abonnieren
Bitte kopieren Sie die angezeigte URL und fügen sie dann in Ihren RSS-Reader ein.
https://www.thieme-connect.de/rss/thieme/de/10.1055-s-00035024.xml
Thromb Haemost 1996; 76(05): 640-650
DOI: 10.1055/s-0038-1650637
DOI: 10.1055/s-0038-1650637
Original Article
Non-Receptor Protein Tyrosine Kinases and Phosphatases in Human Platelets
Weitere Informationen
Publikationsverlauf
Received: 09. Januar 1996
Accepted after revision22. Juli 1996
Publikationsdatum:
11. Juli 2018 (online)
-
References
- 1 Parsons JT, Parsons SJ. Protein-tyrosine kinases, oncogenes, and cancer. Important Adv Oncol 1993; 3-17
- 2 Fantl WJ, Johnson DE, Williams LT. Signalling by receptor tyrosine kinases. Annu Rev Biochem 1993; 62: 453-481
- 3 Ullrich A, Schlessinger J. Signal transduction by receptors with tyrosine kinase activity. Cell 1990; 61: 203-212
- 4 Cantley LC, Auger KR, Carpenter C, Duckworth B, Graziani A, Kapeller R, Soltoff S. Oncogenes and signal transduction. Cell 1991; 64: 281-302
- 5 Brickell PM. The pp60csrc family of protein-tyrosine kinases: Structure, regulation and function. Crit Rev Oncogen 1992; 3: 401-446
- 6 Rudd CE, Janssen O, Prasad KVS, Raab M, da Silva A, Telfer JC, Yamamoto M. src-related protein tyrosine kinases and their surface receptors. Biochim Biophys Acta 1993; 1155: 239-266
- 7 Vassbotn FS, Havnen OK, Heldin GH, Holmsen H. Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor alpha-receptor. J Biol Chem 1994; 269: 13874-13879
- 8 Fischer EH, Charbonneau H, Tonks NK. Protein tyrosine phosphatases: A diverse family of intracellular and transmembrane enzymes. Science 1991; 253: 401-406
- 9 Feng G, Pawson T. Phosphotyrosine phosphatases with SH2 domains: regulators of signal transduction. Trends Genet 1994; 10: 54-58
- 10 Sun H, Tonks NK. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. TIBS 1994; 19: 480-485
- 11 Golden A, Nemeth SP, Brugge JS. Blood platelets express high levels of the pp60c src-specific tyrosine kinase activity. Proc Natl Acad Sci 1986; 83: 852-856
- 12 Golden A, Brugge JS. Thrombin treatment induces rapid changes in tyrosine phosphorylation in platelets. Proc Natl Acad Sci USA 1989; 86: 901-905
- 13 Ferrell JE, Martin GS. Tyrosine-specific protein phosphorylation is regulated by glycoprotein IIb-IIIa in platelets. Proc Natl Acad Sci USA 1989; 86: 2234-2238
- 14 Bachelot C, Cano E, Grelac F, Saleun S, Druker BJ, Levy-Toledano S, Fischer S, Rendu F. Functional implications of tyrosine protein phosphorylation in platelets. Biochem J 1992; 284: 923-928
- 15 Nakamura S, Yamamura H. Thrombin and collagen induce rapid phosphorylation of a common set of cellular proteins on tyrosine in human platelets. J Biol Chem 1989; 264: 7089-7091
- 16 Jackson SP, Schoenwaelder SM, Yuan Y, Rabinowitz I, Salem HH, Mitchell CA. Adhesion receptor activation of phosphatidylinositol 3-kinase. J Biol Chem 1994; 269: 27093-27099
- 17 Razdan K, Heliums JD, Kroll MH. Shear-stress-induced von Willebrand factor binding to platelets causes the activation of tyrosine kinase(s). Biochem J 1994; 302: 681-686
- 18 Grondin P, Plantavid M, Sultan C, Breton M, Mauco G, Chap H. Interaction of pp60csrc, phospholipase C, inositol-lipid, and diacylglycerol kinases with the cytoskeletons of thrombin-stimulated platelets. J Biol Chem 1991; 266: 15705-15709
- 19 Guinebault C, Payrastre B, Racaud-Sultan C, Mazarguil H, Breton M, Mauco G, Plantavid M, Chap H. Integrin-dependent translocation of phosphoinositide 3-kinase to the cytoskeleton of thrombin-activated platelets involves specific interactions of p85a with actin filaments and focal adhesion kinase. J Cell Biol 1995; 129: 831-842
- 20 Tohyama Y, Yanagi S, Sada K, Yamamura H. Translocation of p72sA to the cytoskeleton in thrombin-stimulated platelets. J Biol Chem 1994; 269: 32796-32799
- 21 Ezumi Y, Takayama H, Okuma M. Differential regulation of protein tyrosine phosphatases by integrin aIIb(33 through cytoskeletal reorganisation and tyrosine phosphorylation in human platelets. J Biol Chem 1995; 270: 11927-11934
- 22 Law DA, Nannizzi-Alaimo L, Phillips DR. Outside-in integrin signal transduction. J Biol Chem 1996; 271: 10811-10815
- 23 Vostal JG, Shulman NR. Vinculin is a major platelet protein that undergoes calcium-dependent tyrosine phosphorylation. Biochem J 1993; 294: 675-680
- 24 Daniel JL, Dangelmaier C, Smith JB. Evidence for a role for tyrosine phosphorylation of phospolipase Cy2 in collagen-induced platelet cytosolic calcium mobilisation. Biochem J 1994; 302: 617-622
- 25 Lipfert L, Haimovich B, Schaller MD, Cobb BS, Parsons JT, Brugge JS. Integrin-dependent phosphorylation and activation of the protein tyrosine kinase ppl25FAK in platelets. J Cell Biol 1992; 119: 905-912
- 26 Rendu F, Eldor A, Grelac F, Bachelot C, Gazit A, Gilon C, Levy-Toledano S, Levitzki A. Inhibition of platelet activation by tyrosine kinase inhibitors. Biochem Pharmacol 1992; 44: 881-888
- 27 Salari H, Duronio V, Howard SL, Demos M, Jones K, Reany A, Hudson AT, Pelech SL. Erbstatin blocks platelet activating factor-induced protein-tyrosine phosphorylation, phosphoinositide hydrolysis, protein kinase C activation, serotonin secretion and aggregation of rabbit platelets. FEBS Letts 1990; 263: 104-108
- 28 Gaudette DC, Holub BJ. Effect of genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets. Biochem Biophys Res Commun 1990; 170: 238-242
- 29 Nakashima S, Koike T, Nozawa Y. Genistein, a protein tyrosine kinase inhibitor, inhibits thromboxane A2-mediated human platelet responses. Mol Pharmacol 1990; 39: 475-480
- 30 Asahi M, Yanagi S, Ohta S, Inazu T, Sakai K, Takeuchi F, Taniguchi T, Yamamura H. Thrombin-induced human platelet aggregation is inhibited by protein-tyrosine kinase inhibitors, ST638 and genistein. FEBS Letts 1992; 309: 10-14
- 31 Inazu T, Taniguchi T, Yanagi S, Yamamura H. Protein-tyrosine phosphorylation and aggregation of intact human platelets by vanadate with H202. Biochem Biophys Res Comm 1990; 170: 259-263
- 32 Lerea KM, Tonks NK, Krebs EG, Fischer EH, Glomset JA. Vanadate and molybdate increase tyrosine phosphorylation in a 50-kilodalton protein and stimulate secretion in electropermeabilised platelets. Biochem 1989; 28: 9286-9292
- 33 Shattil SJ, Ginsberg MH, Brugge JS. Adhesive signalling in platelets. Curr Opin Cell Biol 1994; 6: 695-704
- 34 Clark EA, Shattil SJ, Brugge JS. Regulation of protein tyrosine kinases in platelets. Trends Biochem Sci 1994; 19: 464-469
- 35 Clark EA, Brugge JS. Tyrosine phosphorylation in platelets. Potential roles in intracellular signal transduction. Trends Cardiovasc Med 1993; 3: 218-227
- 36 Soriano P, Montgomery C, Geske R, Bradley A. Targeted disruption of c-src proto-oncogene leads to osteopetrosis mice. Cell 1991; 64: 693-702
- 37 Appleby MW, Gross JA, Cooke MP, Levin SD, Qian X, Perlmutter RM. Defective T cell receptor signalling in mice lacking the thymic isoform of p59fyn. Cell 1992; 70: 751-763
- 38 Stein PL, Lee HM, Rich S, Soriano P. pp59fn mutant mice display differential signalling in thymocytes and peripheral T cells. Cell 1992; 70: 741-750
- 39 Hibbs ML, Tarlinton DM, Armes J, Grail D, Hodgson G, Maglitto R, Stacker SA, Dunn AR. Multiple defects in the immune system of lyn-defi-cient mice, culminating in autoimmune disease. Cell 1995; 83: 301-311
- 40 Superti-Furga G, Courtneidge SA. Structure-function relationships in src family and related protein tyrosine kinases. Bioessays 1995; 17: 321-330
- 41 Pawson T, Schlessinger J. SH2 and SH3 domains. Curr Biol 1993; 3: 434-442
- 42 Kaplan KB, Bibbins KB, Swedlow JR, Arnaud M, Morgan DO, Varmus HE. Association of the amino-terminal half of c-src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J 1994; 13: 4745-4756
- 43 Weng Z, Thomas SM, Rickies RJ, Taylor JA, Brauer AW, Seidel-Dugan C, Michael WM, Dreyfuss G, Brugge JS. Identification of src, fyn, and lyn SH3-binding proteins: implications for a function of SH3 domains. Mol Cell Biol 1994; 14: 4509-4521
- 44 Cross FR, Garber EA, Pellman D, Hanafusa H. A short sequence in the pp60src N-terminus is required for pp60csrc myristoylation and membrane association and for cell transformation. Mol Cell Biol 1985; 4: 1834-1842
- 45 Bagrodia S, Chackalaparampil I, Kmiecik TE, Shalloway D. Altered tyrosine 527 phosphorylation and mitotic activation of pp60csrc. Nature 1991; 349: 172-175
- 46 Cooper JA, Howell B. The when and how of Src regulation. Cell 1993; 73: 1051-1054
- 47 Clark EA, Brugge JS. Redistribution of activated pp60c_src to integrin-dependent cytoskeletal complexes in thrombin-stimulated platelets. Mol Cell Biol 1993; 13: 1863-1871
- 48 Hamaguchi M, Hanafusa H. Association of p60src with Triton X-100-resistant cellular structure correlates with morphological transformation. Proc Natl Acad Sci USA 1987; 84: 2312-2316
- 49 Burridge K, Turner C, Romer LH. Tyrosine phosphorylation of paxillin and ppl25FAK accompanies cell adhesion to the extracellular matrix: a role in cytoskeletal assembly. J Cell Biol 1992; 119: 893-903
- 50 Findik D, Reuter C, Presek P. Platelet membrane glycoproteins lib and Ilia are substrates of purified pp60c src protein tyrosine kinase. FEBS Letts 1990; 262: 1-4
- 51 oda A, Druker BJ, Smith M, Salzman EW. Association of pp60src with Triton X-100-insoluble residue in human blood platelets requires platelet aggregation and actin polymerisation. J Biol Chem 1992; 267: 20075-20081
- 52 Horvath AR, Muszbek L, Kellie S. Translocation of pp60csrc to the cyto-skeleton during platelet aggregation. EMBO J 1992; 11: 855-861
- 53 Kaplan KB, Swedlow JR, Morgan DO, Varmus HE. c-Src enhances the spreading of src -/- fibroblasts on fibronectin by a kinase-independent mechanism. Genes and Development 1995; 9: 1505-1517
- 54 Schaller MD, Borgman CA, Cobb BS, Vines RR, Reynolds AB, Parsons JT. ppl25FAK, a structurally distinctive protein tyrosine kinase associated with focal adhesions. Proc Natl Acad Sci USA 1992; 89: 5192-5196
- 55 Komberg L, Earp HS, Parsons JT, Schaller MD, Juliano RL. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 1992; 267: 23439-23442
- 56 Guan J, Shalloway D. Regulation of focal adhesion associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 1992; 358: 690-692
- 57 Hildebrand JD, Schaller MD, Parsons JT. Identification of sequences re-quired for the efficient localisation of the focal adhesion kinase, ppl25FAK, to cellular focal adhesions. J Cell Biol 1993; 123: 993-1005
- 58 Schaller MD, Parsons JT. Focal adhesion kinase and associated proteins. Curr Opin Cell Biol 1994; 6: 705-710
- 59 Schaller MD, Otey CA, Hildebrand Jd, Parsons JT. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J Cell Biol 1995; 130: 1181-1187
- 60 Hildebrand JD, Schaller MD, Parsons JT. Paxillin, a tyrosine phosphory-lated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol Biol Cell 1995; 6: 637-647
- 61 Chen H, Appeddu PA, Parsons JT, Hildebrand JD, Schaller MD, Guan J. Interaction of focal adhesion kinase with cytoskeletal protein talin. J Biol Chem 1995; 270: 16995-16999
- 62 Miyamoto S, Teramoto H, Coso OA, Gutkind JS, Burbelo PD, Akiyama SK, Yamada KM. Integrin function: Molecular hierarchies of cytoskeletal and signalling molecules. J Cell Biol 1995; 131: 791-805
- 63 Calalb MB, Polte TR, Hanks SK. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for src family kinases. Mol Cell Biol 1995; 15: 954-963
- 64 Cobb BS, Schaller MD, Leu T, Parsons JT. Stable association of pp60src and pp59fyn with the focal adhesion-associated protein tyrosine kinase, ppl25FAK. Mol Cell Biol 1994; 14: 147-155
- 65 Schaller MD, Hildebrand JD, Shannon JD, Fox JW, Vines RR, Parsons JT. Autophosphorylation of the Focal Adhesion Kinase, ppl25FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 1994; 14: 1680-1688
- 66 Eide BL, Turck CW, Escobedo JA. Identification of Tyr-397 as the primary site of tyrosine phosphorylation and pp60src association in the focal adhesion kinase, ppl25FAK. Mol Cell Biol 1995; 15: 2819-2827
- 67 Schlaepfer DD, Hanks SK, Hunter T, van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994; 372: 786-791
- 68 Schaller MD, Parsons JT. ppl25FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol 1995; 15: 2635-2645
- 69 Chen H, Guan J. Association of focal adhesion kinase with its potential substrate phosphatidylinositol 3-kinase. Proc Natl Acad Sci USA 1994; 91: 10148-10152
- 70 Bachelot C, Rameh L, Parsons JT, Cantley LC. Association of phosphatidylinositol 3-kinase, via the SH2 domains of p85, with focal adhesion kinase in polyoma middle T-transformed fibroblasts. Biochim Biophys Acta 1996; 1311: 45-52
- 71 Parson JT. Integrin-mediated signalling: regulation by protein tyrosine kinases and small GTP-binding proteins. Curr Opin Cell Biol 1996; 8: 146-152
- 72 Cooray P, Yuan Y, Schoenwaelder SM, Salem HH, Jackson SP. Focal adhesion kinase (ppl25FAK) cleavage and regulation by calpain. Biochem J 1996; 318: 41-47
- 73 Shattil SJ, Haimovich B, Cunningham M, Lipfert L, Parsons JT, Ginsberg MH, Brugge JS. Tyrosine phosphorylation of ppl25FAK in platelets requires coordinated signalling through integrin and agonist receptors. J Biol Chem 1994; 269: 14738-14745
- 74 Haimovich B, Kaneshiki N, Ji P. Protein kinase C regulates tyrosine phosphorylation of ppl25FAK in platelets adherent to fibrinogen. Blood 1996; 87: 152-161
- 75 Avraham H, London R, Fu Y, Ota S, Hiregowdara D, Li J, Jiang S, Pasztor LM, White RA, Groopman JE, Avraham S. Identification and characterisation of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain. Blood 1995; 86 (Suppl. 01) Suppl 282a
- 76 Avraham S, London R, Fu Y, Ota S, Hiregowdara D, Li J, Jiang S, Pasztor LM, White RA, Groopman JE, Avraham H. Identification and characterisation of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain. J Biol Chem 1995; 270: 27742-27751
- 77 Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K, Sasaki T. Cloning and characterisation of cell adhesion kinase , a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J Biol Chem 1995; 270: 21206-21219
- 78 Lev S, Moreno H, Martinez R, Canoll P, Peles E, Musacchio JM, Plowman GD, Rudy B, Schlessinger J. Protein tyrosine kinase PYK2 involved in calcium-induced regulation of ion channel and MAP kinase functions. Nature 1995; 376: 737-745
- 79 Law CL, Sidorenko SP, Chandran KA, Draves KE, Chan AC, Weiss A, Edelhoff S, Disteche CM, Clark EA. Molecular cloning of human Syk. A B-cell protein tyrosine kinase associated with the surface immunoglobulin M-B cell receptor complex. J Biol Chem 1994; 269: 12310-12319
- 80 Arpaia E, Shahar M, Dadi H, Cohen A, Roifman CM. Defective T cell receptor signalling and CD8+ thymic selection in human lacking ZAP-70 kinase. Cell 1994; 76: 947-958
- 81 Negishi I, Mooyama N, Nakayama K, Senju S, Hatakeyama S, Zhang Q, Chan AC, Loh DY. Essential role for ZAP-70 in both positive and negative selection of thymocytes. Nature 1995; 376: 435-438
- 82 Law C, Sidorenko SP, Chandran KA, Draves KE, Chan AC, Weiss A, Edelhoff S, Disteche CM, Clark EA. Molecular cloning of human pp72Syk. J Biol Chem 1994; 269: 12310-12319
- 83 Kolanus W, Romeo C, Seed B. T cell activation by clustered tyrosine kinases. Cell 1993; 74: 171-183
- 84 Coutre C, Gottfried B, Altman A, Mustelin T. p56lck-independent activation and tyrosine phosphorylation of p72syk by T-cell antigen receptor/CD3 stimulation. Proc Natl Acad Sci USA 1994; 91: 5301-5305
- 85 Turner M, Mee PJ, Costello PS, Williams O, Price AA, Duddy LP, Furlong MT, Geahlen RL, Tybulewicz VLJ. Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk. Nature 1995; 378: 298-302
- 86 Cheng AM, Rowley B, Pao W, Hayday A, Bolen JB, Pawson T. Syk tyrosine kinase required for mouse viability and B-cell development. Nature 1995; 378: 303-306
- 87 Shiue L, Zoller MJ, Brugge JS. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. J Biol Chem 1995; 270: 10498-10502
- 88 Chan AC, Desai DM, Weiss A. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev Immunol 1994; 12: 555-592
- 89 Taniguchi T, Kitagawa H, Yasue S, Yanagi S, Sakai K, Asahi M, Ohta S, Takeuchi F, Nakamura S, Yamamura H. Protein tyrosine kinase p72syk is activated by thrombin and is negatively regulated through Ca2+ mobilisation in platelets. J Biol Chem 1993; 268: 2277-2279
- 90 Huang MM, Indik Z, Brass LF, Hoxie JA, Schreiber AD, Brugge JS. Activation of FcgRII induces tyrosine phosphorylation of multiple proteins including FcgRII. J Biol Chem 1992; 267: 5467-5473
- 91 Chacko GW, Duchemin A, Coggeshall KM, Osborne JM, Brandt JT, Anderson CL. Clustering of the platelet Fcg receptor induces noncovalent association with the tyrosine kinase p72s. A J Biol Chem 1994; 269: 32435-32440
- 92 Chacko GW, Brandt JT, Coggeshall KM, Anderson CL. Phosphoinositide 3-kinase and p72sA noncovalently associate with the low affinity Fcg receptor on human platelets through an immunoreceptor tyrosine-based activation motif. J Biol Chem 1996; 271: 10775-10781
- 93 Yanaga F, Poole A, Asselin J, Blake R, Schieven GL, Clark EA, Watson SP. Syk interacts with tyrosine-phosphorylated proteins in human platelets activated by collagen and cross-linking of the Fcglla receptor. Biochem J 1995; 311: 471-478
- 94 Yanagi S, Sada K, Tohyama Y, Tsubokawa M, Nagai K, Yonezawa K, Yamamura H. Translocation, activation and association of protein-tyrosine kinase (p72sA) with phosphatidylinositol 3-kinase are early events during platelet activation. Eur J Biochem 1994; 224: 329-333
- 95 Clark EA, Shattil SJ, Ginsberg MH, Bolen J, Brugge JS. Regulation of the protein tyrosine kinase pp72sA by platelet agonists and the integrin aIIbβ3 . J Biol Chem 1994; 269: 28859-28864
- 96 Clark EA, Trikha M, Markland FS, Brugge JS. Structurally distinct disin-tegrins contortrostatin and multisquamatin differentially regulate platelet tyrosine phosphorylation. J Biol Chem 1994; 269: 21940-21943
- 97 Wilks AF, Harpur AG. Cytokine signal transduction and the JAK family of protein tyrosine kinases. Bioessays 1994; 16: 313-320
- 98 Wilks AF, Harpur AG, Kurban RR, Ralph SJ, Zurcher G, Ziemiecki A. Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. Mol Cell Biol 1991; 11: 2057-2065
- 99 Rodriguez-Linares B, Watson SP. Phosphorylation of JAK2 in thrombin-stimulated human platelets. FEBS Letts 1994; 352: 335-338
- 100 Ferrel JE, Martin GS. Platelet tyrosine-specific protein phosphorylation is regulated by thrombin. Mol Cell Biol 1988; 8: 3603-3610
- 101 Pumiglia KM, Feinstein MB. Thrombin and thrombin receptor agonist peptide induce tyrosine phosphorylation and tyrosine kinases in the platelet cytoskeleton. Biochem J 1993; 294: 253-260
- 102 Golden A, Brugge JS, Shattil SJ. Role of platelet membrane glycoprotein Ilb-IIIa in agonist-induced tyrosine phosphorylation of platelet proteins. J Cell Biol 1990; 111: 3117-3127
- 103 Fox JEB, Lipfert L, Clark EA, Reynolds CC, Austin CD, Brugge JS. On the role of the platelet membrane skeleton in mediating signal transduction. J Biol Chem 1993; 268: 25973-25984
- 104 Wu H, Parsons JT. Cortactin, an 80/85-kilodalton pp60src substrate, is a filamentous actin-binding protein enriched in the cell cortex. J Cell Biol 1993; 120: 1417-1426
- 105 Li RY, Gaits F, Ragab A, Ragab-Thomas JMF, Chap H. Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertusis toxin-sensitive heterodimeric G-protein. EMBO J 1995; 14: 2519-2526
- 106 Huang M, Lipfert L, Cunningham M, Brugge JS, Ginsberg MH, Shattil SJ. Adhesive ligand binding to integrin aIIbβ3 stimulates tyrosine phosphorylation of novel protein substrates before phosphorylation of ppl25FAK. J Cell Biol 1993; 122: 473-483
- 107 Fox JEB. The platelet cytoskeleton. Thromb Haemost 1993; 70: 884-893
- 108 Plopper GE, McNamee HP, Dike LE, Bojanowski K, Ingber DE. Convergence on integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol Biol Cell 1995; 6: 1349-1365
- 109 Haimovich B, Lipfert L, Brugge JS, Shattil SJ. Tyrosine phosphorylation and cytoskeletal reorganisation in platelets are triggered by interaction of integrin receptors with their immobilised ligands. J Biol Chem 1993; 268: 15868-15877
- 110 Miyamoto S, Akiyama SK, Yamada KM. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 1995; 267: 883-885
- 111 Li RY, Gaits F, Ragab A, Ragad-Thomas JMF, Chap H. Translocation of an SH2-containing protein tyrosine phosphatase (SH-PTP1) to the cytoskeleton of thrombin-activated platelets. FEBS Letts 1994; 343: 89-93
- 112 Frangioni JV, Oda A, Smith M, Salzman EW, Neel BG. Calpain-catalysed cleavage and subcellular relocation of protein phosphotyrosine phosphatase IB (PTP-1B) in human platelets. EMBO J 1993; 12: 4843-4856
- 113 Charbonneau H, Tonks NK, Walsh KA, Fischer EH. The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase. Proc Natl Acad Sci USA 1988; 85: 7182-7186
- 114 Frangioni JV, Beahm PH, Shifrin V, Jost CA, Neel BG. The non-transmembrane tyrosine phosphatase PTP-1B localises to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell 1992; 68: 545-560
- 115 Flint AJ, Gebbink FGB, Franza BR, Hill DE, Tonks NK. Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation. EMBO J 1993; 12: 1937-1946
- 116 Schievella AR, Paige LA, Johnson KA, Hill DE, Erikson RL. Protein tyrosine phosphatase IB undergoes mitosis-specific phosphorylation on serine. Cell Growth Differ 1993; 4: 239-246
- 117 Shen S, Bastien L, Posner BI, Chretien P. A protein tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases. Nature 1991; 352: 736-739
- 118 Plutzky J, Neel BG, Rosenberg RD. Isolation of a src homology 2-contain-ing tyrosine phosphatase. Proc Natl Acad Sci USA 1992; 89: 1123-1127
- 119 Yi T, Cleveland JL, Ihle JN. Protein tyrosine phosphatase containing SH2 domains: characterisation, preferential expression in haematopoietic cells, and localisation to human chromosome 12 pl2-pl3. Mol Cell Biol 1992; 12: 836-846
- 120 Matthews RJ, Bowne DB, Flores E, Thomas ML. Characterisation of haematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol Cell Biol 1992; 12: 2396-2405
- 121 Adachi M, Fischer EH, Ihle J, Imai K, Jirik F, Neel B, Pawson T, Thomas T, Ullrich A, Zhao Z. Mammalian SH2-containing protein tyrosine phosphatases. Cell 1996; 85: 15
- 122 Tsui HW, Siminovitch KA, Souza L, Tsui FWL. Motheaten and viable motheaten mice have viable mutations in the haematopoietic cell phosphatase gene. Nature Genetics 1993; 4: 124-129
- 123 Schultz LD, Schweitzer PA, Rajan TV, Yi T, Ihle JN, Matthews RJ, Thomas ML, Beier DR. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene. Cell 1993; 73: 1445-1454
- 124 Kozlowski M, Mlinaric-Rascan I, Feng GS, Shen R, Pawson T, Siminovitch KA. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J Exp Med 1993; 178: 2157-2163
- 125 Yi T, Mui AL, Krystal G, Ihle JN. Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor beta chain and down-regulates IL-3-induced tyrosine phosphorylation and mitogenesis. Mol Cell Biol 1993; 13: 7577-7586
- 126 Falet H, Ramos-Morales F, Bachelot C, Fischer S, Rendu F. Association of the protein tyrosine phosphatase PTP1C with the protein tyrosine kinase c-src in human platelets. FEBS Letts 1996; 383: 165-169
- 127 Zhao Z, Shen SH, Fischer EH. Stimulation by phospholipids of a protein-tyrosine-phosphatase containing two src homology 2 domains. Proc Natl Acad Sci USA 1993; 90: 4251-4255
- 128 Freeman RM, Plutzky J, Neel BG. Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew. Proc Natl Acad Sci USA 1992; 89: 11239-11243
- 129 Feng GS, Hui CC, Pawson T. SH2-containing phosphotyrosine phosphatase as target of protein-tyrosine kinases. Science 1993; 259: 1607-1611
- 130 Vogel W, Lammers R, Huang J, Ullrich A. Activation of phosphotyrosine phosphatase by tyrosine phosphorylation. Science 1993; 259: 1611-1614
- 131 Adachi M, Sekiya M, Miyachi T, Matsuno K, Hinoda Y, Imai K, Yachi A. Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3 with sequence similarity to the src-homology region 2. FEBS Letts 1992; 314: 335-339
- 132 Ahmad S, Banville D, Zhao Z, Fischer EH, Shen SH. A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains. Proc Natl Acad Sci USA 1993; 90: 2197-2201
- 133 Lechleider RJ, Freeman Jr RM, Neel BG. Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2. J Biol Chem 1993; 268: 13434-13438
- 134 Lechleider RJ, Sugimoto S, Bennett AM, Kashishian AS, Cooper JA, Shoelson SE, Walsh CT, Neel BG. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyro-sine-1009, on the human platelet-derived growth factor receptor. J Biol Chem 1993; 268: 21478-21481
- 135 Dechert U, Adam M, Harder KW, Clark-Lewis I, Jirik F. Characterisation of protein tyrosine phosphatase SH-PTP2. Study of phosphopeptide substrates and possible regulatory role of SH2 domains. J Biol Chem 1994; 269: 5602-5611
- 136 Li W, Nishimura R, Kashishian A, Batzer AG, Kim WJH, Cooper JA, Schlessinger J. A new function for a phosphotyrosine phosphatase-linking GRB2-SOS to a receptor tyrosine kinase. Mol Cell Biol 1994; 14: 509-517
- 137 Oda A, Druker BJ, Ariyoshi H, Smith M, Salzman EW. pp60src is an endogenous substrate for calpain in human blood platelets. J Biol Chem 1993; 268: 12603-12608
- 138 Saido TC, Sorimachi H, Suzuki K. Calpain: new perspectives in molecular diversity and physiological-pathological involvement. FASEB J 1994; 8: 814-822
- 139 Fox JEB, Taylor RG, Taffarel M, Boyles JK, Goll DE. Evidence that activation of platelet calpain is induced as a consequence of binding of adhesive ligand to the integrin, glycoprotein Ilb-IIIa. J Cell Biol 1993; 120: 1501-1507
- 140 Fox JEB, Santos G, Zuerbig S, Saido TC. Role of the cytoskeleton in regulating integrin-induced transmembrane signalling. Thromb Haemost 1995; 73: 987 (Abstr)
- 141 Fox JEB, Austin CD, Reynolds CC, Steffen PK. Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets. J Biol Chem 1991; 266: 13289-13295
- 142 Fox JEB, Austin CD, Boyles JK, Steffen PK. Role of membrane skeleton in preventing the shedding of procoagulant-rich microvesicles from the platelet plasma membrane. J Cell Biol 1990; 111: 483-493
- 143 Fox JEB, Reynolds CC, Austin CD. The role of calpain in stimulus-re-sponse coupling: evidence that calpain mediates agonist-induced expression of procoagulant activity in platelets. Blood 1990; 76: 2510-2519
- 144 Gemmell CH, Sefton MV, Yeo EL. Platelet-derived microparticle formation involves glycoprotein Ilb-IIIa. J Biol Chem 1993; 268: 14586-14589
- 145 Basse F, Gaffet P, Bienvenue A. Correlation between inhibition of cytoskeleton proteins and anti-vesiculation effect of calpeptin during A23187-induced activation of human platelets: are vesicles shed by filopod fragmentation. Biochim Biophys Acta 1994; 1190: 217-224
- 146 Yano Y, Shiba E, Kambayashi J, Sakon M, Kawasaki T, Fujitani K, Kang J, Mori T. The effect of calpeptin (a calpain specific inhibitor) on agonist induced microparticle formation from the platelet plasma membrane. Thromb Res 1993; 71: 385-396
- 147 Zwaal RF, Comfurius P, Bevers EM. Platelet procoagulant activity and microvesicle formation. Its putative role in hemostasis and thrombosis. Biochim Biophys Acta 1992; 1180: 1-8
- 148 Beckerle MC, Burridge K, DeMartino GN, Croall DE. Colocalisation of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 1987; 51: 569-577
- 149 Ariyoshi H, Oda A, Salzman EW. Participation of calpain in protein-tyrosine phosphorylation and dephosphorylation in human blood platelets. Arterioscl Thromb Vase Biol 1995; 15: 511-514
- 150 Douglas CG, Holub B. Effect of Genistein, a tyrosine kinase inhibitor, on U46619-induced phosphoinositide phosphorylation in human platelets. Biochem Biophys Res Comm 1990; 238-242
- 151 Schoenwaelder SM, Jackson SP, Yuan Y, Teasdale MS, Salem HH, Mitchell CA. Tyrosine kinases regulate the cytoskeletal attachment of integrin aIIbβ3 (platelet glycoprotein Ilb/IIIa) and the cellular retraction of fibrin polymers. J Biol Chem 1994; 269: 32479-32487