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Regulation of calcium transport in pancreatic acinar plasma membranes from guinea pig

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Abstract

The regulation of the guinea-pig pancreatic acinar plasma membrane Ca2+ pump by protein kinase A, protein kinase C and calmodulin was investigated. The results were compared with the effects of these regulators on the high affinity Ca2+-ATPase found in this membrane preparation. The catalytic subunit of cyclic AMP-dependent protein kinase stimulated Ca2+ transport 2-fold, but had no effect on Ca2+-dependent ATPase activity. Purified protein kinase C, the phorbol ester 12-O-tetradecanoyl phorbol-13-acetate and diacylglycerol derivative, 1-stearoyl-2-arachidonoyl-sn-glycerol, failed to stimulate the Ca2+-uptake but augmented the Ca2+-dependent ATPase activity. Exogenously added calmodulin failed to stimulate either activity. In addition, two antagonists of calmodulin activity, trifluoperazine and compound 48/80 produced a concentration-dependent inhibition of Ca2+-transport. These data suggest the presence of endogenous calmodulin within guinea-pig pancreatic acinar plasma membranes. Both calmodulin antagonists failed to influence the Ca2+-dependent ATPase activity. The ability of boiled extracts from guinea-pig pancreatic acinar plasma membranes to stimulate the Ca2+-ATPase activity in calmodulin-depleted erythrocyte plasma membranes confirmed the presence of endogenous calmodulin. Our results imply a role for calmodulin and cAMP-dependent protein kinase, but not protein kinase C, in the regulation of Ca2+ efflux from pancreatic acinar cells. These results also provide further evidence suggesting that the high affinity Ca2+-ATPase does not catalyze the plasma membrane Ca2+-transport activity observed in pancreatic acini.

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Abbreviations

AMP:

adenosine 5′-monophosphate

CaM:

calmodulin

EDTA:

ethylenediaminetetraacetate

EGTA:

ethylene glycol bis (β-aminoethyl ether)-N,N,N′,N′-tetraacetic acid

PKA:

protein kinase A

PKC:

protein kinase C

PS:

phosphatidylserine

SA-DG:

1 stearoyl-2-arachidonoyl-sn-glycerol

TFP:

trifluoperazine

TPA:

12-O-tetradecanoyl phorbol-13-acetate

References

  1. Dormer RL, Brown GR, Doughney C, McPherson MA: Intracellular Ca2+ in pancreatic acinar cells: regulation and role in stimulation of enzyme secretion. Biosci Rep 7: 333–344, 1987

    Google Scholar 

  2. Mahey R, Bridges MA, Katz S: Relationship between Ca2+-transport and ATP hydrolytic activities in guinea-pig pancreatic acinar plasma membranes. Mol Cell Biochem 105: 137–147, 1991

    Google Scholar 

  3. Muallem S, Pandol SJ, Beeker TG: Calcium mobilizing hormones activate the plasma membrane Ca2+ pump of pancreatic acinar cells. J Membr Biol 106: 57–69, 1988

    Google Scholar 

  4. Bayerdörffer E, Eckhardt L, Haase W, Schutz I: Electrogenic calcium transport in plasma membrane of rat pancreatic acinar cells. J Membr Biol 84: 45–60, 1985

    Google Scholar 

  5. Kribben A, Tyrakowski T, Schulz I: Characterization of Mg-ATP-dependent Ca2+ transport in cat pancreatic microsomes. Am J Physiol 244: G480-G490, 1983

    Google Scholar 

  6. Ansah T-A, Molla A, Katz S: Ca2+-ATPase activity in pancreatic acinar plasma membranes. Regulation by calmodulin and acidic phospholipids. J Biol Chem 259: 13442–13450, 1984

    Google Scholar 

  7. Al-Mutairy AR, Dormer RL: Isolation of plasma membranes from pancreatic acinar cells: demonstration of a Ca2+-activated Mg2+-ATPase activity. Biochem Soc Trans 13: 900–901, 1985

    Google Scholar 

  8. Dormer RL, Al-Mutairy AR: Pancreatic acinar cell plasma-membrane enzymes involved in stimulus-secretion coupling. In: E Reid, GMW Cook and JP Luzio (eds.) Cells, Membranes, and Disease, Including Renal. Plenum Publishing Corporation, New York, 1987, pp 273–283

    Google Scholar 

  9. Allen BG, Katz S: Isolation and characterization of the calcium- and phospholipid-dependent protein kinase (protein kinase C) subtypes from bovine heart. Biochemistry 30: 4334–4343, 1991

    Google Scholar 

  10. Schatzmann HJ: Calcium extrusion across the plasma membrane by the calcium-pump and the Ca2+-Na+ exchange system. In: D Marmé (ed) Calcium and Cell Physiology. Springer-Verlag, New York, 1985, pp 18–52

    Google Scholar 

  11. Carafoli E, Niggli V, Penniston JT: Purification and reconstitution of the calcium, magnesium ATPase of the erythrocyte membrane. Ann NY Acid Sci 358: 159–168, 1980

    Google Scholar 

  12. Meyer T, Regenass U, Fabbro D, Alter E, Rösel J, Müller M, Caravatti G, Matter A: A derivative of staurosporine (CGP 41 251) shows selectivity for protein kinase C inhibition and in vitro anti -proliferative as well as in vivo anti-tumor activity. Int J Cancer 43: 851–856, 1989

    Google Scholar 

  13. Norman JA, Ansell J, Stone GA, Wennogle LP, Wasley JWF: CGS 9343B, a novel, potent, and selective inhibitor of calmodulin activity. Mol Pharmacol 31: 535–540, 1987

    Google Scholar 

  14. Neyes L, Reinlib L, Carafoli E: Phosphorylation of the Ca2+-pumping ATPase of heart sarcolemma and erythrocyte plasma membrane by the cAMP-dependent protein kinase. J Biol Chem 260: 10283–10287, 1985

    Google Scholar 

  15. Caroni P, Carafoli E: Regulation of Ca2+-pumping ATPase of heart sarcolemma by a phosphorylation-dephosphorylation process. J Biol Chem 256: 9371–9373, 1981

    Google Scholar 

  16. Smallwood JI, Gügi B, Rasmussen H: regulation of erythrocyte Ca2+ pump activity by protein kinase C. J Biol Chem 263: 2195–2202, 1988

    Google Scholar 

  17. Wang KKW, Wright LC, Machan CL, Allen BG, Conigrave AD, Roufogalis BD: Protein kinase C phosphorylates the carboxyl terminus of the plasma membrane Ca2+-ATPase from human erythrocytes. J Biol Chem 266: 9078–9085, 1991

    Google Scholar 

  18. Furukawa K-I, Tawada Y, Shigekawa M: Protein kinase C activation stimulates plasma membrane Ca2+ pump in cultured vascular smooth muscle cells. J Biol Chem 264: 4844–4849, 1989

    Google Scholar 

  19. Ochs DL, Belanger DM, Kalnitsky-Aliff J: Calcium-stimulated ATPase activity in plasma membrane vesicles from pancreatic acinar cells. Biochem Biophys Res Commun 156: 746–751, 1988

    Google Scholar 

  20. Lin S-H, Fain JN: Purification of (Ca2+-Mg2+)-ATPase from rat liver plasma membranes. J Biol Chem 259: 3016–3020, 1984

    Google Scholar 

  21. Lotersztajn S, Hanoune J, Pecker F: A high affinity calcium-stimulated magnesium-dependent ATPase in rat liver plasma membranes. Dependence on an endogenous protein activator distinct from calmodulin. J Biol Chem 256: 11209–11215, 1981

    Google Scholar 

  22. Verma AK, Penniston JT: A high affinity Ca2+-stimulated and Mg2+-dependent ATPase in rat corpus luteum plasma membrane fractions. J Biol Chem 256: 1269–1275, 1981

    Google Scholar 

  23. Carafoli E, Zurini M, Benaim G: The calcium pump of plasma membrane. In: Calcium and the Cell. Wiley, Chichester, 1986, pp 58–72

    Google Scholar 

  24. Caroni P, Zurini M, Clark A, Carafoli E: Further characterization and reconstitution of the purified Ca2+-pumping ATPase of heart sarcolemma. J Biol Chem 258: 7305–7310, 1983

    Google Scholar 

  25. Lucchesi PA, Cooney RA, Mangsen-Baker C, Honeyman TW, Scheid CR: Assessment of transport capacity of plasmalemmal Ca2+ pump in smooth muscle. Am J Physiol 255: C226-C236, 1988

    Google Scholar 

  26. Gietzen K, Adamczyk-Engelmann P, Wüthrich A, Konstantinova A, Bader H: Compound 48/80 is a selective and powerful inhibitor of calmodulin-regulated functions. Biochim Biophys Acta 736: 109–118, 1983

    Google Scholar 

  27. Mousli M, Bronner C, Landry Y, Bockaert J, Rouot B: Direct activation of GTP-binding regulatory proteins (G-Proteins) by Substance P and compound 48/80. FEBS Lett 259: 260–262, 1990

    Google Scholar 

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Authors and Affiliations

  1. Division of Pharmacology and Toxicology, Faculty of Pharmaceutical Sciences, University of British Columbia, 2146 East Mall, V6T 1Z3, Vancouver, B.C., Canada

    Rajesh Mahey, Bruce G. Allen & Sidney Katz

  2. Department of Pharmacology, Faculty of Medicine, University of British Columbia, Vancouver, B.C., Canada

    Michael A. Bridges

Authors
  1. Rajesh Mahey
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  2. Bruce G. Allen
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  3. Michael A. Bridges
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  4. Sidney Katz
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Mahey, R., Allen, B.G., Bridges, M.A. et al. Regulation of calcium transport in pancreatic acinar plasma membranes from guinea pig. Mol Cell Biochem 112, 155–162 (1992). https://doi.org/10.1007/BF00227572

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  • DOI: https://doi.org/10.1007/BF00227572

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