메뉴 건너뛰기




Volumn 52, Issue 17, 1992, Pages 4773-4778

Characterization of Protein Tyrosine Kinases from Human Breast Cancer: Involvement of the c-src Oncogene Product

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; PROTEIN TYROSINE KINASE;

EID: 0026674221     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (319)

References (45)
  • 1
    • 37049183697 scopus 로고
    • Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene
    • Slamon, D. J., Clark, G. M., Wong, S. G., Levin, W. J., Ullrich, A., and McGuire, W. L. Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science (Washington DC), 235: 177-182, 1987.
    • (1987) Science (Washington DC) , vol.235 , pp. 177-182
    • Slamon, D.J.1    Clark, G.M.2    Wong, S.G.3    Levin, W.J.4    Ullrich, A.5    McGuire, W.L.6
  • 3
    • 0024217774 scopus 로고
    • Lack of evidence for the prognostic significance of c-erbB-1 amplification in human breast carcinoma
    • Ali, I. U., Campbell, G., Lidereau, R., and Callahan, R. Lack of evidence for the prognostic significance of c-erbB-1 amplification in human breast carcinoma. Oncol. Res., i: 139-146, 1988.
    • (1988) Oncol. Res. , vol.1 , pp. 139-146
    • Ali, I.U.1    Campbell, G.2    Lidereau, R.3    Callahan, R.4
  • 4
    • 0023952496 scopus 로고
    • Amplification of c-erbB-2 and aggressive human breast tumors?
    • Ali, I. U., Campbell, G., Lidereau, R., and Callahan, R. Amplification of c-erbB-2 and aggressive human breast tumors? Science (Washington DC), 240: 1795-1796, 1988.
    • (1988) Science (Washington DC) , vol.240 , pp. 1795-1796
    • Ali, I.U.1    Campbell, G.2    Lidereau, R.3    Callahan, R.4
  • 5
    • 0023124598 scopus 로고
    • Amplification of the neu (c-erbB-2) oncogene in human mammary tumors is relatively frequent and is often accompanied by amplification of the linked c-erbA oncogene
    • Van de Vijver, M. J., Van de Bersselaar, R., Devilee, P., Cornelisse, C., Peterse, J., and Nusse, R. Amplification of the neu (c-erbB-2) oncogene in human mammary tumors is relatively frequent and is often accompanied by amplification of the linked c-erbA oncogene. Mol. Cell. Biol., 7: 2019-2023, 1987.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2019-2023
    • Van de Vijver, M.J.1    Van de Bersselaar, R.2    Devilee, P.3    Cornelisse, C.4    Peterse, J.5    Nusse, R.6
  • 7
    • 0024259860 scopus 로고
    • Overexpression of either c-myc or c-erbB-2/neu proto-oncogenes in human breast carcinomas: correlation with poor prognosis
    • Guerin, M., Barrois, M., Terrier, M. J., Spielmann, M., and Riou, G. Overexpression of either c-myc or c-erbB-2/neu proto-oncogenes in human breast carcinomas: correlation with poor prognosis. Oncol. Res., i; 21-31, 1988.
    • (1988) Oncol. Res. , vol.1 , pp. 21-31
    • Guerin, M.1    Barrois, M.2    Terrier, M.J.3    Spielmann, M.4    Riou, G.5
  • 10
    • 0021911679 scopus 로고
    • Epidermal growth factor receptors and oestrogen receptors in human breast cancer
    • Sainsbury, J. R. C., Sherbet, G. V., Famdon, J. R., and Harris, A. L. Epidermal growth factor receptors and oestrogen receptors in human breast cancer. Lancet, 2: 364-366, 1985.
    • (1985) Lancet , vol.2 , pp. 364-366
    • Sainsbury, J.R.C.1    Sherbet, G.V.2    Famdon, J.R.3    Harris, A.L.4
  • 12
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A., and Schlessinger, J. Signal transduction by receptors with tyrosine kinase activity. Cell, 61: 203-212, 1990.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 13
    • 0024425432 scopus 로고
    • Oncogenes, growth factors, and signal transduction
    • Druker, B. J., Mamon, H. J., and Roberts, T. M. Oncogenes, growth factors, and signal transduction. N. Engl. J. Med., 321: 1383-1391, 1989.
    • (1989) N. Engl. J. Med. , vol.321 , pp. 1383-1391
    • Druker, B.J.1    Mamon, H.J.2    Roberts, T.M.3
  • 14
    • 0024447087 scopus 로고
    • Growth factors as transforming proteins
    • Heldin, C-H., and Westermark, B. Growth factors as transforming proteins. Eur. J. Biochem., 184:487-496, 1989.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 487-496
    • Heldin, C.-H.1    Westermark, B.2
  • 15
    • 0024546195 scopus 로고
    • Tyrosine kinase activity in breast cancer, benign breast disease, and normal breast tissue
    • Hennipman, A., van Oirschot, B. A., Smits, J., Rijksen, G., and Staal, G. E. J. Tyrosine kinase activity in breast cancer, benign breast disease, and normal breast tissue. Cancer Res., 49: 516-521, 1989.
    • (1989) Cancer Res. , vol.49 , pp. 516-521
    • Hennipman, A.1    van Oirschot, B.A.2    Smits, J.3    Rijksen, G.4    Staal, G.E.J.5
  • 16
    • 0022646559 scopus 로고
    • Metabolic comparison between basophils and other leukocytes from human blood
    • De Boer, M., and Roos, D. Metabolic comparison between basophils and other leukocytes from human blood. J. Immunol., 136: 3447-3454, 1986.
    • (1986) J. Immunol. , vol.136 , pp. 3447-3454
    • De Boer, M.1    Roos, D.2
  • 17
    • 0026317853 scopus 로고
    • Nonradioactive assays of protein-tyrosine kinase activity using anti-phosphotyrosine antibodies
    • Rijksen, G., van Oirschot, B. A., and Staal, G. E. J. Nonradioactive assays of protein-tyrosine kinase activity using anti-phosphotyrosine antibodies. Methods Enzymol., 200: 98-107, 1991.
    • (1991) Methods Enzymol. , vol.200 , pp. 98-107
    • Rijksen, G.1    van Oirschot, B.A.2    Staal, G.E.J.3
  • 19
    • 0026008039 scopus 로고
    • Description of an enzyme-linked immunosorbent assay for the detection of protein tyrosine kinase
    • Lazaro, L., Gonzalez, M., Roy, G., Villar, L. M., and Gonzalez-Porque, P. Description of an enzyme-linked immunosorbent assay for the detection of protein tyrosine kinase. Anal. Biochem., 192: 257-261, 1991.
    • (1991) Anal. Biochem. , vol.192 , pp. 257-261
    • Lazaro, L.1    Gonzalez, M.2    Roy, G.3    Villar, L.M.4    Gonzalez-Porque, P.5
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227:680-685, 1970.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0020501846 scopus 로고
    • Isolation of Monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses
    • Lipsich, L. A., Lewis, A. J., and Brugge, J. S. Isolation of Monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol., 48: 352-360, 1983.
    • (1983) J. Virol. , vol.48 , pp. 352-360
    • Lipsich, L.A.1    Lewis, A.J.2    Brugge, J.S.3
  • 23
    • 0025775939 scopus 로고
    • Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets
    • Huang, M-M., Bolen, J. B., Barnwell, J. W., Shattil, S. J., and Brugge, J. S. Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets. Proc. Natl. Acad. Sci. USA, 88: 7844-7848, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7844-7848
    • Huang, M.-M.1    Bolen, J.B.2    Barnwell, J.W.3    Shattil, S.J.4    Brugge, J.S.5
  • 24
    • 0019304427 scopus 로고
    • The protein encoded by the transforming gene of avian sarcoma virus (pp60c-src) and a homologous protein in normal cells (pp60c-src) are associated with the plasma membrane
    • Courtneidge, S. A., Levinson, A. D., and Bishop, J. M. The protein encoded by the transforming gene of avian sarcoma virus (pp60c-src) and a homologous protein in normal cells (pp60c-src) are associated with the plasma membrane. Proc. Natl. Acad. Sci. USA, 77: 3783-3787, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3783-3787
    • Courtneidge, S.A.1    Levinson, A.D.2    Bishop, J.M.3
  • 25
    • 0018906822 scopus 로고
    • Evidence that the src gene product of Rous sarcoma virus is membrane associated
    • Krueger, J. G., Wang, E., and Goldberg, A. R. Evidence that the src gene product of Rous sarcoma virus is membrane associated. Virology, 101: 25-40, 1980.
    • (1980) Virology , vol.101 , pp. 25-40
    • Krueger, J.G.1    Wang, E.2    Goldberg, A.R.3
  • 26
    • 0345692404 scopus 로고
    • Fine structural mapping of a critical NH2-terminal region of p60c-src
    • Pellman, D., Garber, E. A., Cross, F. R., and Hanafusa, H. Fine structural mapping of a critical NH2-terminal region of p60c-src. Proc. Natl. Acad. Sci. USA, 82: 1623-1627, 1985.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1623-1627
    • Pellman, D.1    Garber, E.A.2    Cross, F.R.3    Hanafusa, H.4
  • 27
    • 0021670592 scopus 로고
    • Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein
    • Buss, J. E., Kamps, M. P., and Sefton, B. M. Myristic acid is attached to the transforming protein of Rous sarcoma virus during or immediately after synthesis and is present in both soluble and membrane-bound forms of the protein. Mol. Cell. Biol., 4: 2697-2704, 1984.
    • (1984) Mol. Cell. Biol. , vol.4 , pp. 2697-2704
    • Buss, J.E.1    Kamps, M.P.2    Sefton, B.M.3
  • 28
    • 0023666521 scopus 로고
    • Acylation of proteins with myristic acid occurs cotranslationally
    • Wilcox, C., Hu, J-S., and Olson, E. N. Acylation of proteins with myristic acid occurs cotranslationally. Science (Washington DC), 238: 1275-1278, 1987.
    • (1987) Science (Washington DC) , vol.238 , pp. 1275-1278
    • Wilcox, C.1    Hu, J.-S.2    Olson, E.N.3
  • 29
    • 0024314396 scopus 로고
    • Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinase
    • Morgan, D. O., Kaplan, J. M., Bishop, J. M., and Varmus, H. E. Mitosis-specific phosphorylation of p60c-src by p34cdc2-associated protein kinase. Cell, 57: 775-786, 1989.
    • (1989) Cell , vol.57 , pp. 775-786
    • Morgan, D.O.1    Kaplan, J.M.2    Bishop, J.M.3    Varmus, H.E.4
  • 30
    • 0025881652 scopus 로고
    • The Ick tyrosine protein kinase
    • Sefton, B. M. The Ick tyrosine protein kinase. Oncogene, 6:683-686,1991.
    • (1991) Oncogene , vol.6 , pp. 683-686
    • Sefton, B.M.1
  • 31
    • 0025738887 scopus 로고
    • Biochemical characteristics of cytosolic and particulate forms of protein tyrosine kinases from Mmethyl-N-nitrosurea (MNU)-induced rat mammary carcinoma
    • Srivastava, A. K., Chiasson, J-C., Chiasson, J-L., Lacroix, A., and Windsich, L. Biochemical characteristics of cytosolic and particulate forms of protein tyrosine kinases from Mmethyl-N-nitrosurea (MNU)-induced rat mammary carcinoma. Mol. Cell. Biochem., 106: 87-97, 1991.
    • (1991) Mol. Cell. Biochem. , vol.106 , pp. 87-97
    • Srivastava, A.K.1    Chiasson, J.-C.2    Chiasson, J.-L.3    Lacroix, A.4    Windsich, L.5
  • 32
    • 0022930029 scopus 로고
    • Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues Biol
    • Rosen, N., Bolen, J. B., Schwartz, A. M., Cohen, P., DeSeau, V., and Israel, M. A. Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues. J. Biol. Chem., 261: 13754-13759, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 13754-13759
    • Rosen, N.1    Bolen, J.B.2    Schwartz, A.M.3    Cohen, P.4    DeSeau, V.5    Israel, M.A.6
  • 33
    • 0025192786 scopus 로고
    • Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis
    • Cartwright, C. A., Meisler, A. I., and Eckhart, W. Activation of the pp60c-src protein kinase is an early event in colonic carcinogenesis. Proc. Natl. Acad. Sci. USA, 87: 558-562, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 558-562
    • Cartwright, C.A.1    Meisler, A.I.2    Eckhart, W.3
  • 36
  • 37
    • 0023807507 scopus 로고
    • Regulation by the autophosphorylation site in overexpressed pp60c-src
    • Kmiecik, T. E., Johnson, P. J., and Shalloway, D. Regulation by the autophosphorylation site in overexpressed pp60c-src. Mol. Cell. Biol., 8: 4541-4546, 1988.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4541-4546
    • Kmiecik, T.E.1    Johnson, P.J.2    Shalloway, D.3
  • 38
    • 0024472698 scopus 로고
    • pp60c-src' Variants containing lesions that affect phosphorylation at tyrosines 416 and 527
    • Harvey, R., Hehir, K. M., Smith, A. E., and Cheng, S. H. pp60c-src' Variants containing lesions that affect phosphorylation at tyrosines 416 and 527. Mol. Cell. Biol., 9: 3647-3656, 1989.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3647-3656
    • Harvey, R.1    Hehir, K.M.2    Smith, A.E.3    Cheng, S.H.4
  • 39
    • 0025194606 scopus 로고
    • Activation of p56/cAc through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation
    • Abraham, N., and Veillette, A. Activation of p56/cAc through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation. Mol. Cell. Biol., 10: 5197-5206, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5197-5206
    • Abraham, N.1    Veillette, A.2
  • 40
    • 0025274026 scopus 로고
    • The amino-terminal region of pp60c-src has a modulatory role and contains multiple sites of tyrosine phosphorylation
    • Espino, P. C., Harvey, R., Schweickhardt, R. L., White, G. A., Smith, A. E., and Cheng, S. H. The amino-terminal region of pp60c-src has a modulatory role and contains multiple sites of tyrosine phosphorylation. Oncogene, 5: 283-293, 1990.
    • (1990) Oncogene , vol.5 , pp. 283-293
    • Espino, P.C.1    Harvey, R.2    Schweickhardt, R.L.3    White, G.A.4    Smith, A.E.5    Cheng, S.H.6
  • 41
    • 0025211917 scopus 로고
    • Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src
    • Hirai, H., and Varmus, H. E. Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src. Mol. Cell. Biol., 10: 1307-1318, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1307-1318
    • Hirai, H.1    Varmus, H.E.2
  • 42
    • 0025345747 scopus 로고
    • Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain
    • O'Brien, M. C., Fukui, Y., and Hanafusa, H. Activation of the proto-oncogene p60c-src by point mutations in the SH2 domain. Mol. Cell. Biol., 10: 2855-2862, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2855-2862
    • O'Brien, M.C.1    Fukui, Y.2    Hanafusa, H.3
  • 43
    • 0020566206 scopus 로고
    • Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus
    • Takeya, T., and Hanafusa, H. Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell, 32:881-890, 1983.
    • (1983) Cell , vol.32 , pp. 881-890
    • Takeya, T.1    Hanafusa, H.2
  • 44
    • 0023515851 scopus 로고
    • Cell transformation by the viral src oncogene
    • Jove, R., and Hanafusa, H. Cell transformation by the viral src oncogene. Annu. Rev. Cell Biol., 3: 31-56, 1987.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 31-56
    • Jove, R.1    Hanafusa, H.2
  • 45
    • 0024573727 scopus 로고
    • Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p561ck
    • Veillette, A., Bookman, M. A., Horak, E. M., Samelson, L. E., and Bolen, J. B. Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p561ck. Nature (Lond.), 338: 257-259, 1989.
    • (1989) Nature (Lond.) , vol.338 , pp. 257-259
    • Veillette, A.1    Bookman, M.A.2    Horak, E.M.3    Samelson, L.E.4    Bolen, J.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.