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ISSN 2522-9028 (Print)
ISSN 2522-9036 (Online)
DOI: https://doi.org/10.15407/fz

Fiziologichnyi Zhurnal

is a scientific journal issued by the

Bogomoletz Institute of Physiology
National Academy of Sciences of Ukraine

Editor-in-chief: V.F. Sagach

The journal was founded in 1955 as
1955 – 1977 "Fiziolohichnyi zhurnal" (ISSN 0015 – 3311)
1978 – 1993 "Fiziologicheskii zhurnal" (ISSN 0201 – 8489)
1994 – 2016 "Fiziolohichnyi zhurnal" (ISSN 0201 – 8489)
2017 – "Fiziolohichnyi zhurnal" (ISSN 2522-9028)

Fiziol. Zh. 2004; 50(3): 16-23


Regulation of intracellular calciumreleasedchannels in secretory cells of chironomus plumosus larvae by cyclicnucleotides

S.V.Bychkova, V.V. Man’ko, M.Yu.Klevets

    I.Franko Univercity, Lviv



Abstract

We investigate action of cAMP and cGMP on calcium con- tent in tissue of salivary gland of Chironomus plumosus larvae L. using arsenaso III. In order to permeabilize cells we incu- bate it in medium with saponine (0,1 mg/ml during 10 min) with next incubation in necessary solution. The internal incu- bation solution contents (in mM): 15.3 NaCl, 129.94 KCl, 0.35 Na2HPO4, 0.44 KH2PO4, 5.55 glucose, pH 7.0. It was shown that cAMP (1mkM) didn’t cause release calcium through IP3-channels, because IP3 didn’t intensify affect of cAMP, which has been established before. We observed that cAMP (100mkM) intensified ryanodine’s action to increase calcium content in saponin-treated gland tissue. We concluded that cAMP (100mkM) activated calcium releasing though ry- anodine-sensitive channels and inhibited IP3-dependent calcium releasing without any stimulation. Different concentration of cGMP didn’t cause change in calcium con- tent in saponin-treated gland tissue. But at presence of tapsigargine in incubation medium cGMP (100mkM) inhib- ited Са2+-released channels.

References

  1. Горшкова Т.В., Афиногенова С.А., Макаровская Е.Е. и др. Видовые и органные различия в активности и регуляции аденилат- и гуанилатциклазы // Укр. биохим. журн. – 1987. – 59. – №4. – С.9.
  2. Бичкова С., Манько В., Клевець М. Вплив цАМФ на функціонування внутрішньоклітинних Са2+-транс- портних систем секреторних клітин // Вісн. Львів. унту. Серія біологічна. – 2003. – Вип. 32. – С. 222–228.
  3. Бычкова С.В., Манько В.В., Клевець М.Ю. Комбинированное действие инозитол-1, 4, 5-трифосфата и рианодина на содержание кальция в пермеабилизированных клетках слюнных желез: Материалы 5-го Славяно-Балтийского научного форума «Санкт-Петербург – Гастро-2003» (10–12 сент. 2003 г.). – Гастроэнтерология. – 2003. – № 2–3. – С. 26.
  4. Реутов В.П., Оролов С.Н. Физиологическое значение гуанилатциклазы и роль окиси азота и нитросоединений в регуляции активности этого фермента // Физиология человека. – 1993. – 19. – № 1. – С.124–137.
  5. Манько В.В., Стельмах С.В., Ларіна О.А. Пермеа- білізовані клітини слинних залоз личинки Chironomus plumosus як об’єкт для дослідження внутріш- ньоклітинних Са2+-транспортувальних систем секре- торних клітин: Матеріали VIII Укр. біохім. з’їзду (1– 3 жовт. 2002 р., м. Чернівці) // Укр. біохім. журн. – 2002. – 64, № 4а (додаток 1). – С. 59–60.
  6. Bredt D. S., Snyder. S. H. Nitric oxide, a novel neuronal messenger // Neuron – 1992. – 8. – P.3–11.
  7. Bruce J.I.E., Shuttleworth T.J., Giovannucci D.R., Yule D.I. Phosphorylation of Inositol 1,4,5-Trisphosphate Регуляція циклічними нуклеотидами Вплив цГМФ на вміст Са2+ у тканині слинних залоз (нмоль/залозу), інкубованих за різних умов (M±m) Умова досліду Контроль цГМФ (100 мкмоль/л) Вихідне середовище інкубації 1,410±0,173 1,467±0,199; P=0,715 (n=9) Введеннягепарину (500 мкг/мл) 1,175 ± 0,162 1,184 ± 0,236; Р = 0,978 (n = 8)ріанодину (500 нмоль/л) 1,606 ± 0,437 1,231 ± 1,231; Р = 0,393 (n =8)тапсигаргіну (1 мкмоль/л) 1,068 ± 0,176 1,487 ± 1,487; Р = 0,022 (n = 7)
  8. ISSN 0201-8489 Фізіол. журн., 2004, Т. 50, № 3 23 С.В. Бичкова, В.В.Манько, М.Ю. Клевець Receptors in Parotid Acinar Cells. A mechanism for the synergistic effects of cAMP on Ca2+ signaling // J. Biol. Chem. – 2002. – 277. – № 2. – P.1340–1348.
  9. Bychkova S.V., Man’ko V.V., Klevets M.Ju. Ryanodine-in-duced calcium release in secretory cells of Chironomus plumosus larvae salivary glands. – In.: Joint Meeting British Pharmalogical Society and the Physiological Society, University of Manchester (9–12 Sept. 2003). – P.107.
  10. 9. Cornwell, T.L., Pryzwansky R.B., Wyatt T.A., Lincoln T.M. Regulation of sarcoplasmic reticulum protein phosphorylation by localized cGMP-dependent protein kinase in vascular smooth muscle cells // Mol. Pharmacol. – 1991. – 40. P.923–931.
  11. 10. DeSouza N., Reiken S., Ondrias K. et al. Protein kinase A and two phosphatases are components of inositol 1,4,5-trisphosphate receptor macromolecular signaling complex // J. Biol. Chem. – 2002. – 277. – №.42. – P.39397–39400.
  12. Ferris C.D., Huganir R.L. et al. Inositol trisphosphate receptor: phosphorylation by protein kinase C and calcium calmodulin-dependent protein kinases in reconstituted lipid vesicles // Proc. Natl. Acad. Sci. USA. – 1991. – 88, № 6 – P.2232–2235.
  13. Furuichi T., Yoshikawa S., Miyawaki A. et al. Primary structure and functional expression of the inositol 1,4,5-trisphosphate-binding protein P400 // Nature. – 1989 – 342. – P. 32–38.
  14. Galione A. Cyclic ADP-ribose, the ADP-ribosyl cyclase pathway and calcium signaling // Mol. Cell. Endocrinol. –1994. – 98. – P.125–131.
  15. Galione A., White A., Wilmott N. et al. cGMP mobilizes intracellular Ca2+ in sea urchin eggs by stimulating cyclic ADP-ribose synthesis // Nature. – 1993. – 365. – P.456–459.
  16. Giovannucci D.R., Groblewski G.E., Sneyd J, Yule D.I. Targeted phosphorylation of inositol 1,4,5-trisphos- phate receptors selectively inhibits localized Ca2+ release and shapes oscillatory Ca2+ signals // J. Biol. Chem. – 2000. – 275. – №43. – P.33704–33711.
  17. Hajnoczky G., Gao E., Nomura T. et al. Multiple mechanisms by which protein kinase A potentiates inositol 1,4,5-trisphosphate-induced Ca2+ mobilization in permeabilized hepatocytes // Ibid. – 1993. – 293 (Pt 2). – P.413–422.
  18. Komalavilas P., Lincoln T.M. Phosphorylation of the inositol 1,4,5-trisphosphate receptor. Cyclic GMP-dependent protein kinase mediates cAMP and cGMP dependent phosphorylation in the intact rat aorta // Ibid. – 1996. – 271, № 36. – P.21933–21938.
  19. Lee H. C. Cyclic ADP-ribose: a new member of a super family of signaling cyclic nucleotides // Cell. Signal. – 1994. – 6. – P.591–600.
  20. 19. Manko V. Larina O., Klevets M.Yu. The effect of nitric oxide on Na+-Ca2+ exchange current in secretory cells. – In.: 3rd European Biophysics Congress, Mьnchen, Germany (9–13 Sept. 2000) // Eur. Biophys. J. with Biophys. Letters. – 2000. – 29, № 4–5. – P. 327 (4D-6).
  21. 20. Mignery G.A., Newton C.L., Archer B.T., Sьdhof T.C. Structure and expression of the rat inositol 1,4,5- trisphosphate receptor // J. Biol. Chem. – 1990. – 265. – P.12679–12685.
  22. Murthy K. S., Jin J.-G., Grider J. R., Makhlouf G. M. Characterization of PACAP receptors and signaling pathways in rabbit gastric muscle cells // Amer. J. Physiol. – 1997. – 272 (Gastrointest. Liver Physiol. – Vol. 35) – P.G1391–G1399.
  23. Murthy K. S., Makhlouf G. M. VIP/PACAP-mediated activation of membrane-bound NO synthase in smooth muscle is mediated by pertussis toxin-sensitive G i1-2 //J. Biol. Chem. – 1994. –269. – P.15977–15980.
  24. Murthy K. S., Makhlouf G. M. cGMP-mediated Ca2+release from IP3-insensitive Ca2+ stores in smoothmuscle // Amer. J. Physiol. Cell Physiol. – 1998. – 274,№ 5. – C1199–C1205.
  25. Murthy K. S., Severi C., Grider J.P., Makhlouf G.M.Inhibition of IP3and IP3-dependent Ca2+ mobilization by cyclic nucleotides in isolated gastric muscle cells // Amer. J. Physiol. – 1993. – 264 (Gastrointest. Liver Physiol.– Vol. 27). – P.G967–G974.
  26. Ozawa T. Ryanodine-sensetive Ca2+ release mechanism of rat pancreatic acinar cells is modulated by calmodulin // Biochem.Biophys. Acta. – 1999. – 1452. – P.254–262.
  27. Rooney T. A., Joseph S. K., Queen C., Thomas A. P. Cyclic GMP induces oscillatory calcium signals in rat hepatocytes // J. Biol. Chem. – 1996. – 271. – P.19817–19825.
  28. Rubin R.P., Adolf M.A. Cyclic AMP regulation of calcium mobilization and amylase release from isolated permeabilized rat parotid cells // J. Pharmacol. Exp. Ther. – 1994. –  268. – № 2. – P. 600–606.
  29. Rubtsov A.M. Molecular mechanisms of regulation of the activity of sarcoplasmic reticulum Ca-release channels (ryanodine receptors), muscle fatigue, and Severin’s phenomenon // Biochemistry (Mosc). – 2001. – 66 (10). – P.1132–1143.
  30. 29. Stelmakh S.V., Manko V.V., Klevets M.Yu. The identify of IP3-channels in salivary glands secretory cells of Chironomus plumosus larvae. – In.: Programme and Abstracts of 4th Parnas conference “Molecular mechanisms of cell activation: Biological signals and their target enzymes” (15–17 Sep. 2002, Wrocіaw). – S.l. – 2002. – P. 110.
  31. 30. Sutko J.L., Airey J.A., Welch W., Ruest L. The pharmacology of ryanodine and related compounds // Pharmacol. Rev. – 1997. – 49. – P.53–98.
  32. Zhang X., Wen J., Bidasee K. R. et al. Ryanodine and inositol trisphosphate receptors are differentially distributed and expressed in rat parotid gland // Bioch. J. – 1999. – 340. – P. 519–527.

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