메뉴 건너뛰기




Volumn 68, Issue 4, 1997, Pages 1720-1727

Phosphorylation by protein kinase C of annexin 2 in chromaffin cells stimulated by nicotine

Author keywords

Annexin; Chromaffin cells; Phosphorylation; Protein kinase C; Secretion

Indexed keywords

ANNEXIN; NICOTINE; PROTEIN KINASE C;

EID: 0031000590     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1997.68041720.x     Document Type: Article
Times cited : (19)

References (33)
  • 1
    • 0025291478 scopus 로고
    • The stimulatory effect of calpactin (annexin 2) in chromaffin cells: Requirement for both the N-terminal and core domains of p36 and ATP
    • Ali S. M. and Burgoyne R. D. (1990) The stimulatory effect of calpactin (annexin 2) in chromaffin cells: requirement for both the N-terminal and core domains of p36 and ATP. Cell. Signal. 2, 265-276.
    • (1990) Cell. Signal , vol.2 , pp. 265-276
    • Ali, S.M.1    Burgoyne, R.D.2
  • 2
    • 0024390672 scopus 로고
    • A role for calpactin in calcium-dependent exocytosis in chromaffin cells
    • Ali S. M., Geisow M. J., and Burgoyne R. D. (1989) A role for calpactin in calcium-dependent exocytosis in chromaffin cells. Nature 340, 313-315.
    • (1989) Nature , vol.340 , pp. 313-315
    • Ali, S.M.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 3
    • 0020420363 scopus 로고
    • Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes
    • Avruch J., Nemenoff R. A., Blackshear J., Pierce M. W., and Osathanondt R. (1982) Insulin-stimulated tyrosine phosphorylation of the insulin receptor in detergent extracts of human placental membranes. J. Biol. Chem. 257, 15162-15166.
    • (1982) J. Biol. Chem. , vol.257 , pp. 15162-15166
    • Avruch, J.1    Nemenoff, R.A.2    Blackshear, J.3    Pierce, M.W.4    Osathanondt, R.5
  • 4
    • 0022979266 scopus 로고
    • Characterization of hormone and protein release from α-toxin-permeabilized chromaffin cells in primary culture
    • Bader M. F., Thierse D., Aunis D., Ahnert-Hilger G., and Gratzl M. (1986) Characterization of hormone and protein release from α-toxin-permeabilized chromaffin cells in primary culture. J. Biol. Chem. 261, 5777-5783.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5777-5783
    • Bader, M.F.1    Thierse, D.2    Aunis, D.3    Ahnert-Hilger, G.4    Gratzl, M.5
  • 5
    • 0018254448 scopus 로고
    • Calcium-dependent exocytosis in bovine adrenal medullary cells with leaky plasma membranes
    • Baker B. F. and Knight D. E. (1978) Calcium-dependent exocytosis in bovine adrenal medullary cells with leaky plasma membranes. Nature 276, 620-622.
    • (1978) Nature , vol.276 , pp. 620-622
    • Baker, B.F.1    Knight, D.E.2
  • 6
    • 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. (1976) 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) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0030013509 scopus 로고    scopus 로고
    • Annexin 2 in exocytosis: Catecholamine secretion requires translocation of p36 to the subplasmalemmal region in chromaffin cells
    • Chasserot-Golaz S., Vitale N., Sagot I., Delouche B., Sirrig S., Pradel L. A., Henry J. P., Aunis D., and Bader M. F. (1996) Annexin 2 in exocytosis: catecholamine secretion requires translocation of p36 to the subplasmalemmal region in chromaffin cells. J. Cell Biol. 133, 1217-1236.
    • (1996) J. Cell Biol. , vol.133 , pp. 1217-1236
    • Chasserot-Golaz, S.1    Vitale, N.2    Sagot, I.3    Delouche, B.4    Sirrig, S.5    Pradel, L.A.6    Henry, J.P.7    Aunis, D.8    Bader, M.F.9
  • 9
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust D. S. and Creutz C. E. (1988) Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 331, 88-91.
    • (1988) Nature , vol.331 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 10
    • 0018733531 scopus 로고
    • Calculation programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Fabiato A. and Fabiato F. (1979) Calculation programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J. Physiol. (Paris) 75, 463-505.
    • (1979) J. Physiol. (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 11
    • 0017891182 scopus 로고
    • Functional and morphological characterization of isolated adrenal medullary cells
    • Fenwick E. M., Fajdiga P. B., Howe B. S., and Livett B. G. (1978) Functional and morphological characterization of isolated adrenal medullary cells. J. Cell Biol. 76, 12-30.
    • (1978) J. Cell Biol. , vol.76 , pp. 12-30
    • Fenwick, E.M.1    Fajdiga, P.B.2    Howe, B.S.3    Livett, B.G.4
  • 12
    • 0016192094 scopus 로고
    • +) and ionic strength determined from equilibrium studies of the reaction
    • +) and ionic strength determined from equilibrium studies of the reaction. J. Biol. Chem. 249, 3465-3474.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3465-3474
    • Flodgaard, H.1    Fleron, P.2
  • 13
    • 0001171815 scopus 로고
    • Amino-terminal sequence of p36 associated p11: Identification of the site of tyrosine phosphorylation and homology with S100
    • Glenney J. R. and Tack B. C. (1985) Amino-terminal sequence of p36 associated p11: identification of the site of tyrosine phosphorylation and homology with S100. Proc. Natl. Acad. Sci. USA 82, 7884-7888.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 7884-7888
    • Glenney, J.R.1    Tack, B.C.2
  • 14
    • 0022755882 scopus 로고
    • The protein kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo
    • Gould R., Woodgett J., Isacke C., and Hunter H. (1986) The protein kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. Mol. Cell. Biol. 6, 2738-2744.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2738-2744
    • Gould, R.1    Woodgett, J.2    Isacke, C.3    Hunter, H.4
  • 15
    • 0025193521 scopus 로고
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells
    • 2 and vanadate stimulate protein tyrosine phosphorylation in intact cells. J. Biol. Chem. 265, 2896-2902.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2896-2902
    • Heffetz, D.1    Bushkin, I.2    Dror, R.3    Zick, Y.4
  • 16
    • 0021751197 scopus 로고
    • Isoquinoline sulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C
    • Hikada H., Inagaki M., Kawamoto S., and Sasaki Y. (1984) Isoquinoline sulfonamides, novel and potent inhibitors of cyclic nucleotide dependent protein kinase and protein kinase C. Biochemistry 23, 5036-5041.
    • (1984) Biochemistry , vol.23 , pp. 5036-5041
    • Hikada, H.1    Inagaki, M.2    Kawamoto, S.3    Sasaki, Y.4
  • 17
    • 0022753927 scopus 로고
    • Modulation of p36 phosphorylation in human cells: Studies using anti-p36 monoclonal antibodies
    • Isacke C. M., Trowbridge I., and Hunter T. (1986) Modulation of p36 phosphorylation in human cells: studies using anti-p36 monoclonal antibodies. Mol. Cell. Biol. 6, 2745-2751.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2745-2751
    • Isacke, C.M.1    Trowbridge, I.2    Hunter, T.3
  • 18
    • 0023054163 scopus 로고
    • Functionally distinct serine phosphorylation sites of P36, the cellular substrate of retroviral protein kinase; differential inhibition of reassociation
    • Johnsson N., Nguyen V. P., Söling H. D., and Weber K. (1986) Functionally distinct serine phosphorylation sites of P36, the cellular substrate of retroviral protein kinase; differential inhibition of reassociation. EMBO J. 5, 3455-3460.
    • (1986) EMBO J. , vol.5 , pp. 3455-3460
    • Johnsson, N.1    Nguyen, V.P.2    Söling, H.D.3    Weber, K.4
  • 19
    • 0027052218 scopus 로고
    • Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein
    • Johnstone S. A., Hubaishy I., and Waisman D. (1992) Phosphorylation of annexin II tetramer by protein kinase C inhibits aggregation of lipid vesicles by the protein. J. Biol. Chem. 267, 25976-25981.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25976-25981
    • Johnstone, S.A.1    Hubaishy, I.2    Waisman, D.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0023038646 scopus 로고
    • Phosphorylation of a chromaffin granule-binding protein in stimulated chromaffin cells
    • Michener M. L., Dawson W. B., and Creutz C. E. (1986) Phosphorylation of a chromaffin granule-binding protein in stimulated chromaffin cells. J. Biol. Chem. 261, 6548-6555.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6548-6555
    • Michener, M.L.1    Dawson, W.B.2    Creutz, C.E.3
  • 24
    • 0022393403 scopus 로고
    • Pig thyroid spectrin. A membrane-associated protein related in structure and function to brain spectrin
    • Regnouf F., Nguyen E., Cassoly R., and Pradel L. A. (1985) Pig thyroid spectrin. A membrane-associated protein related in structure and function to brain spectrin. Eur. J. Biochem. 153, 313-319.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 313-319
    • Regnouf, F.1    Nguyen, E.2    Cassoly, R.3    Pradel, L.A.4
  • 25
    • 0026046034 scopus 로고
    • Biochemical characterization of annexins I and II isolated from pig nervous tissue
    • Regnouf F., Rendon A., and Pradel L. A. (1991) Biochemical characterization of annexins I and II isolated from pig nervous tissue. J. Neurochem. 56, 1985-1996.
    • (1991) J. Neurochem. , vol.56 , pp. 1985-1996
    • Regnouf, F.1    Rendon, A.2    Pradel, L.A.3
  • 27
    • 0026063254 scopus 로고
    • The participation of annexin 2 (calpactin 1) in calcium-evoked exocytosis requires protein kinase C
    • Sarafian T., Pradel L. A., Henry J. P., Aunis D., and Bader M. F. (1991) The participation of annexin 2 (calpactin 1) in calcium-evoked exocytosis requires protein kinase C. J. Cell Biol. 114, 1135-1147.
    • (1991) J. Cell Biol. , vol.114 , pp. 1135-1147
    • Sarafian, T.1    Pradel, L.A.2    Henry, J.P.3    Aunis, D.4    Bader, M.F.5
  • 28
    • 1842414770 scopus 로고
    • Differential regulation of histamine- and bradykinin-stimulated phospholipase C by protein kinase C isoforms in adrenal chromaffin cells
    • Edinburgh
    • Sena C. M., Rosario L. M., Parker P., Patel V., and Boarder M. R. (1995) Differential regulation of histamine- and bradykinin-stimulated phospholipase C by protein kinase C isoforms in adrenal chromaffin cells, in 8th International Symposium on Chromaffin Cell Biology, Edinburgh, p. 134.
    • (1995) 8th International Symposium on Chromaffin Cell Biology , pp. 134
    • Sena, C.M.1    Rosario, L.M.2    Parker, P.3    Patel, V.4    Boarder, M.R.5
  • 32
    • 0001542867 scopus 로고
    • Improved technique for fluorimetric estimation of catecholamines
    • von Euler U. S. and Lishajko F. (1961) Improved technique for fluorimetric estimation of catecholamines. Acta Physiol. Scand. 51, 348-355.
    • (1961) Acta Physiol. Scand. , vol.51 , pp. 348-355
    • Von Euler, U.S.1    Lishajko, F.2
  • 33
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • Waisman D. M. (1995) Annexin II tetramer: structure and function. Mol. Cell. Biochem. 149/150, 301-322.
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 301-322
    • Waisman, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.