Dephosphorylation of cofilin in parotid acinar cells

Journal of Biochemistry

Volumn 120, Issue 1, 1996, Pages 35-41

  Takuma, Taishin ^a   Ichida, Tokuro ^a   Yokoyama, Noriko ^b   Tamura, Shinri ^c   Obinata, Takashi ^d  

^a HEALTH SCIENCES UNIVERSITY OF HOKKAIDO   (Japan)

^b UNIVERSITY OF WESTERN ONTARIO   (Canada)

^c TOHOKU UNIVERSITY   (Japan)

^d CHIBA UNIVERSITY   (Japan)

Author keywords

Amylase exocytosis; Cofilin dephosphorylation; Parotid gland; Protein phosphatase

Indexed keywords

AMYLASE; CALCIMYCIN; CALYCULIN A; CARBACHOL; COFILIN; CYCLIC AMP; ISOPRENALINE; PHORBOL ESTER; TACROLIMUS;

ACINAR CELL; ANIMAL TISSUE; ARTICLE; DEPHOSPHORYLATION; EXOCYTOSIS; NONHUMAN; PAROTID GLAND; PROTEIN PHOSPHORYLATION; RAT;

ANIMALIA;

EID: 0029736847     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021390     Document Type: Article

References (42)

1. Harper, J.F. (1988) Stimulus-secretion coupling: Second messenger-regulated exocytosis. Adv. 2nd Messenger Phosphoprotein Res. 22, 193-318
2. Takuma, T. and Ichida, T. (1994) Catalytic subunit of protein kinase A induces amylase release from streptolysin O-permeabilized parotid acini. J. Biol. Chem. 269, 22124-22128
3. Jahn, R., Unger, C., and Söling, H.D. (1980) Specific protein phosphorylation during stimulation of amylase secretion by β-agonists or dibutyryl adenosine 3′,5′-monophosphate in the rat parotid gland. Eur. J. Biochem. 112, 345-352
4. r = 30,000 protein by cyclic AMP-dependent protein kinase in a cell-free system. Biochem. Int. 4, 39-46
5. Baum, B.J., Freiberg, J.M., Ito, H., Roth, G.S., and Filburn, C.R. (1981) β-Adrenergic regulation of protein phosphorylation and its relationship to exocrine secretion in dispersed rat parotid gland acinar cells. J. Biol. Chem. 256, 9731-9736
6. Dowd, F.J., Watson, E.L., Horio, B., Lau, Y.S., and Park, K. (1981) Phosphorylation of rabbit parotid microsomal protein occurs only with β-adrenergic stimulation. Biochem. Biophys. Res. Commun. 101, 281-288
7. Freedman, S.D. and Jamieson, D.J. (1982) Hormone-induced protein phosphorylation. I. The relationship between secretagogue action and endogenous protein phosphorylation in intact cells from the exocrine pancreas and parotid. J. Cell Biol. 95, 903-908
8. Spearman, T.N., Hurley, K.P., Olivas, R., Ulrich, R.G., and Butcher, F.R. (1984) Subcellular location of stimulus-affected endogenous phosphoproteins in the rat parotid gland. J. Cell Biol. 99, 1354-1363
9. Quissell, D.O., Deisher, L.M., and Barzen, K.A. (1985) The rate-determining step in cAMP-mediated exocytosis in the rat parotid and submandibular glands appears to involve analogous 26-kDa integral membrane phosphoproteins. Proc. Natl. Acad. Sci. USA 82, 3237-3241
10. Freedman, S.D. and Jamieson, J.D. (1982) Hormone-induced protein phosphorylation. II. Localization to the ribosomal fraction from rat exocrine pancreas and parotid of a 29,000-dalton protein phosphorylated in situ in response to secretagogues. J. Cell Biol. 95, 909-917
11. Jahn, R. and Söling, H.D. (1983) Phosphorylation of the ribosomal protein S6 in response to secretagogues in the guinea pig exocrine pancreas, parotid and lacrimal gland. FEBS Lett. 153, 71-76
12. Thiel, G., Schmidt, W.E., Meyer, H.E., and Söling, H.-D. (1988) Purification and characterization of a 22-kDa microsomal protein from rat parotid gland which is phosphorylated following stimulation by agonists involving cAMP as second messenger. Eur. J. Biochem. 170, 643-651
13. Thiel, G. and Söling, H.D. (1988) cAMP-dependent protein phosphorylation of membrane proteins in the parotid gland, platelets and liver. Eur. J. Biochem. 174, 601-609
14. Quissell, D.O. and Deisher, L.M. (1992) Purification and partial characterization of analogous 26-kDa rat submandibular and parotid gland integral membrane phosphoproteins that may have a role in exocytosis. Arch. Oral Biol. 37, 289-295
15. r= 30,000 protein. Biochem. Int. 4, 517-523
16. Burnham, D.B. and Williams, J.A. (1982) Effects of carbachol, cholecystokinin, and insulin on protein phosphorylation in isolated pancreatic acini. J. Biol. Chem. 257, 10523-10528
17. 2+ ionophore A23187 and 12-O-tetradecanoylphorbol 13-acetate. Biochem. J. 235, 125-131
18. 2+/calmodulin-dependent protein phosphatase and secretion in pancreatic acinar cells. J. Biol. Chem. 269, 15111-15117
19. Segawa, A. and Yamashina, S. (1989) Role of microfilaments in exocytosis: A new hypothesis. Cell Struct. Funct. 14, 531-544
20. Rothman, J.E. (1994) Mechanisms of intracellular protein transport. Nature 372, 55-63
21. Muallem, S., Kwiatkowska, K., Xu, X., and Yin, H.L. (1995) Actin filament disassembly is a sufficient final trigger for exocyto- sis in nonexcitable cells. J. Cell Biol. 128, 589-598
22. Nishida, E., Maekawa, S., and Sakai, H. (1984) Cofilin, a protein in porcine brain that binds to actin filaments and inhibits their interaction with myosin and tropomyosin. Biochemistry 23, 5307-5313
23. Yonezawa, N., Nishida, E., and Sakai, H. (1985) pH control of actin polymerization by cofilin. J. Biol. Chem. 260, 14410-14412
24. Morgan, T.E., Lockerbie, R.O., Minamide, L.S., Browning, M.D., and Bamburg, J.R. (1993) Isolation and characterization of a regulated form of actin depolymerizing factor. J. Cell Biol. 122, 623-633
25. 2+. Biochem. J. 301, 41-47
26. Takuma, T. and Ichida, T. (1994) Evidence for the involvement of protein phosphorylation in cyclic AMP-mediated amylase exocytosis from parotid acinar cells. FEBS Lett. 340, 29-33
27. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
28. Abe, H., Ohshima, S., and Obinata, T. (1989) A cofilin-like protein is involved in the regulation of actin assembly in developing skeletal muscle. J. Biochem. 106, 696-702
29. Khandelwal, R.L. and Enno, T.L. (1985) Purification and characterization of a high molecular weight phosphoprotein phosphatase from rabbit liver. J. Biol. Chem. 260, 14335-14343
30. Sharma, R.K., Taylor, W.A., and Wang, J.H. (1983) Use of calmodulin affinity chromatography for purification of specific calmodulin-dependent enzymes. Methods Enzymol. 102, 210-219
31. Tamura, S., Yasui, A., and Tsuiki, S. (1989) Expression of rat protein phosphatase 2C (IA) in Escherichia coli. Biochem. Biophys. Res. Commun. 163, 131-136
32. 2+/calmodulin-dependent protein kinase II by protein phosphatase 2C. J. Biol. Chem. 268, 133-137
33. Shenolikar, S. and Ingebritsen, T.S. (1984) Protein (serine and threonine) phosphate phosphatases. Methods Enzymol. 107, 102-129
34. Bernfeld, P. (1955) Amylases, a and b. Methods Enzymol. 1, 149-158
35. Takuma, T., Ichida, T., Okumura, K., and Kanazawa, M. (1993) Protein phosphatase inhibitor calyculin A induces hyperphosphorylation of cytokeratins and inhibits amylase exocytosis in the rat parotid acini. FEBS Lett. 323, 145-150
36. Ohta, Y., Nishida, E., Sakai, H., and Miyamoto, E. (1989) Dephosphorylation of cofilin accompanies heat shock-induced nuclear accumulation of cofilin. J. Biol. Chem. 264, 16143-16148
37. Abe, H., Nagaoka, R., and Obinata, T. (1993) Cytoplasmic localization and nuclear transport of cofilin in cultured myotubes. Exp. Cell Res. 206, 1-10
38. Saito, T., Lamy, F., Roger, P.P., Lecocq, R., and Dumont, J.E. (1994) Characterization and identification as cofilin and destrin of two thyrotropin- and phorbol ester-regulated phosphoproteins in thyroid cells. Exp. Cell Res. 212, 49-61
39. Kanamori, T., Hayakawa, T., Suzuki, M., and Titani, K. (1995) Identification of two 17-kDa rat parotid gland phosphoproteins, subjects for dephosphorylation upon β-adrenergic stimulation, as destrin- and cofilin-like proteins. J. Biol. Chem. 270, 8061-8067
40. Suzuki, K., Yamaguchi, T., Tanaka, T., Kawanishi, T., Nishimaki-Mogami, T., Yamamoto, K., Tsuji, T., Irimura, T., Hayakawa, T., and Takahashi, A. (1995) Activation induces dephosphorylation of cofilin and its translocation to plasma membranes in neutrophil-like differentiated HL-60 cells. J. Biol. Chem. 270, 19551-19556
41. Batzri, S., Selinger, Z., Schramm, M., and Robinovitch, M.R. (1973) Potassium release mediated by the epinephrine α-receptor in rat parotid slices. Properties and relation to enzyme secretion. J. Biol. Chem. 248, 361-368
42. Takemura, H. (1984) Inhibitory effect of carbachol on isoproterenol-induced amylase release from isolated rat parotid cells. Jpn. J. Pharmacol. 35, 9-17