Calcified Tissue International

, Volume 43, Issue 6, pp 370–375 | Cite as

1,25 Dihydroxyvitamin D3 affects calmodulin distribution among subcellular fractions of skeletal muscle

  • Ana R. de Boland
  • Virginia Massheimer
  • Luis M. Fernandez
Laboratory Investigations
Received:
Revised:

Summary

1,25 Dihydroxyvitamin D3 has been shown to stimulate calcium fluxes across skeletal muscle membranes. The involvement of calmodulin in the effects of the metabolite was investigated. Primary cultures of chick embryo skeletal muscle myoblasts and soleus muscles from vitamin D-deficient or 1,25 (OH)2D3-treated chicks were used. Culture of myoblasts and vitamin D-deficient soleus with 1,25 (OH)2D3 (0.05 ng/ml) for 24 and 1 hour, respectively, significantly increased45Ca uptake by the preparations. In the presence of the calmodulin antagonists flufenazine or compound 48/80 in the uptake medium, no differences between control and treated cultures were observed. The calmodulin content of myoblasts and soleus homogenates and subcellular fractions derived therefrom was estimated by measuring their capacity to stimulate calmodulin-depleted cAMP phosphodiesterase. No changes in total calmodulin cellular content could be detected in response to 1,25(OH)2D3. However, the sterol produced an increase in calmodulin levels of microsomes, mitochondria, and crude myofibrillar fraction and a proportional decrease in cytosolic calmodulin concentration. The 1,25(OH)2D3-dependent changes in calmodulin distribution among subcellular fractions of soleus muscle were observed eitherin vivo orin vitro. The effectsin vitro were already detectable after 5 minutes of treatment with the sterol and parallel 1,25(OH)2D3-dependent changes in tissue Ca uptake. The results suggest that changes in calmodulin intracellular distribution may underly part of the mechanism by which 1,25(OH)2D3 affects muscle calcium transport.

Key words

1,25 dihydroxyvitamin D3 Skeletal muscle Calmodulin Calmodulin antagonists Calcium uptake 
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References

  1. 1.
    Matthews C, Heimberg KW, Ritz E, Agostini B, Fritzsche J, Hasselbach W (1977) Effect of 1,25-dihydroxycholecalciferol on impaired calcium transport by the sarcoplasmic reticulum in experimental uremia. Kidney Int 11:227–235PubMedGoogle Scholar
  2. 2.
    Boland R, Boland AR de, Ritz E, Hasselbach W (1983) Effect of 1,25-dihydroxy-cholecalciferol on sarcoplasmic reticulum calcium transport in strontium-fed chicks. Calcif Tissue Int 35:190–194PubMedCrossRefGoogle Scholar
  3. 3.
    Giuliani DL, Boland R (1984) Effects of vitamin D3 metabolites on calcium fluxes in intact chicken skeletal muscle and myoblasts cultured in vitro. Calcif Tissue Int 36:200–205PubMedCrossRefGoogle Scholar
  4. 4.
    Boland AR de, Boland R (1985) In vitro cellular muscle calcium metabolism. Characterizaton of effects of 1,25-dihydroxy-vitamin D3 and 25-hydroxy-vitamin D3. Z Naturforsch 40c:102–108Google Scholar
  5. 5.
    Boland AR de, Boland R (1985) Suppression of 1,25-dihydroxy-vitamin D3-dependent calcium transport by protein synthesis inhibitors and changes in phospholipids in skeletal muscle. Biochim Biophys Acta 845:237–241PubMedCrossRefGoogle Scholar
  6. 6.
    Boland R, Norman A, Ritz E, Hasselbach W (1985) Presence of a 1,25-dihydroxy-vitamin D3 receptor in chick skeletal muscle myoblasts. Biochem Biophys Res Commun 128:305–311PubMedCrossRefGoogle Scholar
  7. 7.
    Simpson RU, Thomas GA, Arnold AS (1985) Identification of 1,25-dihydroxyvitamin D3 receptors and activities in muscle. J Biol Chem 260:8282–8291Google Scholar
  8. 8.
    Boland AR de, Boland R (1987) Rapid changes in skeletal muscle calcium uptake induced in vitro by 1,25-dihydroxy-vitamin D3 are suppressed by calcium channel blockers. Endocrinology 120:1858–1864PubMedCrossRefGoogle Scholar
  9. 9.
    Vicenzi FF, Hinds TR (1980) Calmodulin and plasma membrane calcium transport. In: Cheung WY (ed) Calcium and cell function vol 1. Academic Press, New York, p 127Google Scholar
  10. 10.
    Michalak M, Famulski K, Carafoli E (1984) The Ca2+-pumping ATPase in skeletal muscle sarcolemma. Calmodulin dependence, regulation by cAMP-dependent phosphorylation and purification. J Biol Chem 259:15540–15547PubMedGoogle Scholar
  11. 11.
    Tuana BS, Mac Lennan DH (1984) Calmidazolium and compound 48/80 inhibit calmodulin-dependent protein phosphorylation and ATP-dependent Ca2+ uptake but not Ca2+-ATPase activity in skeletal muscle sarcoplasmic reticulum. J Biol Chem 259:6979–6983PubMedGoogle Scholar
  12. 12.
    Bikle DD, Munson S, Chafouleas G (1984) The role of calmodulin in 1,25-dihydroxy-vitamin D regulation of calcium transport across the intestinal brush border membrane. In: Bronner F, Peterlik M (eds) Epithelial calcium and phosphate transport: molecular and cellular aspects. Alan R. Liss, Inc, New York, p 193Google Scholar
  13. 13.
    Wasserman RH, Taylor AM (1973) Intestinal absorption of phosphate in the chick: effect of vitamin D3 and other parameters. J Nutr 103:586–599PubMedGoogle Scholar
  14. 14.
    Paul J (1975) Cell and tissue culture. Churchill Livingstone, Great BritainGoogle Scholar
  15. 15.
    Bothe V, Schmidt-Gayk H, Armbruster FP, Mayer E (1984) Assay for the diagnosis of hyper- and hypovitaminosis. D Arztl Lab 30:151–156Google Scholar
  16. 16.
    Bouillon R, DeMoor P, Baggiolini EG, Uskokovic MR (1980) A radioimmunoassay for 1,25-dihydroxycholecalciferol. Clin Chem 26:562–567PubMedGoogle Scholar
  17. 17.
    Boland AR de, Albornoz LE, Boland R (1983) The effect of cholecalciferol in vivo on proteins and lipids of skeletal muscle from rachitic chicks. Calcif Tissue Int 35:798–805PubMedCrossRefGoogle Scholar
  18. 18.
    Schimel SD, Kent C, Bischoff R, y Vagelos PR (1973) Plasma membranes from cultured muscle cells: isolation procedures and separation of putative plasma membrane marker enzymes. Proc Natl Acad Sci USA 70:3195–3199CrossRefGoogle Scholar
  19. 19.
    Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275PubMedGoogle Scholar
  20. 20.
    Wallace RW, Tallant EA, Cheung WY (1983) Assay of calmodulin by Ca2+-dependent phosphodiesterase. Methods Enzymol 102:39–47PubMedCrossRefGoogle Scholar
  21. 21.
    Fiske CH, Subbarow Y (1925) The colorimetric determination of phosphorus. J Biol Chem 66:375–400Google Scholar
  22. 22.
    Snedecor GW, Cochran WG (1967) Statistical methods. The Iowa State University Press, Ames, IowaGoogle Scholar
  23. 23.
    Tillack TW, Boland R, Martonosi A (1974) Ultrastructure of developing sarcoplasmic reticulum. J Biol Chem 249:624–633PubMedGoogle Scholar
  24. 24.
    Carafoli E, Inesi G, Rosen BP (1984) Calcium transport across biological membranes. In: Sigel H (ed) Metal ions in biological systems. Calcium and its role in biology, vol 17. Marcel Dekker, Inc, New York, p 129Google Scholar
  25. 25.
    Hirata M, Suematsu E, Koga T (1982) Calmodulin antagonists inhibit Ca2+ uptake of mitochondria of guinea pig peritoneal macrophages. Biochem Biophys Res Commun 105:1176–1181PubMedCrossRefGoogle Scholar
  26. 26.
    Thomasset M, Molla A, Parkes A, Demaille JG (1981) Intestinal calmodulin and calcium-binding protein differ in their distribution and in the effect of vitamin D steroids on their concentration. FEBS Lett 127:13–16PubMedCrossRefGoogle Scholar
  27. 27.
    Bauman VK, Valinietse MY, Babarykin DA (1984) Vitamin D3 and 1,25-dihydroxy-vitamin D3 stimulate the skeletal muscle-calcium mobilization in rachitic chicks. Arch Biochem Biophys 231:211–216PubMedCrossRefGoogle Scholar
  28. 28.
    Hatase O, Tokuda M, Itano T, Matsui H, Doi A (1982) Purification and characterization of calmodulin from rat liver mitochondria. Biochem Biophys Res Commun 104:673–679PubMedCrossRefGoogle Scholar
  29. 29.
    Means AR, Tash JS, Chafouleas JG (1982) Physiological implications of the presence, distribution, and regulation of calmodulin in eukaryotic cells. Physiol Rev 62:1–39PubMedGoogle Scholar
  30. 30.
    Saito A, Seiler S, Chu A, Fleisher S (1984) Preparation and morphology of sarcoplasmic reticulum terminal cisternae from rabbit skeletal muscle. J Cell Biol 99:875–885PubMedCrossRefGoogle Scholar
  31. 31.
    Dedman JR, Potter JD, Means AR (1977) Biological cross-reactivity of rat testis phosphodiesterase activator protein and rabbit skeletal muscle troponin-c. J Biol Chem 252:2437–2440PubMedGoogle Scholar
  32. 32.
    Drittanti L, Boland AR de, Boland R (1987) Changes in muscle lipid metabolism induced in vitro by 1,25-dihydroxy-vitamin D3. Biochim Biophys Acta 918:83–92PubMedGoogle Scholar

Copyright information

© Springer-Verlag New York Inc. 1988

Authors and Affiliations

  • Ana R. de Boland
    • 1
  • Virginia Massheimer
    • 1
  • Luis M. Fernandez
    • 1
  1. 1.Departmento de BiologíaUniversidad Nacional del SurBahía BlancaArgentina

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