H2O2-induced tyrosine phosphorylation of protein kinase Cδ by a mechanism independent of inhibition of protein-tyrosine phosphatase in CHO and COS-7 cells

Biochemical and Biophysical Research Communications

Volumn 273, Issue 3, 2000, Pages 960-966

  Yamamoto, Toshiyoshi ^a   Matsuzaki, Hidenori ^a   Konishi, Hiroaki ^a   Ono, Yoshitaka ^a   Kikkawa, Ushio ^a  

^a KOBE UNIVERSITY   (Japan)

Author keywords

H2O2; Protein kinase C; Tyrosine phosphorylation

Indexed keywords

ARSENOSOBENZENE; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; MOLYBDIC ACID; PROTEIN KINASE C; PROTEIN TYROSINE PHOSPHATASE; VANADIC ACID;

ANIMAL CELL; ARTICLE; CHO CELL; ENZYME ACTIVATION; ENZYME PHOSPHORYLATION; NONHUMAN; PRIORITY JOURNAL;

EID: 0034647787     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2000.3048     Document Type: Article

References (31)

1. Finkel T. Oxygen radicals and signaling. Curr. Opinion Cell Biol. 10:1998;248-253.
2. Rhee S. G. Redox signaling: Hydrogen peroxide as intracellular messenger. Exp. Mol. Med. 31:1999;53-59.
3. Nishida E., Gotoh Y. The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem. Sci. 18:1993;128-131.
4. Seger R., Krebs E. G. The MAPK signaling cascade. FASEB J. 9:1995;726-735.
5. 2 stimulate mitogen-activated protein kinase activity in NIH-3T3 cells through the formation of reactive oxygen intermediates. Cancer Res. 54:1994;12-15.
6. 2 for platelet-derived growth factor signal transduction. Science. 270:1995;296-299.
7. 2. Role in cell survival following oxidant injury. J. Biol. Chem. 271:1996;4138-4142.
8. Knebel A., Rahmsdorf H. J, . Ullrich A., Herrlich P. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J. 15:1996;5314-5325.
9. Rao G. N. Hydrogen peroxide induces complex formation of Shc-Grb2-SOS with receptor tyrosine kinase and activates Ras and extracellular signal-regulated protein kinases group of mitogen-activated protein kinases. Oncogene. 13:1996;713-719.
10. Bae Y. S., Kang S. W., Seo M. S., Baines I. C., Tekle E., Chock P. B., Rhee S. G. Epidermal growth factor (EGF)-induced generation of gydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J. Biol. Chem. 272:1997;217-221.
11. Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 7:1995;484-496.
12. Li W., Mischak H., Yu J.-C., Wang L.-M., Mushinski J. F., Heidaran M. A., Pierce J. H. Tyrosine phosphorylation of protein kinase C δ in response to its activation. J. Biol. Chem. 269:1994;2349-2352.
13. Ha gene in murine keratinocytes induces tyrosine phosphorylation and reduced activity of protein kinase C δ J. Biol. Chem. 268:1993;26079-26081.
14. 2. Proc. Natl. Acad. Sci. USA. 94:1997;11233-11237.
15. 2-induced apoptosis in CHO cells. Biochem. Biophys. Res. Commun. 264:1999;840-846.
16. Yarden Y., Escobedo J. A., Kuang W-J., Yang-Feng T. L., Daniel T. O., Tremble P. M., Chen E. Y., Ando M. E., Harkins R. N., Francke U., Fried V. A., Ullrich A., Williams L. T. Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors. Nature. 323:1986;226-232.
17. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
18. Tokmakov A. A., Sahara S., Sato K., Nishida E., Fukami Y. Phosphoregulatory tyrosine of Xenopus mitogen-activated protein kinase is out of the reach of the enzyme catalytic center after autophosphorylation. Biochemical evidence for conformational changes upon phosphorylation. Eur. J. Biochem. 241:1996;322-329.
19. Koshio O., Akanuma Y., Kasuga M. Hydrogen peroxide stimulates tyrosine phosphorylation of the insulin receptor and its tyrosine kinase activity in intact cells. Biochem. J. 250:1988;95-101.
20. 2 and vanadate stimulate tyrosine phosphorylation of potential target proteins for the insulin receptor kinase in intact cells. Biochem. J. 288:1992;631-635.
21. Gordon J. A. Use of vanadate as protein-phosphotyrosine phosphatase inhibitor. Methods Enzymol. 201:1991;477-482.
22. Fantus I. G., Kadota S., Deragon G., Foster B., Posner B. I. Pervanadate [peroxide(s) of vanadate] mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase. Biochemistry. 28:1989;8864-8871.
23. Walton K. M., Dixon J. E. Protein tyrosine phosphatases. Annu. Rev. Biochem. 62:1993;101-120.
24. Imoto M., Kakeya H., Sawa T., Hayashi C., Hamada M., Takeuchi T., Umezawa K. Dephostatin, a novel protein tyrosine phosphatase inhibitor produced by Streptomyces. II. Structure determination. J. Antibiotics. 46:1993;1716-1719.
25. Garcia-Morales P., Minami Y., Luong E., Klausner R. D., Samelson L. E. Tyrosine phosphorylation in T cells is regulated by phosphatase activity: Studies with phenylarsine oxide. Proc. Natl. Acad. Sci. USA. 87:1990;9255-9259.
26. Santini F., Beaven M. A. Tyrosine phosphorylation of a mitogen-activated protein kinase-like protein occurs at a late step in exocytosis. Studies with tyrosine phosphatase inhibitors and various secretagogues in rat RBL-2H3 cells. J. Biol. Chem. 268:1993;22716-22722.
27. Barchowsky A., Roussel R. R., Klei L. R., James P. E., Ganju N., Smith K. R., Dudek E. J. Low levels of arsenic trioxide stimulate proliferative signals in primary vascular cells without activating stress effector pathways. Toxicol. Appl. Pharmacol. 159:1999;65-75.
28. Denning M. F., Dlugosz A. A., Threadgill D. W., Magnuson T., Yuspa S. H. Activation of the epidermal growth factor receptor signal transduction pathway stimulates tyrosine phosphorylation of protein kinase Cδ J. Biol. Chem. 271:1996;5325-5331.
29. Yuan Z. M., Utsugisawa T., Ishiko T., Nakada S., Huang Y., Kharbanda S., Weichselbaum R., Kufe D. Activation of protein kinase C δ by the c-Abl tyrosine kinase in response to ionizing radiation. Oncogene. 16:1998;1643-1648.
30. Szallasi Z., Denning M. F., Chang E.-Y., Rivera J., Yuspa S. H., Lehel C., Olah Z., Anderson W. B., Blumberg P. M. Development of a rapid approach to identification of tyrosine phosphorylation sites: application to PKCδ phosphorylated upon activation of the high affinity receptor for IgE in rat basophilic leukemia cells. Biochem. Biophys. Res. Commun. 214:1995;888-894.
31. Li W., Chen X.-H., Kelley C. A., Alimandi M., Zhang J., Chen Q., Bottaro D. P., Pierce J. H. Identification of tyrosine 187 as a protein kinase C δ phosphorylation site. J. Biol. Chem. 271:1996;26404-26409.