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Volumn 25, Issue 3, 2014, Pages 273-283

PDGF receptor signaling networks in normal and cancer cells

Author keywords

Myeloproliferative neoplasms; Oncogenes; PDGFRA; PDGFRB; Receptor tyrosine kinase

Indexed keywords

CALCIUM; IMATINIB; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE C; PLATELET DERIVED GROWTH FACTOR B; PLATELET DERIVED GROWTH FACTOR BETA RECEPTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; STAT1 PROTEIN; STAT3 PROTEIN; VASCULOTROPIN A; BENZAMIDE DERIVATIVE; PIPERAZINE DERIVATIVE; PROTEIN KINASE INHIBITOR; PYRIMIDINE DERIVATIVE;

EID: 84902087291     PISSN: 13596101     EISSN: 18790305     Source Type: Journal    
DOI: 10.1016/j.cytogfr.2014.03.003     Document Type: Review
Times cited : (195)

References (160)
  • 1
    • 1842280753 scopus 로고
    • A platelet-dependent serum factor that stimulates the proliferation of arterial smooth muscle cells in vitro
    • Ross R., Glomset J., Kariya B., Harker L. A platelet-dependent serum factor that stimulates the proliferation of arterial smooth muscle cells in vitro. Proc Natl Acad Sci U S A 1974, 71:1207-1210.
    • (1974) Proc Natl Acad Sci U S A , vol.71 , pp. 1207-1210
    • Ross, R.1    Glomset, J.2    Kariya, B.3    Harker, L.4
  • 2
    • 0017280448 scopus 로고
    • A platelet factor stimulating human normal glial cells
    • Westermark B., Wasteson A. A platelet factor stimulating human normal glial cells. Exp Cell Res 1976, 98:170-174.
    • (1976) Exp Cell Res , vol.98 , pp. 170-174
    • Westermark, B.1    Wasteson, A.2
  • 3
    • 0016283728 scopus 로고
    • Platelets as a source of fibroblast growth-promoting activity
    • Kohler N., Lipton A. Platelets as a source of fibroblast growth-promoting activity. Exp Cell Res 1974, 87:297-301.
    • (1974) Exp Cell Res , vol.87 , pp. 297-301
    • Kohler, N.1    Lipton, A.2
  • 4
    • 0020640259 scopus 로고
    • Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus
    • Waterfield M.D., Scrace G.T., Whittle N., Stroobant P., Johnsson A., Wasteson A., et al. Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus. Nature 1983, 304:35-39.
    • (1983) Nature , vol.304 , pp. 35-39
    • Waterfield, M.D.1    Scrace, G.T.2    Whittle, N.3    Stroobant, P.4    Johnsson, A.5    Wasteson, A.6
  • 5
    • 0022541219 scopus 로고
    • Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors
    • Yarden Y., Escobedo J.A., Kuang W.J., Yang-Feng T.L., Daniel T.O., Tremble P.M., et al. Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors. Nature 1986, 323:226-232.
    • (1986) Nature , vol.323 , pp. 226-232
    • Yarden, Y.1    Escobedo, J.A.2    Kuang, W.J.3    Yang-Feng, T.L.4    Daniel, T.O.5    Tremble, P.M.6
  • 6
    • 0020034489 scopus 로고
    • Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factor
    • Ek B., Westermark B., Wasteson A., Heldin C.H. Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factor. Nature 1982, 295:419-420.
    • (1982) Nature , vol.295 , pp. 419-420
    • Ek, B.1    Westermark, B.2    Wasteson, A.3    Heldin, C.H.4
  • 7
    • 34047127376 scopus 로고    scopus 로고
    • PDGF receptors as targets in tumor treatment
    • Ostman A., Heldin C.H. PDGF receptors as targets in tumor treatment. Adv Cancer Res 2007, 97:247-274.
    • (2007) Adv Cancer Res , vol.97 , pp. 247-274
    • Ostman, A.1    Heldin, C.H.2
  • 8
    • 44149090296 scopus 로고    scopus 로고
    • Role of platelet-derived growth factors in physiology and medicine
    • Andrae J., Gallini R., Betsholtz C. Role of platelet-derived growth factors in physiology and medicine. Genes Dev 2008, 22:1276-1312.
    • (2008) Genes Dev , vol.22 , pp. 1276-1312
    • Andrae, J.1    Gallini, R.2    Betsholtz, C.3
  • 9
    • 2942676788 scopus 로고    scopus 로고
    • The PDGF family: four gene products form five dimeric isoforms
    • Fredriksson L., Li H., Eriksson U. The PDGF family: four gene products form five dimeric isoforms. Cytokine Growth Factor Rev 2004, 15:197-204.
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 197-204
    • Fredriksson, L.1    Li, H.2    Eriksson, U.3
  • 10
    • 0042125242 scopus 로고    scopus 로고
    • Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall
    • Lindblom P., Gerhardt H., Liebner S., Abramsson A., Enge M., Hellstrom M., et al. Endothelial PDGF-B retention is required for proper investment of pericytes in the microvessel wall. Genes Dev 2003, 17:1835-1840.
    • (2003) Genes Dev , vol.17 , pp. 1835-1840
    • Lindblom, P.1    Gerhardt, H.2    Liebner, S.3    Abramsson, A.4    Enge, M.5    Hellstrom, M.6
  • 11
    • 0035003785 scopus 로고    scopus 로고
    • PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor
    • Bergsten E., Uutela M., Li X., Pietras K., Östman A., Heldin C.H., et al. PDGF-D is a specific, protease-activated ligand for the PDGF beta-receptor. Nat Cell Biol 2001, 3:512-516.
    • (2001) Nat Cell Biol , vol.3 , pp. 512-516
    • Bergsten, E.1    Uutela, M.2    Li, X.3    Pietras, K.4    Östman, A.5    Heldin, C.H.6
  • 12
    • 0033776193 scopus 로고    scopus 로고
    • PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor
    • Li X., Ponten A., Aase K., Karlsson L., Abramsson A., Uutela M., et al. PDGF-C is a new protease-activated ligand for the PDGF alpha-receptor. Nat Cell Biol 2000, 2:302-309.
    • (2000) Nat Cell Biol , vol.2 , pp. 302-309
    • Li, X.1    Ponten, A.2    Aase, K.3    Karlsson, L.4    Abramsson, A.5    Uutela, M.6
  • 13
    • 6344236867 scopus 로고    scopus 로고
    • Tissue plasminogen activator is a potent activator of PDGF-CC
    • Fredriksson L., Li H., Fieber C., Li X., Eriksson U. Tissue plasminogen activator is a potent activator of PDGF-CC. Embo J 2004, 23:3793-3802.
    • (2004) Embo J , vol.23 , pp. 3793-3802
    • Fredriksson, L.1    Li, H.2    Fieber, C.3    Li, X.4    Eriksson, U.5
  • 14
    • 46749118298 scopus 로고    scopus 로고
    • Activation of PDGF-CC by tissue plasminogen activator impairs blood-brain barrier integrity during ischemic stroke
    • Su E.J., Fredriksson L., Geyer M., Folestad E., Cale J., Andrae J., et al. Activation of PDGF-CC by tissue plasminogen activator impairs blood-brain barrier integrity during ischemic stroke. Nat Med 2008, 14:731-737.
    • (2008) Nat Med , vol.14 , pp. 731-737
    • Su, E.J.1    Fredriksson, L.2    Geyer, M.3    Folestad, E.4    Cale, J.5    Andrae, J.6
  • 15
    • 0034717056 scopus 로고    scopus 로고
    • Angiotensin II induces transactivation of two different populations of the platelet-derived growth factor beta receptor. Key role for the p66 adaptor protein Shc
    • Heeneman S., Haendeler J., Saito Y., Ishida M., Berk B.C. Angiotensin II induces transactivation of two different populations of the platelet-derived growth factor beta receptor. Key role for the p66 adaptor protein Shc. J Biol Chem 2000, 275:15926-15932.
    • (2000) J Biol Chem , vol.275 , pp. 15926-15932
    • Heeneman, S.1    Haendeler, J.2    Saito, Y.3    Ishida, M.4    Berk, B.C.5
  • 16
    • 70450222713 scopus 로고    scopus 로고
    • The dopamine D4 receptor activates intracellular platelet-derived growth factor receptor beta to stimulate ERK1/2
    • Gill R.S., Hsiung M.S., Sum C.S., Lavine N., Clark S.D., Van Tol H.H. The dopamine D4 receptor activates intracellular platelet-derived growth factor receptor beta to stimulate ERK1/2. Cell Signal 2010, 22:285-290.
    • (2010) Cell Signal , vol.22 , pp. 285-290
    • Gill, R.S.1    Hsiung, M.S.2    Sum, C.S.3    Lavine, N.4    Clark, S.D.5    Van Tol, H.H.6
  • 17
    • 37549043128 scopus 로고    scopus 로고
    • TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC
    • Siegbahn A., Johnell M., Nordin A., Aberg M., Velling T. TF/FVIIa transactivate PDGFRbeta to regulate PDGF-BB-induced chemotaxis in different cell types: involvement of Src and PLC. Arterioscler Thromb Vasc Biol 2008, 28:135-141.
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 135-141
    • Siegbahn, A.1    Johnell, M.2    Nordin, A.3    Aberg, M.4    Velling, T.5
  • 18
    • 33746086369 scopus 로고    scopus 로고
    • Angiotensin II stimulates phosphorylation of an ectodomain-truncated platelet-derived growth factor receptor-beta and its binding to class IA PI3K in vascular smooth muscle cells
    • Gao B.B., Hansen H., Chen H.C., Feener E.P. Angiotensin II stimulates phosphorylation of an ectodomain-truncated platelet-derived growth factor receptor-beta and its binding to class IA PI3K in vascular smooth muscle cells. Biochem J 2006, 397:337-344.
    • (2006) Biochem J , vol.397 , pp. 337-344
    • Gao, B.B.1    Hansen, H.2    Chen, H.C.3    Feener, E.P.4
  • 19
    • 34248137400 scopus 로고    scopus 로고
    • Vascular endothelial growth factor can signal through platelet-derived growth factor receptors
    • Ball S.G., Shuttleworth C.A., Kielty C.M. Vascular endothelial growth factor can signal through platelet-derived growth factor receptors. J Cell Biol 2007, 177:489-500.
    • (2007) J Cell Biol , vol.177 , pp. 489-500
    • Ball, S.G.1    Shuttleworth, C.A.2    Kielty, C.M.3
  • 20
    • 84861385990 scopus 로고    scopus 로고
    • Vascular endothelial growth factor A competitively inhibits platelet-derived growth factor (PDGF)-dependent activation of PDGF receptor and subsequent signaling events and cellular responses
    • Pennock S., Kazlauskas A. Vascular endothelial growth factor A competitively inhibits platelet-derived growth factor (PDGF)-dependent activation of PDGF receptor and subsequent signaling events and cellular responses. Mol Cell Biol 2012, 32:1955-1966.
    • (2012) Mol Cell Biol , vol.32 , pp. 1955-1966
    • Pennock, S.1    Kazlauskas, A.2
  • 21
    • 0030756325 scopus 로고    scopus 로고
    • Pericyte loss and microaneurysm formation in PDGF-B-deficient mice
    • Lindahl P., Johansson B.R., Leveen P., Betsholtz C. Pericyte loss and microaneurysm formation in PDGF-B-deficient mice. Science 1997, 277:242-245.
    • (1997) Science , vol.277 , pp. 242-245
    • Lindahl, P.1    Johansson, B.R.2    Leveen, P.3    Betsholtz, C.4
  • 22
    • 0030808324 scopus 로고    scopus 로고
    • The PDGF alpha receptor is required for neural crest cell development and for normal patterning of the somites
    • Soriano P. The PDGF alpha receptor is required for neural crest cell development and for normal patterning of the somites. Development 1997, 124:2691-2700.
    • (1997) Development , vol.124 , pp. 2691-2700
    • Soriano, P.1
  • 23
    • 6944220086 scopus 로고    scopus 로고
    • A specific requirement for PDGF-C in palate formation and PDGFR-alpha signaling
    • Ding H., Wu X., Bostrom H., Kim I., Wong N., Tsoi B., et al. A specific requirement for PDGF-C in palate formation and PDGFR-alpha signaling. Nat Genet 2004, 36:1111-1116.
    • (2004) Nat Genet , vol.36 , pp. 1111-1116
    • Ding, H.1    Wu, X.2    Bostrom, H.3    Kim, I.4    Wong, N.5    Tsoi, B.6
  • 24
    • 0035106689 scopus 로고    scopus 로고
    • The two PDGF receptors maintain conserved signaling in vivo despite divergent embryological functions
    • Klinghoffer R.A., Mueting-Nelsen P.F., Faerman A., Shani M., Soriano P. The two PDGF receptors maintain conserved signaling in vivo despite divergent embryological functions. Mol Cell 2001, 7:343-354.
    • (2001) Mol Cell , vol.7 , pp. 343-354
    • Klinghoffer, R.A.1    Mueting-Nelsen, P.F.2    Faerman, A.3    Shani, M.4    Soriano, P.5
  • 25
    • 47849085516 scopus 로고    scopus 로고
    • Becaplermin gel in the treatment of diabetic neuropathic foot ulcers
    • Papanas N., Maltezos E. Becaplermin gel in the treatment of diabetic neuropathic foot ulcers. Clin Interv Aging 2008, 3:233-240.
    • (2008) Clin Interv Aging , vol.3 , pp. 233-240
    • Papanas, N.1    Maltezos, E.2
  • 26
    • 0035153593 scopus 로고    scopus 로고
    • Platelet-derived growth factor B-chain of hematopoietic origin is not necessary for granulation tissue formation and its absence enhances vascularization
    • Buetow B.S., Crosby J.R., Kaminski W.E., Ramachandran R.K., Lindahl P., Martin P., et al. Platelet-derived growth factor B-chain of hematopoietic origin is not necessary for granulation tissue formation and its absence enhances vascularization. Am J Pathol 2001, 159:1869-1876.
    • (2001) Am J Pathol , vol.159 , pp. 1869-1876
    • Buetow, B.S.1    Crosby, J.R.2    Kaminski, W.E.3    Ramachandran, R.K.4    Lindahl, P.5    Martin, P.6
  • 27
    • 0033613119 scopus 로고    scopus 로고
    • Platelet-derived growth factor beta receptor regulates interstitial fluid homeostasis through phosphatidylinositol-3' kinase signaling
    • Heuchel R., Berg A., Tallquist M., Ahlen K., Reed R.K., Rubin K., et al. Platelet-derived growth factor beta receptor regulates interstitial fluid homeostasis through phosphatidylinositol-3' kinase signaling. Proc Natl Acad Sci U S A 1999, 96:11410-11415.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11410-11415
    • Heuchel, R.1    Berg, A.2    Tallquist, M.3    Ahlen, K.4    Reed, R.K.5    Rubin, K.6
  • 28
    • 77957738175 scopus 로고    scopus 로고
    • New insights into the mechanisms of hematopoietic cell transformation by activated receptor tyrosine kinases
    • Toffalini F., Demoulin J.B. New insights into the mechanisms of hematopoietic cell transformation by activated receptor tyrosine kinases. Blood 2010, 116:2429-2437.
    • (2010) Blood , vol.116 , pp. 2429-2437
    • Toffalini, F.1    Demoulin, J.B.2
  • 29
    • 84890467312 scopus 로고    scopus 로고
    • Targeting the PDGF signaling pathway in tumor treatment
    • Heldin C.H. Targeting the PDGF signaling pathway in tumor treatment. Cell Commun Signal 2013, 11:97.
    • (2013) Cell Commun Signal , vol.11 , pp. 97
    • Heldin, C.H.1
  • 30
    • 84901199522 scopus 로고    scopus 로고
    • PDGFRA alterations in cancer: characterization of a gain-of-function V536E transmembrane mutant as well as loss-of-function and passenger mutations
    • Velghe A.I., Van Cauwenberghe S., Polyansky A.A., Chand D., Montano-Almendras C.P., Charni S., et al. PDGFRA alterations in cancer: characterization of a gain-of-function V536E transmembrane mutant as well as loss-of-function and passenger mutations. Oncogene 2014, 10.1038/onc.2013.218.
    • (2014) Oncogene
    • Velghe, A.I.1    Van Cauwenberghe, S.2    Polyansky, A.A.3    Chand, D.4    Montano-Almendras, C.P.5    Charni, S.6
  • 31
    • 84856323402 scopus 로고    scopus 로고
    • Tyrosine kinase gene fusions in cancer: translating mechanisms into targeted therapies
    • Medves S., Demoulin J.B. Tyrosine kinase gene fusions in cancer: translating mechanisms into targeted therapies. J Cell Mol Med 2012, 16:237-248.
    • (2012) J Cell Mol Med , vol.16 , pp. 237-248
    • Medves, S.1    Demoulin, J.B.2
  • 32
    • 84867870486 scopus 로고    scopus 로고
    • Platelet-derived growth factors and their receptors in normal and malignant hematopoiesis
    • Demoulin J.B., Montano-Almendras C.P. Platelet-derived growth factors and their receptors in normal and malignant hematopoiesis. Am J Blood Res 2012, 2:44-56.
    • (2012) Am J Blood Res , vol.2 , pp. 44-56
    • Demoulin, J.B.1    Montano-Almendras, C.P.2
  • 33
    • 84902121228 scopus 로고    scopus 로고
    • Review of current classification, molecular alterations, and tyrosine kinase inhibitor therapies in myeloproliferative disorders with hypereosinophilia
    • Havelange V., Demoulin J.B. Review of current classification, molecular alterations, and tyrosine kinase inhibitor therapies in myeloproliferative disorders with hypereosinophilia. J Blood Med 2013, 4:111-121.
    • (2013) J Blood Med , vol.4 , pp. 111-121
    • Havelange, V.1    Demoulin, J.B.2
  • 35
    • 65249139405 scopus 로고    scopus 로고
    • Lack of evidence of stimulatory autoantibodies to platelet-derived growth factor receptor in patients with systemic sclerosis
    • Classen J.F., Henrohn D., Rorsman F., Lennartsson J., Lauwerys B.R., Wikstrom G., et al. Lack of evidence of stimulatory autoantibodies to platelet-derived growth factor receptor in patients with systemic sclerosis. Arthritis Rheum 2009, 60:1137-1144.
    • (2009) Arthritis Rheum , vol.60 , pp. 1137-1144
    • Classen, J.F.1    Henrohn, D.2    Rorsman, F.3    Lennartsson, J.4    Lauwerys, B.R.5    Wikstrom, G.6
  • 37
    • 65249190778 scopus 로고    scopus 로고
    • Lack of detection of agonist activity by antibodies to platelet-derived growth factor receptor alpha in a subset of normal and systemic sclerosis patient sera
    • Loizos N., Lariccia L., Weiner J., Griffith H., Boin F., Hummers L., et al. Lack of detection of agonist activity by antibodies to platelet-derived growth factor receptor alpha in a subset of normal and systemic sclerosis patient sera. Arthritis Rheum 2009, 60:1145-1151.
    • (2009) Arthritis Rheum , vol.60 , pp. 1145-1151
    • Loizos, N.1    Lariccia, L.2    Weiner, J.3    Griffith, H.4    Boin, F.5    Hummers, L.6
  • 38
    • 80054112357 scopus 로고    scopus 로고
    • A phase 1 study of imatinib for corticosteroid-dependent/refractory chronic graft-versus-host disease: response does not correlate with anti-PDGFRA antibodies
    • Chen G.L., Arai S., Flowers M.E., Otani J.M., Qiu J., Cheng E.C., et al. A phase 1 study of imatinib for corticosteroid-dependent/refractory chronic graft-versus-host disease: response does not correlate with anti-PDGFRA antibodies. Blood 2011, 118:4070-4078.
    • (2011) Blood , vol.118 , pp. 4070-4078
    • Chen, G.L.1    Arai, S.2    Flowers, M.E.3    Otani, J.M.4    Qiu, J.5    Cheng, E.C.6
  • 39
    • 33644514694 scopus 로고    scopus 로고
    • Bovine papillomavirus E5 oncoprotein binds to the activated form of the platelet-derived growth factor beta receptor in naturally occurring bovine urinary bladder tumours
    • Borzacchiello G., Russo V., Gentile F., Roperto F., Venuti A., Nitsch L., et al. Bovine papillomavirus E5 oncoprotein binds to the activated form of the platelet-derived growth factor beta receptor in naturally occurring bovine urinary bladder tumours. Oncogene 2006, 25:1251-1260.
    • (2006) Oncogene , vol.25 , pp. 1251-1260
    • Borzacchiello, G.1    Russo, V.2    Gentile, F.3    Roperto, F.4    Venuti, A.5    Nitsch, L.6
  • 40
    • 52149090536 scopus 로고    scopus 로고
    • Platelet-derived growth factor-alpha receptor activation is required for human cytomegalovirus infection
    • Soroceanu L., Akhavan A., Cobbs C.S. Platelet-derived growth factor-alpha receptor activation is required for human cytomegalovirus infection. Nature 2008, 455:391-395.
    • (2008) Nature , vol.455 , pp. 391-395
    • Soroceanu, L.1    Akhavan, A.2    Cobbs, C.S.3
  • 41
    • 84866893032 scopus 로고    scopus 로고
    • PDGF receptor-alpha does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway
    • Vanarsdall A.L., Wisner T.W., Lei H., Kazlauskas A., Johnson D.C. PDGF receptor-alpha does not promote HCMV entry into epithelial and endothelial cells but increased quantities stimulate entry by an abnormal pathway. PLoS Pathog 2012, 8:e1002905.
    • (2012) PLoS Pathog , vol.8
    • Vanarsdall, A.L.1    Wisner, T.W.2    Lei, H.3    Kazlauskas, A.4    Johnson, D.C.5
  • 43
    • 84860548973 scopus 로고    scopus 로고
    • Mutation in the platelet-derived growth factor receptor alpha inhibits adeno-associated virus type 5 transduction
    • Pilz I.H., Di Pasquale G., Rzadzinska A., Leppla S.H., Chiorini J.A. Mutation in the platelet-derived growth factor receptor alpha inhibits adeno-associated virus type 5 transduction. Virology 2012, 428:58-63.
    • (2012) Virology , vol.428 , pp. 58-63
    • Pilz, I.H.1    Di Pasquale, G.2    Rzadzinska, A.3    Leppla, S.H.4    Chiorini, J.A.5
  • 44
    • 42949086499 scopus 로고    scopus 로고
    • RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry
    • Elwell C.A., Ceesay A., Kim J.H., Kalman D., Engel J.N. RNA interference screen identifies Abl kinase and PDGFR signaling in Chlamydia trachomatis entry. PLoS Pathog 2008, 4:e1000021.
    • (2008) PLoS Pathog , vol.4
    • Elwell, C.A.1    Ceesay, A.2    Kim, J.H.3    Kalman, D.4    Engel, J.N.5
  • 45
    • 84869096442 scopus 로고    scopus 로고
    • Long-term follow-up of FIP1L1-PDGFRA-mutated patients with eosinophilia: survival and clinical outcome
    • Pardanani A., D'Souza A., Knudson R.A., Hanson C.A., Ketterling R.P., Tefferi A. Long-term follow-up of FIP1L1-PDGFRA-mutated patients with eosinophilia: survival and clinical outcome. Leukemia 2012, 26:2439-2441.
    • (2012) Leukemia , vol.26 , pp. 2439-2441
    • Pardanani, A.1    D'Souza, A.2    Knudson, R.A.3    Hanson, C.A.4    Ketterling, R.P.5    Tefferi, A.6
  • 46
    • 66849087150 scopus 로고    scopus 로고
    • FIP1L1-PDGFRalpha D842V, a novel panresistant mutant, emerging after treatment of FIP1L1-PDGFRalpha T674I eosinophilic leukemia with single agent sorafenib
    • Lierman E., Michaux L., Beullens E., Pierre P., Marynen P., Cools J., et al. FIP1L1-PDGFRalpha D842V, a novel panresistant mutant, emerging after treatment of FIP1L1-PDGFRalpha T674I eosinophilic leukemia with single agent sorafenib. Leukemia 2009, 23:845-851.
    • (2009) Leukemia , vol.23 , pp. 845-851
    • Lierman, E.1    Michaux, L.2    Beullens, E.3    Pierre, P.4    Marynen, P.5    Cools, J.6
  • 47
    • 71649102124 scopus 로고    scopus 로고
    • Multicentre phase II studies evaluating imatinib plus hydroxyurea in patients with progressive glioblastoma
    • Reardon D.A., Dresemann G., Taillibert S., Campone M., van den Bent M., Clement P., et al. Multicentre phase II studies evaluating imatinib plus hydroxyurea in patients with progressive glioblastoma. Br J Cancer 2009, 101:1995-2004.
    • (2009) Br J Cancer , vol.101 , pp. 1995-2004
    • Reardon, D.A.1    Dresemann, G.2    Taillibert, S.3    Campone, M.4    van den Bent, M.5    Clement, P.6
  • 48
    • 84896544087 scopus 로고    scopus 로고
    • Targeting the PDGF signaling pathway in the treatment of non-malignant diseases
    • Heldin C.H. Targeting the PDGF signaling pathway in the treatment of non-malignant diseases. J Neuroimmun Pharmacol 2014, 9:69-79.
    • (2014) J Neuroimmun Pharmacol , vol.9 , pp. 69-79
    • Heldin, C.H.1
  • 49
    • 0030977132 scopus 로고    scopus 로고
    • Immunoglobulin-like domain 4-mediated receptor-receptor interactions contribute to platelet-derived growth factor-induced receptor dimerization
    • Omura T., Heldin C.H., Ostman A. Immunoglobulin-like domain 4-mediated receptor-receptor interactions contribute to platelet-derived growth factor-induced receptor dimerization. J Biol Chem 1997, 272:12676-12682.
    • (1997) J Biol Chem , vol.272 , pp. 12676-12682
    • Omura, T.1    Heldin, C.H.2    Ostman, A.3
  • 50
    • 2442437841 scopus 로고    scopus 로고
    • Autoinhibition of the platelet-derived growth factor beta-receptor tyrosine kinase by its C-terminal tail
    • Chiara F., Bishayee S., Heldin C.H., Demoulin J.B. Autoinhibition of the platelet-derived growth factor beta-receptor tyrosine kinase by its C-terminal tail. J Biol Chem 2004, 279:19732-19738.
    • (2004) J Biol Chem , vol.279 , pp. 19732-19738
    • Chiara, F.1    Bishayee, S.2    Heldin, C.H.3    Demoulin, J.B.4
  • 51
    • 77953696895 scopus 로고    scopus 로고
    • Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration
    • Wardega P., Heldin C.H., Lennartsson J. Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration. Cell Signal 2010, 22:1363-1368.
    • (2010) Cell Signal , vol.22 , pp. 1363-1368
    • Wardega, P.1    Heldin, C.H.2    Lennartsson, J.3
  • 52
    • 0031899815 scopus 로고    scopus 로고
    • Activation of Src family members is not required for the platelet-derived growth factor beta receptor to initiate mitogenesis
    • DeMali K.A., Kazlauskas A. Activation of Src family members is not required for the platelet-derived growth factor beta receptor to initiate mitogenesis. Mol Cell Biol 1998, 18:2014-2022.
    • (1998) Mol Cell Biol , vol.18 , pp. 2014-2022
    • DeMali, K.A.1    Kazlauskas, A.2
  • 53
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer R.A., Sachsenmaier C., Cooper J.A., Soriano P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J 1999, 18:2459-2471.
    • (1999) EMBO J , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 54
    • 0034212787 scopus 로고    scopus 로고
    • No requirement for src family kinases for PDGF signaling in fibroblasts expressing SV40 large T antigen
    • Broome M.A., Courtneidge S.A. No requirement for src family kinases for PDGF signaling in fibroblasts expressing SV40 large T antigen. Oncogene 2000, 19:2867-2869.
    • (2000) Oncogene , vol.19 , pp. 2867-2869
    • Broome, M.A.1    Courtneidge, S.A.2
  • 55
    • 34247354963 scopus 로고    scopus 로고
    • Myeloproliferative disease induced by TEL-PDGFRB displays dynamic range sensitivity to Stat5 gene dosage
    • Cain J.A., Xiang Z., O'Neal J., Kreisel F., Colson A., Luo H., et al. Myeloproliferative disease induced by TEL-PDGFRB displays dynamic range sensitivity to Stat5 gene dosage. Blood 2007, 109:3906-3914.
    • (2007) Blood , vol.109 , pp. 3906-3914
    • Cain, J.A.1    Xiang, Z.2    O'Neal, J.3    Kreisel, F.4    Colson, A.5    Luo, H.6
  • 56
    • 0034458943 scopus 로고    scopus 로고
    • SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling
    • Blake R.A., Broome M.A., Liu X., Wu J., Gishizky M., Sun L., et al. SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling. Mol Cell Biol 2000, 20:9018-9027.
    • (2000) Mol Cell Biol , vol.20 , pp. 9018-9027
    • Blake, R.A.1    Broome, M.A.2    Liu, X.3    Wu, J.4    Gishizky, M.5    Sun, L.6
  • 57
    • 0029791504 scopus 로고    scopus 로고
    • Mutation of a Src phosphorylation site in the PDGF beta-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis
    • Hansen K., Johnell M., Siegbahn A., Rorsman C., Engstrom U., Wernstedt C., et al. Mutation of a Src phosphorylation site in the PDGF beta-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis. EMBO J 1996, 15:5299-5313.
    • (1996) EMBO J , vol.15 , pp. 5299-5313
    • Hansen, K.1    Johnell, M.2    Siegbahn, A.3    Rorsman, C.4    Engstrom, U.5    Wernstedt, C.6
  • 58
    • 70350572219 scopus 로고    scopus 로고
    • Identification of c-Src tyrosine kinase substrates in platelet-derived growth factor receptor signaling
    • Amanchy R., Zhong J., Hong R., Kim J.H., Gucek M., Cole R.N., et al. Identification of c-Src tyrosine kinase substrates in platelet-derived growth factor receptor signaling. Mol Oncol 2009, 3:439-450.
    • (2009) Mol Oncol , vol.3 , pp. 439-450
    • Amanchy, R.1    Zhong, J.2    Hong, R.3    Kim, J.H.4    Gucek, M.5    Cole, R.N.6
  • 59
    • 0033568349 scopus 로고    scopus 로고
    • C-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
    • Plattner R., Kadlec L., DeMali K.A., Kazlauskas A., Pendergast A.M. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev 1999, 13:2400-2411.
    • (1999) Genes Dev , vol.13 , pp. 2400-2411
    • Plattner, R.1    Kadlec, L.2    DeMali, K.A.3    Kazlauskas, A.4    Pendergast, A.M.5
  • 60
    • 1542314233 scopus 로고    scopus 로고
    • Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor
    • Plattner R., Koleske A.J., Kazlauskas A., Pendergast A.M. Bidirectional signaling links the Abelson kinases to the platelet-derived growth factor receptor. Mol Cell Biol 2004, 24:2573-2583.
    • (2004) Mol Cell Biol , vol.24 , pp. 2573-2583
    • Plattner, R.1    Koleske, A.J.2    Kazlauskas, A.3    Pendergast, A.M.4
  • 61
    • 0037084333 scopus 로고    scopus 로고
    • C-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis
    • Furstoss O., Dorey K., Simon V., Barila D., Superti-Furga G., Roche S. c-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis. EMBO J 2002, 21:514-524.
    • (2002) EMBO J , vol.21 , pp. 514-524
    • Furstoss, O.1    Dorey, K.2    Simon, V.3    Barila, D.4    Superti-Furga, G.5    Roche, S.6
  • 62
    • 0037384252 scopus 로고    scopus 로고
    • A new link between the c-Abl tyrosine kinase and phosphoinositide signalling through PLC-gamma1
    • Plattner R., Irvin B.J., Guo S., Blackburn K., Kazlauskas A., Abraham R.T., et al. A new link between the c-Abl tyrosine kinase and phosphoinositide signalling through PLC-gamma1. Nat Cell Biol 2003, 5:309-319.
    • (2003) Nat Cell Biol , vol.5 , pp. 309-319
    • Plattner, R.1    Irvin, B.J.2    Guo, S.3    Blackburn, K.4    Kazlauskas, A.5    Abraham, R.T.6
  • 63
    • 24944563129 scopus 로고    scopus 로고
    • Abl tyrosine kinase regulates a Rac/JNK and a Rac/Nox pathway for DNA synthesis and Myc expression induced by growth factors
    • Boureux A., Furstoss O., Simon V., Roche S. Abl tyrosine kinase regulates a Rac/JNK and a Rac/Nox pathway for DNA synthesis and Myc expression induced by growth factors. J Cell Sci 2005, 118:3717-3726.
    • (2005) J Cell Sci , vol.118 , pp. 3717-3726
    • Boureux, A.1    Furstoss, O.2    Simon, V.3    Roche, S.4
  • 64
    • 0034978163 scopus 로고    scopus 로고
    • Regulation of c-myc expression by PDGF through Rho GTPases
    • Chiariello M., Marinissen M.J., Gutkind J.S. Regulation of c-myc expression by PDGF through Rho GTPases. Nat Cell Biol 2001, 3:580-586.
    • (2001) Nat Cell Biol , vol.3 , pp. 580-586
    • Chiariello, M.1    Marinissen, M.J.2    Gutkind, J.S.3
  • 65
    • 84055191095 scopus 로고    scopus 로고
    • Activation of Rac1 by Src-dependent phosphorylation of Dock180(Y1811) mediates PDGFRalpha-stimulated glioma tumorigenesis in mice and humans
    • Feng H., Hu B., Liu K.W., Li Y., Lu X., Cheng T., et al. Activation of Rac1 by Src-dependent phosphorylation of Dock180(Y1811) mediates PDGFRalpha-stimulated glioma tumorigenesis in mice and humans. J Clin Invest 2011, 121:4670-4684.
    • (2011) J Clin Invest , vol.121 , pp. 4670-4684
    • Feng, H.1    Hu, B.2    Liu, K.W.3    Li, Y.4    Lu, X.5    Cheng, T.6
  • 67
    • 0035160210 scopus 로고    scopus 로고
    • Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation
    • Craig A.W., Zirngibl R., Williams K., Cole L.A., Greer P.A. Mice devoid of fer protein-tyrosine kinase activity are viable and fertile but display reduced cortactin phosphorylation. Mol Cell Biol 2001, 21:603-613.
    • (2001) Mol Cell Biol , vol.21 , pp. 603-613
    • Craig, A.W.1    Zirngibl, R.2    Williams, K.3    Cole, L.A.4    Greer, P.A.5
  • 68
    • 84878419114 scopus 로고    scopus 로고
    • The Fer tyrosine kinase is important for platelet-derived growth factor-BB-induced signal transducer and activator of transcription 3 (STAT3) protein phosphorylation, colony formation in soft agar, and tumor growth in vivo
    • Lennartsson J., Ma H., Wardega P., Pelka K., Engstrom U., Hellberg C., et al. The Fer tyrosine kinase is important for platelet-derived growth factor-BB-induced signal transducer and activator of transcription 3 (STAT3) protein phosphorylation, colony formation in soft agar, and tumor growth in vivo. J Biol Chem 2013, 288:15736-15744.
    • (2013) J Biol Chem , vol.288 , pp. 15736-15744
    • Lennartsson, J.1    Ma, H.2    Wardega, P.3    Pelka, K.4    Engstrom, U.5    Hellberg, C.6
  • 69
    • 1542328927 scopus 로고    scopus 로고
    • Structure, regulation and function of PKB/AKT - a major therapeutic target
    • Hanada M., Feng J., Hemmings B.A. Structure, regulation and function of PKB/AKT - a major therapeutic target. Biochim Biophys Acta 2004, 1697:3-16.
    • (2004) Biochim Biophys Acta , vol.1697 , pp. 3-16
    • Hanada, M.1    Feng, J.2    Hemmings, B.A.3
  • 70
    • 0032547385 scopus 로고    scopus 로고
    • Signal transduction via platelet-derived growth factor receptors
    • Heldin C.H., Östman A., Rönnstrand L. Signal transduction via platelet-derived growth factor receptors. Biochim Biophys Acta 1998, 1378:F79-F113.
    • (1998) Biochim Biophys Acta , vol.1378
    • Heldin, C.H.1    Östman, A.2    Rönnstrand, L.3
  • 71
    • 67449100489 scopus 로고    scopus 로고
    • The transcription of FOXO genes is stimulated by FOXO3 and repressed by growth factors
    • Essaghir A., Dif N., Marbehant C.Y., Coffer P.J., Demoulin J.B. The transcription of FOXO genes is stimulated by FOXO3 and repressed by growth factors. J Biol Chem 2009, 284:10334-10342.
    • (2009) J Biol Chem , vol.284 , pp. 10334-10342
    • Essaghir, A.1    Dif, N.2    Marbehant, C.Y.3    Coffer, P.J.4    Demoulin, J.B.5
  • 72
    • 34247198341 scopus 로고    scopus 로고
    • The forkhead transcription factor FoxO1 regulates proliferation and transdifferentiation of hepatic stellate cells
    • Adachi M., Osawa Y., Uchinami H., Kitamura T., Accili D., Brenner D.A. The forkhead transcription factor FoxO1 regulates proliferation and transdifferentiation of hepatic stellate cells. Gastroenterology 2007, 132:1434-1446.
    • (2007) Gastroenterology , vol.132 , pp. 1434-1446
    • Adachi, M.1    Osawa, Y.2    Uchinami, H.3    Kitamura, T.4    Accili, D.5    Brenner, D.A.6
  • 73
    • 23844491841 scopus 로고    scopus 로고
    • Forkhead transcription factors inhibit vascular smooth muscle cell proliferation and neointimal hyperplasia
    • Abid M.R., Yano K., Guo S., Patel V.I., Shrikhande G., Spokes K.C., et al. Forkhead transcription factors inhibit vascular smooth muscle cell proliferation and neointimal hyperplasia. J Biol Chem 2005, 280:29864-29873.
    • (2005) J Biol Chem , vol.280 , pp. 29864-29873
    • Abid, M.R.1    Yano, K.2    Guo, S.3    Patel, V.I.4    Shrikhande, G.5    Spokes, K.C.6
  • 74
    • 0033517190 scopus 로고    scopus 로고
    • NF-kappaB is a target of AKT in anti-apoptotic PDGF signalling
    • Romashkova J.A., Makarov S.S. NF-kappaB is a target of AKT in anti-apoptotic PDGF signalling. Nature 1999, 401:86-90.
    • (1999) Nature , vol.401 , pp. 86-90
    • Romashkova, J.A.1    Makarov, S.S.2
  • 75
    • 0034623313 scopus 로고    scopus 로고
    • PDGF-induced Akt phosphorylation does not activate NF-kappa B in human vascular smooth muscle cells and fibroblasts
    • Rauch B.H., Weber A., Braun M., Zimmermann N., Schror K. PDGF-induced Akt phosphorylation does not activate NF-kappa B in human vascular smooth muscle cells and fibroblasts. FEBS Lett 2000, 481:3-7.
    • (2000) FEBS Lett , vol.481 , pp. 3-7
    • Rauch, B.H.1    Weber, A.2    Braun, M.3    Zimmermann, N.4    Schror, K.5
  • 76
    • 12344253991 scopus 로고    scopus 로고
    • Activation of vascular smooth muscle cells by TNF and PDGF: overlapping and complementary signal transduction mechanisms
    • Peppel K., Zhang L., Orman E.S., Hagen P.O., Amalfitano A., Brian L., et al. Activation of vascular smooth muscle cells by TNF and PDGF: overlapping and complementary signal transduction mechanisms. Cardiovasc Res 2005, 65:674-682.
    • (2005) Cardiovasc Res , vol.65 , pp. 674-682
    • Peppel, K.1    Zhang, L.2    Orman, E.S.3    Hagen, P.O.4    Amalfitano, A.5    Brian, L.6
  • 77
    • 84862694326 scopus 로고    scopus 로고
    • ETV6-PDGFRB and FIP1L1-PDGFRA stimulate human hematopoietic progenitor proliferation and differentiation into eosinophils: role of NF-kappaB
    • Montano-Almendras C.P., Essaghir A., Schoemans H., Varis I., Noel L.A., Velghe A.I., et al. ETV6-PDGFRB and FIP1L1-PDGFRA stimulate human hematopoietic progenitor proliferation and differentiation into eosinophils: role of NF-kappaB. Haematologica 2012, 97:1064-1072.
    • (2012) Haematologica , vol.97 , pp. 1064-1072
    • Montano-Almendras, C.P.1    Essaghir, A.2    Schoemans, H.3    Varis, I.4    Noel, L.A.5    Velghe, A.I.6
  • 78
    • 0036024621 scopus 로고    scopus 로고
    • Activation of NF-kappaB is required for PDGF-B chain to transform NIH3T3 cells
    • Shimamura T., Hsu T.C., Colburn N.H., Bejcek B.E. Activation of NF-kappaB is required for PDGF-B chain to transform NIH3T3 cells. Exp Cell Res 2002, 274:157-167.
    • (2002) Exp Cell Res , vol.274 , pp. 157-167
    • Shimamura, T.1    Hsu, T.C.2    Colburn, N.H.3    Bejcek, B.E.4
  • 79
    • 0032493369 scopus 로고    scopus 로고
    • Evidence for a role of NF-kappaB in the survival of hematopoietic cells mediated by interleukin 3 and the oncogenic TEL/platelet-derived growth factor receptor beta fusion protein
    • Besancon F., Atfi A., Gespach C., Cayre Y.E., Bourgeade M.F. Evidence for a role of NF-kappaB in the survival of hematopoietic cells mediated by interleukin 3 and the oncogenic TEL/platelet-derived growth factor receptor beta fusion protein. Proc Natl Acad Sci U S A 1998, 95:8081-8086.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8081-8086
    • Besancon, F.1    Atfi, A.2    Gespach, C.3    Cayre, Y.E.4    Bourgeade, M.F.5
  • 80
    • 4143050198 scopus 로고    scopus 로고
    • Platelet-derived growth factor stimulates membrane lipid synthesis through activation of phosphatidylinositol 3-kinase and sterol regulatory element-binding proteins
    • Demoulin J.B., Ericsson J., Kallin A., Rorsman C., Ronnstrand L., Heldin C.H. Platelet-derived growth factor stimulates membrane lipid synthesis through activation of phosphatidylinositol 3-kinase and sterol regulatory element-binding proteins. J Biol Chem 2004, 279:35392-35402.
    • (2004) J Biol Chem , vol.279 , pp. 35392-35402
    • Demoulin, J.B.1    Ericsson, J.2    Kallin, A.3    Rorsman, C.4    Ronnstrand, L.5    Heldin, C.H.6
  • 81
    • 23844530704 scopus 로고    scopus 로고
    • Control of lipid metabolism by phosphorylation-dependent degradation of the SREBP family of transcription factors by SCF(Fbw7)
    • Sundqvist A., Bengoechea-Alonso M.T., Ye X., Lukiyanchuk V., Jin J., Harper J.W., et al. Control of lipid metabolism by phosphorylation-dependent degradation of the SREBP family of transcription factors by SCF(Fbw7). Cell Metab 2005, 1:379-391.
    • (2005) Cell Metab , vol.1 , pp. 379-391
    • Sundqvist, A.1    Bengoechea-Alonso, M.T.2    Ye, X.3    Lukiyanchuk, V.4    Jin, J.5    Harper, J.W.6
  • 82
    • 50049116472 scopus 로고    scopus 로고
    • SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth
    • Porstmann T., Santos C.R., Griffiths B., Cully M., Wu M., Leevers S., et al. SREBP activity is regulated by mTORC1 and contributes to Akt-dependent cell growth. Cell Metab 2008, 8:224-236.
    • (2008) Cell Metab , vol.8 , pp. 224-236
    • Porstmann, T.1    Santos, C.R.2    Griffiths, B.3    Cully, M.4    Wu, M.5    Leevers, S.6
  • 83
    • 0036007120 scopus 로고    scopus 로고
    • An allelic series at the PDGFalphaR locus indicates unequal contributions of distinct signaling pathways during development
    • Klinghoffer R.A., Hamilton T.G., Hoch R., Soriano P. An allelic series at the PDGFalphaR locus indicates unequal contributions of distinct signaling pathways during development. Dev Cell 2002, 2:103-113.
    • (2002) Dev Cell , vol.2 , pp. 103-113
    • Klinghoffer, R.A.1    Hamilton, T.G.2    Hoch, R.3    Soriano, P.4
  • 84
    • 15044358690 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-kinase regulatory isoforms in development and actin rearrangement
    • Brachmann S.M., Yballe C.M., Innocenti M., Deane J.A., Fruman D.A., Thomas S.M., et al. Role of phosphoinositide 3-kinase regulatory isoforms in development and actin rearrangement. Mol Cell Biol 2005, 25:2593-2606.
    • (2005) Mol Cell Biol , vol.25 , pp. 2593-2606
    • Brachmann, S.M.1    Yballe, C.M.2    Innocenti, M.3    Deane, J.A.4    Fruman, D.A.5    Thomas, S.M.6
  • 85
    • 33644504867 scopus 로고    scopus 로고
    • PTEN tumor suppressor associates with NHERF proteins to attenuate PDGF receptor signaling
    • Takahashi Y., Morales F.C., Kreimann E.L., Georgescu M.M. PTEN tumor suppressor associates with NHERF proteins to attenuate PDGF receptor signaling. EMBO J 2006, 25:910-920.
    • (2006) EMBO J , vol.25 , pp. 910-920
    • Takahashi, Y.1    Morales, F.C.2    Kreimann, E.L.3    Georgescu, M.M.4
  • 86
    • 0033755880 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor association with Na(+)/H(+) exchanger regulatory factor potentiates receptor activity
    • Maudsley S., Zamah A.M., Rahman N., Blitzer J.T., Luttrell L.M., Lefkowitz R.J., et al. Platelet-derived growth factor receptor association with Na(+)/H(+) exchanger regulatory factor potentiates receptor activity. Mol Cell Biol 2000, 20:8352-8363.
    • (2000) Mol Cell Biol , vol.20 , pp. 8352-8363
    • Maudsley, S.1    Zamah, A.M.2    Rahman, N.3    Blitzer, J.T.4    Luttrell, L.M.5    Lefkowitz, R.J.6
  • 87
    • 0346256772 scopus 로고    scopus 로고
    • +-exchanger regulatory factor to the PDGF (platelet-derived growth factor) receptor regulates actin cytoskeleton reorganization by PDGF
    • +-exchanger regulatory factor to the PDGF (platelet-derived growth factor) receptor regulates actin cytoskeleton reorganization by PDGF. Biochem J 2003, 376:505-510.
    • (2003) Biochem J , vol.376 , pp. 505-510
    • Demoulin, J.B.1    Seo, J.K.2    Ekman, S.3    Grapengiesser, E.4    Hellman, U.5    Ronnstrand, L.6
  • 89
    • 2342418250 scopus 로고    scopus 로고
    • Gab1 contributes to cytoskeletal reorganization and chemotaxis in response to platelet-derived growth factor
    • Kallin A., Demoulin J.B., Nishida K., Hirano T., Ronnstrand L., Heldin C.H. Gab1 contributes to cytoskeletal reorganization and chemotaxis in response to platelet-derived growth factor. J Biol Chem 2004, 279:17897-17904.
    • (2004) J Biol Chem , vol.279 , pp. 17897-17904
    • Kallin, A.1    Demoulin, J.B.2    Nishida, K.3    Hirano, T.4    Ronnstrand, L.5    Heldin, C.H.6
  • 90
    • 0033600129 scopus 로고    scopus 로고
    • SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis
    • Ronnstrand L., Arvidsson A.K., Kallin A., Rorsman C., Hellman U., Engstrom U., et al. SHP-2 binds to Tyr763 and Tyr1009 in the PDGF beta-receptor and mediates PDGF-induced activation of the Ras/MAP kinase pathway and chemotaxis. Oncogene 1999, 18:3696-3702.
    • (1999) Oncogene , vol.18 , pp. 3696-3702
    • Ronnstrand, L.1    Arvidsson, A.K.2    Kallin, A.3    Rorsman, C.4    Hellman, U.5    Engstrom, U.6
  • 91
    • 0032570586 scopus 로고    scopus 로고
    • The Shp-2 tyrosine phosphatase has opposite effects in mediating the activation of extracellular signal-regulated and c-Jun NH2-terminal mitogen-activated protein kinases
    • Shi Z.Q., Lu W., Feng G.S. The Shp-2 tyrosine phosphatase has opposite effects in mediating the activation of extracellular signal-regulated and c-Jun NH2-terminal mitogen-activated protein kinases. J Biol Chem 1998, 273:4904-4908.
    • (1998) J Biol Chem , vol.273 , pp. 4904-4908
    • Shi, Z.Q.1    Lu, W.2    Feng, G.S.3
  • 92
    • 0029860951 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation
    • Bazenet C.E., Gelderloos J.A., Kazlauskas A. Phosphorylation of tyrosine 720 in the platelet-derived growth factor alpha receptor is required for binding of Grb2 and SHP-2 but not for activation of Ras or cell proliferation. Mol Cell Biol 1996, 16:6926-6936.
    • (1996) Mol Cell Biol , vol.16 , pp. 6926-6936
    • Bazenet, C.E.1    Gelderloos, J.A.2    Kazlauskas, A.3
  • 93
    • 84899474059 scopus 로고    scopus 로고
    • The tyrosine phosphatase SHP2 is required for cell transformation by the receptor tyrosine kinase mutants FIP1L1-PDGFRA and PDGFRA D842V
    • Noël L.A., Arts F.A., Montano-Almendras C.P., Cox L., Gielen O., Toffalini F., et al. The tyrosine phosphatase SHP2 is required for cell transformation by the receptor tyrosine kinase mutants FIP1L1-PDGFRA and PDGFRA D842V. Mol Oncol 2014, 10.1016/j.molonc.2014.02.003.
    • (2014) Mol Oncol
    • Noël, L.A.1    Arts, F.A.2    Montano-Almendras, C.P.3    Cox, L.4    Gielen, O.5    Toffalini, F.6
  • 94
    • 34249026448 scopus 로고    scopus 로고
    • Binding of ras to phosphoinositide 3-kinase p110alpha is required for ras-driven tumorigenesis in mice
    • Gupta S., Ramjaun A.R., Haiko P., Wang Y., Warne P.H., Nicke B., et al. Binding of ras to phosphoinositide 3-kinase p110alpha is required for ras-driven tumorigenesis in mice. Cell 2007, 129:957-968.
    • (2007) Cell , vol.129 , pp. 957-968
    • Gupta, S.1    Ramjaun, A.R.2    Haiko, P.3    Wang, Y.4    Warne, P.H.5    Nicke, B.6
  • 95
    • 0037075815 scopus 로고    scopus 로고
    • SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor
    • Ekman S., Kallin A., Engstrom U., Heldin C.H., Ronnstrand L. SHP-2 is involved in heterodimer specific loss of phosphorylation of Tyr771 in the PDGF beta-receptor. Oncogene 2002, 21:1870-1875.
    • (2002) Oncogene , vol.21 , pp. 1870-1875
    • Ekman, S.1    Kallin, A.2    Engstrom, U.3    Heldin, C.H.4    Ronnstrand, L.5
  • 96
    • 0035006109 scopus 로고    scopus 로고
    • Tyrosine-phosphorylated SOCS-3 inhibits STAT activation but binds to p120 RasGAP and activates Ras
    • Cacalano N.A., Sanden D., Johnston J.A. Tyrosine-phosphorylated SOCS-3 inhibits STAT activation but binds to p120 RasGAP and activates Ras. Nat Cell Biol 2001, 3:460-465.
    • (2001) Nat Cell Biol , vol.3 , pp. 460-465
    • Cacalano, N.A.1    Sanden, D.2    Johnston, J.A.3
  • 97
    • 63249103444 scopus 로고    scopus 로고
    • Negative and positive regulation of MAPK phosphatase 3 controls platelet-derived growth factor-induced Erk activation
    • Jurek A., Amagasaki K., Gembarska A., Heldin C.H., Lennartsson J. Negative and positive regulation of MAPK phosphatase 3 controls platelet-derived growth factor-induced Erk activation. J Biol Chem 2009, 284:4626-4634.
    • (2009) J Biol Chem , vol.284 , pp. 4626-4634
    • Jurek, A.1    Amagasaki, K.2    Gembarska, A.3    Heldin, C.H.4    Lennartsson, J.5
  • 98
    • 77949912964 scopus 로고    scopus 로고
    • Erk 5 is necessary for sustained PDGF-induced Akt phosphorylation and inhibition of apoptosis
    • Lennartsson J., Burovic F., Witek B., Jurek A., Heldin C.H. Erk 5 is necessary for sustained PDGF-induced Akt phosphorylation and inhibition of apoptosis. Cell Signal 2010, 22:955-960.
    • (2010) Cell Signal , vol.22 , pp. 955-960
    • Lennartsson, J.1    Burovic, F.2    Witek, B.3    Jurek, A.4    Heldin, C.H.5
  • 99
    • 33746818290 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase is necessary for platelet-derived growth factor-mediated chemotaxis in primary fibroblasts
    • Amagasaki K., Kaneto H., Heldin C.H., Lennartsson J. c-Jun N-terminal kinase is necessary for platelet-derived growth factor-mediated chemotaxis in primary fibroblasts. J Biol Chem 2006, 281:22173-22179.
    • (2006) J Biol Chem , vol.281 , pp. 22173-22179
    • Amagasaki, K.1    Kaneto, H.2    Heldin, C.H.3    Lennartsson, J.4
  • 100
    • 0033553558 scopus 로고    scopus 로고
    • Platelet-derived growth factor activates p38 mitogen-activated protein kinase through a Ras-dependent pathway that is important for actin reorganization and cell migration
    • Matsumoto T., Yokote K., Tamura K., Takemoto M., Ueno H., Saito Y., et al. Platelet-derived growth factor activates p38 mitogen-activated protein kinase through a Ras-dependent pathway that is important for actin reorganization and cell migration. J Biol Chem 1999, 274:13954-13960.
    • (1999) J Biol Chem , vol.274 , pp. 13954-13960
    • Matsumoto, T.1    Yokote, K.2    Tamura, K.3    Takemoto, M.4    Ueno, H.5    Saito, Y.6
  • 101
    • 5144226407 scopus 로고    scopus 로고
    • Platelet-derived growth factor-BB phosphorylates heat shock protein 27 in cardiac myocytes
    • Takenaka M., Matsuno H., Ishisaki A., Nakajima K., Hirade K., Takei M., et al. Platelet-derived growth factor-BB phosphorylates heat shock protein 27 in cardiac myocytes. J Cell Biochem 2004, 91:316-324.
    • (2004) J Cell Biochem , vol.91 , pp. 316-324
    • Takenaka, M.1    Matsuno, H.2    Ishisaki, A.3    Nakajima, K.4    Hirade, K.5    Takei, M.6
  • 102
    • 0032189249 scopus 로고    scopus 로고
    • Stress-activated protein kinases are negatively regulated by cell density
    • Lallemand D., Ham J., Garbay S., Bakiri L., Traincard F., Jeannequin O., et al. Stress-activated protein kinases are negatively regulated by cell density. EMBO J 1998, 17:5615-5626.
    • (1998) EMBO J , vol.17 , pp. 5615-5626
    • Lallemand, D.1    Ham, J.2    Garbay, S.3    Bakiri, L.4    Traincard, F.5    Jeannequin, O.6
  • 103
    • 0037625636 scopus 로고    scopus 로고
    • Role of JNK, p38, and ERK in platelet-derived growth factor-induced vascular proliferation, migration, and gene expression
    • Zhan Y., Kim S., Izumi Y., Izumiya Y., Nakao T., Miyazaki H., et al. Role of JNK, p38, and ERK in platelet-derived growth factor-induced vascular proliferation, migration, and gene expression. Arterioscler Thromb Vasc Biol 2003, 23:795-801.
    • (2003) Arterioscler Thromb Vasc Biol , vol.23 , pp. 795-801
    • Zhan, Y.1    Kim, S.2    Izumi, Y.3    Izumiya, Y.4    Nakao, T.5    Miyazaki, H.6
  • 104
    • 34248569784 scopus 로고    scopus 로고
    • Molecular mechanisms underlying FIP1L1-PDGFRA-mediated myeloproliferation
    • Buitenhuis M., Verhagen L.P., Cools J., Coffer P.J. Molecular mechanisms underlying FIP1L1-PDGFRA-mediated myeloproliferation. Cancer Res 2007, 67:3759-3766.
    • (2007) Cancer Res , vol.67 , pp. 3759-3766
    • Buitenhuis, M.1    Verhagen, L.P.2    Cools, J.3    Coffer, P.J.4
  • 105
    • 0033166851 scopus 로고    scopus 로고
    • The oncogenic TEL/PDGFR beta fusion protein induces cell death through JNK/SAPK pathway
    • Atfi A., Prunier C., Mazars A., Defachelles A.S., Cayre Y., Gespach C., et al. The oncogenic TEL/PDGFR beta fusion protein induces cell death through JNK/SAPK pathway. Oncogene 1999, 18:3878-3885.
    • (1999) Oncogene , vol.18 , pp. 3878-3885
    • Atfi, A.1    Prunier, C.2    Mazars, A.3    Defachelles, A.S.4    Cayre, Y.5    Gespach, C.6
  • 106
    • 0042388100 scopus 로고    scopus 로고
    • The coupling of TEL/PDGFbetaR to distinct functional responses is modulated by the presence of cytokine: involvement of mitogen-activated protein kinases
    • Wheadon H., Welham M.J. The coupling of TEL/PDGFbetaR to distinct functional responses is modulated by the presence of cytokine: involvement of mitogen-activated protein kinases. Blood 2003, 102:1480-1489.
    • (2003) Blood , vol.102 , pp. 1480-1489
    • Wheadon, H.1    Welham, M.J.2
  • 107
    • 37849002865 scopus 로고    scopus 로고
    • Big mitogen-activated protein kinase 1 (BMK1)/extracellular signal regulated kinase 5 (ERK5) is involved in platelet-derived growth factor (PDGF)-induced vascular smooth muscle cell migration
    • Izawa Y., Yoshizumi M., Ishizawa K., Fujita Y., Kondo S., Kagami S., et al. Big mitogen-activated protein kinase 1 (BMK1)/extracellular signal regulated kinase 5 (ERK5) is involved in platelet-derived growth factor (PDGF)-induced vascular smooth muscle cell migration. Hypertens Res 2007, 30:1107-1117.
    • (2007) Hypertens Res , vol.30 , pp. 1107-1117
    • Izawa, Y.1    Yoshizumi, M.2    Ishizawa, K.3    Fujita, Y.4    Kondo, S.5    Kagami, S.6
  • 108
    • 36549082913 scopus 로고    scopus 로고
    • ERK5 differentially regulates PDGF-induced proliferation and migration of hepatic stellate cells
    • Rovida E., Navari N., Caligiuri A., Dello Sbarba P., Marra F. ERK5 differentially regulates PDGF-induced proliferation and migration of hepatic stellate cells. J Hepatol 2008, 48:107-115.
    • (2008) J Hepatol , vol.48 , pp. 107-115
    • Rovida, E.1    Navari, N.2    Caligiuri, A.3    Dello Sbarba, P.4    Marra, F.5
  • 109
    • 84855598070 scopus 로고    scopus 로고
    • MKP3 negatively modulates PDGF-induced Akt and Erk5 phosphorylation as well as chemotaxis
    • Razmara M., Eger G., Rorsman C., Heldin C.H., Lennartsson J. MKP3 negatively modulates PDGF-induced Akt and Erk5 phosphorylation as well as chemotaxis. Cell Signal 2012, 24:635-640.
    • (2012) Cell Signal , vol.24 , pp. 635-640
    • Razmara, M.1    Eger, G.2    Rorsman, C.3    Heldin, C.H.4    Lennartsson, J.5
  • 110
    • 0034671968 scopus 로고    scopus 로고
    • Retention of PDGFR-beta function in mice in the absence of phosphatidylinositol 3'-kinase and phospholipase Cgamma signaling pathways
    • Tallquist M.D., Klinghoffer R.A., Heuchel R., Mueting-Nelsen P.F., Corrin P.D., Heldin C.H., et al. Retention of PDGFR-beta function in mice in the absence of phosphatidylinositol 3'-kinase and phospholipase Cgamma signaling pathways. Genes Dev 2000, 14:3179-3190.
    • (2000) Genes Dev , vol.14 , pp. 3179-3190
    • Tallquist, M.D.1    Klinghoffer, R.A.2    Heuchel, R.3    Mueting-Nelsen, P.F.4    Corrin, P.D.5    Heldin, C.H.6
  • 111
    • 0035937816 scopus 로고    scopus 로고
    • Phospholipase C-gamma1 is required for the induction of immediate early genes by platelet-derived growth factor
    • Liao H.J., Ji Q.S., Carpenter G. Phospholipase C-gamma1 is required for the induction of immediate early genes by platelet-derived growth factor. J Biol Chem 2001, 276:8627-8630.
    • (2001) J Biol Chem , vol.276 , pp. 8627-8630
    • Liao, H.J.1    Ji, Q.S.2    Carpenter, G.3
  • 112
    • 84892388139 scopus 로고    scopus 로고
    • The mitochondrial reactive oxygen species regulator p66Shc controls PDGF-induced signaling and migration through protein tyrosine phosphatase oxidation
    • Frijhoff J., Dagnell M., Augsten M., Beltrami E., Giorgio M., Ostman A. The mitochondrial reactive oxygen species regulator p66Shc controls PDGF-induced signaling and migration through protein tyrosine phosphatase oxidation. Free Radic Biol Med 2013, 68C:268-277.
    • (2013) Free Radic Biol Med , vol.68 C , pp. 268-277
    • Frijhoff, J.1    Dagnell, M.2    Augsten, M.3    Beltrami, E.4    Giorgio, M.5    Ostman, A.6
  • 113
    • 77957660973 scopus 로고    scopus 로고
    • 12/15-lipoxygenase-derived lipid peroxides control receptor tyrosine kinase signaling through oxidation of protein tyrosine phosphatases
    • Conrad M., Sandin A., Förster H., Seiler A., Frijhoff J., Dagnell M., et al. 12/15-lipoxygenase-derived lipid peroxides control receptor tyrosine kinase signaling through oxidation of protein tyrosine phosphatases. Proc Natl Acad Sci U S A 2010, 107:15774-15779.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 15774-15779
    • Conrad, M.1    Sandin, A.2    Förster, H.3    Seiler, A.4    Frijhoff, J.5    Dagnell, M.6
  • 114
    • 19644394554 scopus 로고    scopus 로고
    • Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II
    • Choi M.H., Lee I.K., Kim G.W., Kim B.U., Han Y.H., Yu D.Y., et al. Regulation of PDGF signalling and vascular remodelling by peroxiredoxin II. Nature 2005, 435:347-353.
    • (2005) Nature , vol.435 , pp. 347-353
    • Choi, M.H.1    Lee, I.K.2    Kim, G.W.3    Kim, B.U.4    Han, Y.H.5    Yu, D.Y.6
  • 115
    • 84882324544 scopus 로고    scopus 로고
    • Selective activation of oxidized PTP1B by the thioredoxin system modulates PDGF-β receptor tyrosine kinase signaling
    • Dagnell M., Frijhoff J., Pader I., Augsten M., Boivin B., Xu J., et al. Selective activation of oxidized PTP1B by the thioredoxin system modulates PDGF-β receptor tyrosine kinase signaling. Proc Natl Acad Sci U S A 2013, 110:13398-13403.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 13398-13403
    • Dagnell, M.1    Frijhoff, J.2    Pader, I.3    Augsten, M.4    Boivin, B.5    Xu, J.6
  • 116
    • 0032576873 scopus 로고    scopus 로고
    • Activation of Stat5 by platelet-derived growth factor (PDGF) is dependent on phosphorylation sites in PDGF beta-receptor juxtamembrane and kinase insert domains
    • Valgeirsdottir S., Paukku K., Silvennoinen O., Heldin C.H., Claesson-Welsh L. Activation of Stat5 by platelet-derived growth factor (PDGF) is dependent on phosphorylation sites in PDGF beta-receptor juxtamembrane and kinase insert domains. Oncogene 1998, 16:505-515.
    • (1998) Oncogene , vol.16 , pp. 505-515
    • Valgeirsdottir, S.1    Paukku, K.2    Silvennoinen, O.3    Heldin, C.H.4    Claesson-Welsh, L.5
  • 117
    • 0034141352 scopus 로고    scopus 로고
    • Platelet-derived growth factor (PDGF)-induced activation of signal transducer and activator of transcription (Stat) 5 is mediated by PDGF beta-receptor and is not dependent on c-src, fyn, jak1 or jak2 kinases
    • Paukku K., Valgeirsdottir S., Saharinen P., Bergman M., Heldin C.H., Silvennoinen O. Platelet-derived growth factor (PDGF)-induced activation of signal transducer and activator of transcription (Stat) 5 is mediated by PDGF beta-receptor and is not dependent on c-src, fyn, jak1 or jak2 kinases. Biochem J 2000, 345:759-766.
    • (2000) Biochem J , vol.345 , pp. 759-766
    • Paukku, K.1    Valgeirsdottir, S.2    Saharinen, P.3    Bergman, M.4    Heldin, C.H.5    Silvennoinen, O.6
  • 118
    • 0029966664 scopus 로고    scopus 로고
    • Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins
    • Vignais M.L., Sadowski H.B., Watling D., Rogers N.C., Gilman M. Platelet-derived growth factor induces phosphorylation of multiple JAK family kinases and STAT proteins. Mol Cell Biol 1996, 16:1759-1769.
    • (1996) Mol Cell Biol , vol.16 , pp. 1759-1769
    • Vignais, M.L.1    Sadowski, H.B.2    Watling, D.3    Rogers, N.C.4    Gilman, M.5
  • 119
    • 0033518113 scopus 로고    scopus 로고
    • Consequences of Stat6 deletion on Sis/PDGF- and IL-4-induced proliferation and transcriptional activation in murine fibroblasts
    • Kriebel P., Patel B.K., Nelson S.A., Grusby M.J., LaRochelle W.J. Consequences of Stat6 deletion on Sis/PDGF- and IL-4-induced proliferation and transcriptional activation in murine fibroblasts. Oncogene 1999, 18:7294-7302.
    • (1999) Oncogene , vol.18 , pp. 7294-7302
    • Kriebel, P.1    Patel, B.K.2    Nelson, S.A.3    Grusby, M.J.4    LaRochelle, W.J.5
  • 120
    • 80053619351 scopus 로고    scopus 로고
    • Multiple oligomerization domains of KANK1-PDGFRB are required for JAK2-independent hematopoietic cell proliferation and signaling via STAT5 and ERK
    • Medves S., Noel L.A., Montano-Almendras C.P., Albu R.I., Schoemans H., Constantinescu S.N., et al. Multiple oligomerization domains of KANK1-PDGFRB are required for JAK2-independent hematopoietic cell proliferation and signaling via STAT5 and ERK. Haematologica 2011, 96:1406-1414.
    • (2011) Haematologica , vol.96 , pp. 1406-1414
    • Medves, S.1    Noel, L.A.2    Montano-Almendras, C.P.3    Albu, R.I.4    Schoemans, H.5    Constantinescu, S.N.6
  • 121
    • 0029785080 scopus 로고    scopus 로고
    • A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9
    • Demoulin J.B., Uyttenhove C., Van Roost E., de Lestre B., Donckers D., Van Snick J., et al. A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9. Mol Cell Biol 1996, 16:4710-4716.
    • (1996) Mol Cell Biol , vol.16 , pp. 4710-4716
    • Demoulin, J.B.1    Uyttenhove, C.2    Van Roost, E.3    de Lestre, B.4    Donckers, D.5    Van Snick, J.6
  • 122
    • 0034690026 scopus 로고    scopus 로고
    • Activation of Stat3 preassembled with platelet-derived growth factor beta receptors requires Src kinase activity
    • Wang Y.Z., Wharton W., Garcia R., Kraker A., Jove R., Pledger W.J. Activation of Stat3 preassembled with platelet-derived growth factor beta receptors requires Src kinase activity. Oncogene 2000, 19:2075-2085.
    • (2000) Oncogene , vol.19 , pp. 2075-2085
    • Wang, Y.Z.1    Wharton, W.2    Garcia, R.3    Kraker, A.4    Jove, R.5    Pledger, W.J.6
  • 123
    • 21044433457 scopus 로고    scopus 로고
    • Activation of JAK-STAT pathway is required for platelet-derived growth factor-induced proliferation of pancreatic stellate cells
    • Masamune A., Satoh M., Kikuta K., Suzuki N., Shimosegawa T. Activation of JAK-STAT pathway is required for platelet-derived growth factor-induced proliferation of pancreatic stellate cells. World J Gastroenterol 2005, 11:3385-3391.
    • (2005) World J Gastroenterol , vol.11 , pp. 3385-3391
    • Masamune, A.1    Satoh, M.2    Kikuta, K.3    Suzuki, N.4    Shimosegawa, T.5
  • 124
    • 8544253276 scopus 로고    scopus 로고
    • An essential role of the Jak-2/STAT-3/cytosolic phospholipase A(2) axis in platelet-derived growth factor BB-induced vascular smooth muscle cell motility
    • Neeli I., Liu Z., Dronadula N., Ma Z.A., Rao G.N. An essential role of the Jak-2/STAT-3/cytosolic phospholipase A(2) axis in platelet-derived growth factor BB-induced vascular smooth muscle cell motility. J Biol Chem 2004, 279:46122-46128.
    • (2004) J Biol Chem , vol.279 , pp. 46122-46128
    • Neeli, I.1    Liu, Z.2    Dronadula, N.3    Ma, Z.A.4    Rao, G.N.5
  • 125
    • 0032933625 scopus 로고    scopus 로고
    • Distinct mechanisms of activation of Stat1 and Stat3 by platelet-derived growth factor receptor in a cell-free system
    • Vignais M.L., Gilman M. Distinct mechanisms of activation of Stat1 and Stat3 by platelet-derived growth factor receptor in a cell-free system. Mol Cell Biol 1999, 19:3727-3735.
    • (1999) Mol Cell Biol , vol.19 , pp. 3727-3735
    • Vignais, M.L.1    Gilman, M.2
  • 126
    • 0038322002 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 is an effector of Jak/STAT signaling and is involved in platelet-derived growth factor BB-induced growth in vascular smooth muscle cells
    • Yellaturu C.R., Rao G.N. Cytosolic phospholipase A2 is an effector of Jak/STAT signaling and is involved in platelet-derived growth factor BB-induced growth in vascular smooth muscle cells. J Biol Chem 2003, 278:9986-9992.
    • (2003) J Biol Chem , vol.278 , pp. 9986-9992
    • Yellaturu, C.R.1    Rao, G.N.2
  • 127
    • 13344282731 scopus 로고    scopus 로고
    • Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway
    • Meraz M.A., White J.M., Sheehan K.C., Bach E.A., Rodig S.J., Dighe A.S., et al. Targeted disruption of the Stat1 gene in mice reveals unexpected physiologic specificity in the JAK-STAT signaling pathway. Cell 1996, 84:431-442.
    • (1996) Cell , vol.84 , pp. 431-442
    • Meraz, M.A.1    White, J.M.2    Sheehan, K.C.3    Bach, E.A.4    Rodig, S.J.5    Dighe, A.S.6
  • 128
    • 0033520477 scopus 로고    scopus 로고
    • Distinct roles for STAT1, STAT3, and STAT5 in differentiation gene induction and apoptosis inhibition by interleukin-9
    • Demoulin J.B., Van Roost E., Stevens M., Groner B., Renauld J.C. Distinct roles for STAT1, STAT3, and STAT5 in differentiation gene induction and apoptosis inhibition by interleukin-9. J Biol Chem 1999, 274:25855-25861.
    • (1999) J Biol Chem , vol.274 , pp. 25855-25861
    • Demoulin, J.B.1    Van Roost, E.2    Stevens, M.3    Groner, B.4    Renauld, J.C.5
  • 129
    • 77954364953 scopus 로고    scopus 로고
    • Transcription factor regulation can be accurately predicted from the presence of target gene signatures in microarray gene expression data
    • Essaghir A., Toffalini F., Knoops L., Kallin A., van Helden J., Demoulin J.B. Transcription factor regulation can be accurately predicted from the presence of target gene signatures in microarray gene expression data. Nucleic Acids Res 2010, 38:e120.
    • (2010) Nucleic Acids Res , vol.38
    • Essaghir, A.1    Toffalini, F.2    Knoops, L.3    Kallin, A.4    van Helden, J.5    Demoulin, J.B.6
  • 130
    • 77954645108 scopus 로고    scopus 로고
    • The interferon-gamma-induced murine guanylate-binding protein-2 inhibits rac activation during cell spreading on fibronectin and after platelet-derived growth factor treatment: role for phosphatidylinositol 3-kinase
    • Messmer-Blust A.F., Balasubramanian S., Gorbacheva V.Y., Jeyaratnam J.A., Vestal D.J. The interferon-gamma-induced murine guanylate-binding protein-2 inhibits rac activation during cell spreading on fibronectin and after platelet-derived growth factor treatment: role for phosphatidylinositol 3-kinase. Mol Biol Cell 2010, 21:2514-2528.
    • (2010) Mol Biol Cell , vol.21 , pp. 2514-2528
    • Messmer-Blust, A.F.1    Balasubramanian, S.2    Gorbacheva, V.Y.3    Jeyaratnam, J.A.4    Vestal, D.J.5
  • 131
    • 0034677195 scopus 로고    scopus 로고
    • Regulation of c-myc expression by IFN-gamma through Stat1-dependent and -independent pathways
    • Ramana C.V., Grammatikakis N., Chernov M., Nguyen H., Goh K.C., Williams B.R., et al. Regulation of c-myc expression by IFN-gamma through Stat1-dependent and -independent pathways. EMBO J 2000, 19:263-272.
    • (2000) EMBO J , vol.19 , pp. 263-272
    • Ramana, C.V.1    Grammatikakis, N.2    Chernov, M.3    Nguyen, H.4    Goh, K.C.5    Williams, B.R.6
  • 133
    • 77952002497 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein 1 (LRP1) forms a signaling complex with platelet-derived growth factor receptor-beta in endosomes and regulates activation of the MAPK pathway
    • Muratoglu S.C., Mikhailenko I., Newton C., Migliorini M., Strickland D.K. Low density lipoprotein receptor-related protein 1 (LRP1) forms a signaling complex with platelet-derived growth factor receptor-beta in endosomes and regulates activation of the MAPK pathway. J Biol Chem 2010, 285:14308-14317.
    • (2010) J Biol Chem , vol.285 , pp. 14308-14317
    • Muratoglu, S.C.1    Mikhailenko, I.2    Newton, C.3    Migliorini, M.4    Strickland, D.K.5
  • 134
    • 33845999302 scopus 로고    scopus 로고
    • Alix facilitates the interaction between c-Cbl and platelet-derived growth factor beta-receptor and thereby modulates receptor down-regulation
    • Lennartsson J., Wardega P., Engstrom U., Hellman U., Heldin C.H. Alix facilitates the interaction between c-Cbl and platelet-derived growth factor beta-receptor and thereby modulates receptor down-regulation. J Biol Chem 2006, 281:39152-39158.
    • (2006) J Biol Chem , vol.281 , pp. 39152-39158
    • Lennartsson, J.1    Wardega, P.2    Engstrom, U.3    Hellman, U.4    Heldin, C.H.5
  • 135
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro C.A., Wing S.S., Huang H., Leverson J.D., Hunter T., Liu Y.C. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 1999, 286:309-312.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 136
    • 1542289711 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor-mediated signal transduction from endosomes
    • Wang Y., Pennock S.D., Chen X., Kazlauskas A., Wang Z. Platelet-derived growth factor receptor-mediated signal transduction from endosomes. J Biol Chem 2004, 279:8038-8046.
    • (2004) J Biol Chem , vol.279 , pp. 8038-8046
    • Wang, Y.1    Pennock, S.D.2    Chen, X.3    Kazlauskas, A.4    Wang, Z.5
  • 138
    • 84879987829 scopus 로고    scopus 로고
    • AKT facilitates EGFR trafficking and degradation by phosphorylating and activating PIKfyve
    • Er E.E., Mendoza M.C., Mackey A.M., Rameh L.E., Blenis J. AKT facilitates EGFR trafficking and degradation by phosphorylating and activating PIKfyve. Sci Signal 2013, 6:ra45.
    • (2013) Sci Signal , vol.6
    • Er, E.E.1    Mendoza, M.C.2    Mackey, A.M.3    Rameh, L.E.4    Blenis, J.5
  • 139
    • 67449116833 scopus 로고    scopus 로고
    • Activation of protein kinase C alpha is necessary for sorting the PDGF beta-receptor to Rab4a-dependent recycling
    • Hellberg C., Schmees C., Karlsson S., Ahgren A., Heldin C.H. Activation of protein kinase C alpha is necessary for sorting the PDGF beta-receptor to Rab4a-dependent recycling. Mol Biol Cell 2009, 20:2856-2863.
    • (2009) Mol Biol Cell , vol.20 , pp. 2856-2863
    • Hellberg, C.1    Schmees, C.2    Karlsson, S.3    Ahgren, A.4    Heldin, C.H.5
  • 140
    • 68049126290 scopus 로고    scopus 로고
    • The fusion proteins TEL-PDGFRbeta and FIP1L1-PDGFRalpha escape ubiquitination and degradation
    • Toffalini F., Kallin A., Vandenberghe P., Pierre P., Michaux L., Cools J., et al. The fusion proteins TEL-PDGFRbeta and FIP1L1-PDGFRalpha escape ubiquitination and degradation. Haematologica 2009, 94:1085-1093.
    • (2009) Haematologica , vol.94 , pp. 1085-1093
    • Toffalini, F.1    Kallin, A.2    Vandenberghe, P.3    Pierre, P.4    Michaux, L.5    Cools, J.6
  • 141
    • 77951216988 scopus 로고    scopus 로고
    • Critical role of the platelet-derived growth factor receptor (PDGFR)-beta transmembrane domain in the TEL-PDGFRbeta cytosolic oncoprotein
    • Toffalini F., Hellberg C., Demoulin J.B. Critical role of the platelet-derived growth factor receptor (PDGFR)-beta transmembrane domain in the TEL-PDGFRbeta cytosolic oncoprotein. J Biol Chem 2010, 285:12268-12278.
    • (2010) J Biol Chem , vol.285 , pp. 12268-12278
    • Toffalini, F.1    Hellberg, C.2    Demoulin, J.B.3
  • 142
    • 0037421971 scopus 로고    scopus 로고
    • A human brain tumor-derived PDGFR-alpha deletion mutant is transforming
    • Clarke I.D., Dirks P.B. A human brain tumor-derived PDGFR-alpha deletion mutant is transforming. Oncogene 2003, 22:722-733.
    • (2003) Oncogene , vol.22 , pp. 722-733
    • Clarke, I.D.1    Dirks, P.B.2
  • 143
    • 84893249799 scopus 로고    scopus 로고
    • PI3K and cancer: lessons, challenges and opportunities
    • Fruman D.A., Rommel C. PI3K and cancer: lessons, challenges and opportunities. Nat Rev Drug Discov 2014, 13:140-156.
    • (2014) Nat Rev Drug Discov , vol.13 , pp. 140-156
    • Fruman, D.A.1    Rommel, C.2
  • 144
    • 38149075090 scopus 로고    scopus 로고
    • Dermatofibrosarcoma protuberans COL1A1-PDGFB fusion is identified in virtually all dermatofibrosarcoma protuberans cases when investigated by newly developed multiplex reverse transcription polymerase chain reaction and fluorescence in situ hybridization assays
    • Patel K.U., Szabo S.S., Hernandez V.S., Prieto V.G., Abruzzo L.V., Lazar A.J., et al. Dermatofibrosarcoma protuberans COL1A1-PDGFB fusion is identified in virtually all dermatofibrosarcoma protuberans cases when investigated by newly developed multiplex reverse transcription polymerase chain reaction and fluorescence in situ hybridization assays. Hum Pathol 2008, 39:184-193.
    • (2008) Hum Pathol , vol.39 , pp. 184-193
    • Patel, K.U.1    Szabo, S.S.2    Hernandez, V.S.3    Prieto, V.G.4    Abruzzo, L.V.5    Lazar, A.J.6
  • 145
    • 84902089183 scopus 로고    scopus 로고
    • Neo-adjuvant imatinib in advanced primary or locally recurrent dermatofibrosarcoma protuberans: a multicenter phase-II DeCOG trial with long-term follow-up
    • Ugurel S., Mentzel T., Utikal J., Helmbold P., Mohr P., Pfohler C., et al. Neo-adjuvant imatinib in advanced primary or locally recurrent dermatofibrosarcoma protuberans: a multicenter phase-II DeCOG trial with long-term follow-up. Clin Cancer Res 2013.
    • (2013) Clin Cancer Res
    • Ugurel, S.1    Mentzel, T.2    Utikal, J.3    Helmbold, P.4    Mohr, P.5    Pfohler, C.6
  • 146
    • 33845991464 scopus 로고    scopus 로고
    • Durable responses to imatinib in patients with PDGFRB fusion gene-positive and BCR-ABL-negative chronic myeloproliferative disorders
    • David M., Cross N.C., Burgstaller S., Chase A., Curtis C., Dang R., et al. Durable responses to imatinib in patients with PDGFRB fusion gene-positive and BCR-ABL-negative chronic myeloproliferative disorders. Blood 2007, 109:61-64.
    • (2007) Blood , vol.109 , pp. 61-64
    • David, M.1    Cross, N.C.2    Burgstaller, S.3    Chase, A.4    Curtis, C.5    Dang, R.6
  • 147
    • 55949102355 scopus 로고    scopus 로고
    • Safety and efficacy of imatinib in chronic eosinophilic leukaemia and hypereosinophilic syndrome: a phase-II study
    • Metzgeroth G., Walz C., Erben P., Popp H., Schmitt-Graeff A., Haferlach C., et al. Safety and efficacy of imatinib in chronic eosinophilic leukaemia and hypereosinophilic syndrome: a phase-II study. Br J Haematol 2008, 143:707-715.
    • (2008) Br J Haematol , vol.143 , pp. 707-715
    • Metzgeroth, G.1    Walz, C.2    Erben, P.3    Popp, H.4    Schmitt-Graeff, A.5    Haferlach, C.6
  • 148
    • 77952429900 scopus 로고    scopus 로고
    • KANK1, a candidate tumor suppressor gene, is fused to PDGFRB in an imatinib-responsive myeloid neoplasm with severe thrombocythemia
    • Medves S., Duhoux F.P., Ferrant A., Toffalini F., Ameye G., Libouton J.M., et al. KANK1, a candidate tumor suppressor gene, is fused to PDGFRB in an imatinib-responsive myeloid neoplasm with severe thrombocythemia. Leukemia 2010, 24:1052-1055.
    • (2010) Leukemia , vol.24 , pp. 1052-1055
    • Medves, S.1    Duhoux, F.P.2    Ferrant, A.3    Toffalini, F.4    Ameye, G.5    Libouton, J.M.6
  • 149
    • 84888409115 scopus 로고    scopus 로고
    • Effect of the tyrosine kinase inhibitor nilotinib in patients with hypereosinophilic syndrome/chronic eosinophilic leukemia: analysis of the phase 2, open-label, single-arm A2101 study
    • Hochhaus A., le Coutre P.D., Kantarjian H.M., Baccarani M., Erben P., Reiter A., et al. Effect of the tyrosine kinase inhibitor nilotinib in patients with hypereosinophilic syndrome/chronic eosinophilic leukemia: analysis of the phase 2, open-label, single-arm A2101 study. J Cancer Res Clin Oncol 2013, 139:1985-1993.
    • (2013) J Cancer Res Clin Oncol , vol.139 , pp. 1985-1993
    • Hochhaus, A.1    le Coutre, P.D.2    Kantarjian, H.M.3    Baccarani, M.4    Erben, P.5    Reiter, A.6
  • 150
    • 79953091929 scopus 로고    scopus 로고
    • Novel imatinib-sensitive PDGFRA-activating point mutations in hypereosinophilic syndrome induce growth factor independence and leukemia-like disease
    • Elling C., Erben P., Walz C., Frickenhaus M., Schemionek M., Stehling M., et al. Novel imatinib-sensitive PDGFRA-activating point mutations in hypereosinophilic syndrome induce growth factor independence and leukemia-like disease. Blood 2011, 117:2935-2943.
    • (2011) Blood , vol.117 , pp. 2935-2943
    • Elling, C.1    Erben, P.2    Walz, C.3    Frickenhaus, M.4    Schemionek, M.5    Stehling, M.6
  • 151
    • 84894041669 scopus 로고    scopus 로고
    • Mutation of NRAS but not KRAS significantly reduces myeloma sensitivity to single-agent bortezomib therapy
    • Mulligan G., Lichter D.I., Di Bacco A., Blakemore S.J., Berger A., Koenig E., et al. Mutation of NRAS but not KRAS significantly reduces myeloma sensitivity to single-agent bortezomib therapy. Blood 2014, 123:632-639.
    • (2014) Blood , vol.123 , pp. 632-639
    • Mulligan, G.1    Lichter, D.I.2    Di Bacco, A.3    Blakemore, S.J.4    Berger, A.5    Koenig, E.6
  • 152
    • 23944476156 scopus 로고    scopus 로고
    • PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib
    • Corless C.L., Schroeder A., Griffith D., Town A., McGreevey L., Harrell P., et al. PDGFRA mutations in gastrointestinal stromal tumors: frequency, spectrum and in vitro sensitivity to imatinib. J Clin Oncol 2005, 23:5357-5364.
    • (2005) J Clin Oncol , vol.23 , pp. 5357-5364
    • Corless, C.L.1    Schroeder, A.2    Griffith, D.3    Town, A.4    McGreevey, L.5    Harrell, P.6
  • 153
    • 0347361543 scopus 로고    scopus 로고
    • PDGFRA germline mutation in a family with multiple cases of gastrointestinal stromal tumor
    • Chompret A., Kannengiesser C., Barrois M., Terrier P., Dahan P., Tursz T., et al. PDGFRA germline mutation in a family with multiple cases of gastrointestinal stromal tumor. Gastroenterology 2004, 126:318-321.
    • (2004) Gastroenterology , vol.126 , pp. 318-321
    • Chompret, A.1    Kannengiesser, C.2    Barrois, M.3    Terrier, P.4    Dahan, P.5    Tursz, T.6
  • 154
    • 84862873559 scopus 로고    scopus 로고
    • Activating PDGFRA mutations in inflammatory fibroid polyps occur in exons 12, 14 and 18 and are associated with tumour localization
    • Huss S., Wardelmann E., Goltz D., Binot E., Hartmann W., Merkelbach-Bruse S., et al. Activating PDGFRA mutations in inflammatory fibroid polyps occur in exons 12, 14 and 18 and are associated with tumour localization. Histopathology 2012, 61:59-68.
    • (2012) Histopathology , vol.61 , pp. 59-68
    • Huss, S.1    Wardelmann, E.2    Goltz, D.3    Binot, E.4    Hartmann, W.5    Merkelbach-Bruse, S.6
  • 155
    • 84890603543 scopus 로고    scopus 로고
    • Large-scale analysis of PDGFRA mutations in melanomas and evaluation of their sensitivity to tyrosine kinase inhibitors imatinib and crenolanib
    • Dai J., Kong Y., Si L., Chi Z., Cui C., Sheng X., et al. Large-scale analysis of PDGFRA mutations in melanomas and evaluation of their sensitivity to tyrosine kinase inhibitors imatinib and crenolanib. Clin Cancer Res 2013, 19:6935-6942.
    • (2013) Clin Cancer Res , vol.19 , pp. 6935-6942
    • Dai, J.1    Kong, Y.2    Si, L.3    Chi, Z.4    Cui, C.5    Sheng, X.6
  • 156
    • 84886028950 scopus 로고    scopus 로고
    • Novel oncogenic PDGFRA mutations in pediatric high-grade gliomas
    • Paugh B.S., Zhu X., Qu C., Endersby R., Diaz A.K., Zhang J., et al. Novel oncogenic PDGFRA mutations in pediatric high-grade gliomas. Cancer Res 2013, 73:6219-6229.
    • (2013) Cancer Res , vol.73 , pp. 6219-6229
    • Paugh, B.S.1    Zhu, X.2    Qu, C.3    Endersby, R.4    Diaz, A.K.5    Zhang, J.6
  • 157
    • 73649123907 scopus 로고    scopus 로고
    • Integrated genomic analysis identifies clinically relevant subtypes of glioblastoma characterized by abnormalities in PDGFRA, IDH1, EGFR, and NF1
    • Verhaak R.G., Hoadley K.A., Purdom E., Wang V., Qi Y., Wilkerson M.D., et al. Integrated genomic analysis identifies clinically relevant subtypes of glioblastoma characterized by abnormalities in PDGFRA, IDH1, EGFR, and NF1. Cancer Cell 2010, 17:98-110.
    • (2010) Cancer Cell , vol.17 , pp. 98-110
    • Verhaak, R.G.1    Hoadley, K.A.2    Purdom, E.3    Wang, V.4    Qi, Y.5    Wilkerson, M.D.6
  • 158
    • 77957667714 scopus 로고    scopus 로고
    • PDGFRA gene rearrangements are frequent genetic events in PDGFRA-amplified glioblastomas
    • Ozawa T., Brennan C.W., Wang L., Squatrito M., Sasayama T., Nakada M., et al. PDGFRA gene rearrangements are frequent genetic events in PDGFRA-amplified glioblastomas. Genes Dev 2010, 24:2205-2218.
    • (2010) Genes Dev , vol.24 , pp. 2205-2218
    • Ozawa, T.1    Brennan, C.W.2    Wang, L.3    Squatrito, M.4    Sasayama, T.5    Nakada, M.6


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