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Modulation Influence of p-Chloromercuribenzoate on Plasma Membrane Na+-Ca2+Exchanger of the Secretory Cells of Chironomus Larvae Salivary Gland

  • Nataly V. Fedirko
  • Myron Yu. Klevets
  • Volodymyr V. Manko
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 500)

Abstract

Investigations the role of SH-groups of Ca2+-transport systems molecules in secretory cells functioning have special significance because of: (i) Ca2+ cations have extraordinary importance in secretory process; (ii) SH-groups have importance to maintain of lipid bilaer structure [5,11]; (iii) one of the most sensitive links, obviously, for all membrane Ca2+transporting systems are SH-groups of aminoacid’s residues since its: * have high reactive ability [9]; ** determine fourth structure of protein molecule [9], besides its are form part of regulatory domains of these transport systems and especially Na+-Ca2+-exchanger molecule dogs cardiomyocites [1]. It has also known that SH-groups are form part of large intracellular loop f of Na+-Ca2+exchanger molecule [10]. Availability of SH-groups in the Nat Ca2+exchanger molecule of secretory cell membrane in Chironomus larvae salivary gland we have supposed on the base of changes in Na+-Ca2+exchange current at alkalisation of external solution [6,8] and influence of Cd2+,Ni2+ and La3+[3]. Therefore the target of this study was to investigate the influence of SH-groups specific blocator — p-chloromercuribenzoate (PCMB) on the Na+-Ca2+exchange in the secretory cell membrane of investigated glands.

Keywords

Salivary Gland Secretory Cell Exchange Current Pump Functioning Thiol Reagent 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Beauge, L., DiPolo, R., 1992, Chemical Biophys. J. 61: A388 Google Scholar
  2. 2.
    Dixon, M., Webb, E.C., 1958 Enzymes Longmans, Gree and Co.London-New York-Toronto.Google Scholar
  3. 3.
    Fedirko, N., Klevets, M., Manko, V., 1998, Modulation Pathophys. 5 Suppl. 1:134 CrossRefGoogle Scholar
  4. 4.
    Fedirko, N.V., M.Yu. Klevets, 1999, Evidence Physiol. J. 45 (4):84. Google Scholar
  5. 5.
    Ibarra, C., Ripoche, P., Bourguet, J., 1989, Effect Membr. Biol. 110(2):115. CrossRefGoogle Scholar
  6. 6.
    Klevets, M.Yu., V.V. Manko, N. V. Fedirko, 1996, Investigation Neurophys. 28(4/5):193. Google Scholar
  7. 7.
    Lee, C., Okabe, E., 1995, Hydroxyl J. Pharmac. 67(1):21. Google Scholar
  8. 8.
    Manko, V.V., 1998, Influence Ukr. Biochem. J. 70(6):3. Google Scholar
  9. 9.
    Monte, D., Bellomo, G., Thor, H., Nicotera, P., Orrenius, S., 1984, Menadione-induced Arch. Bioch. Bioph. 235(2):343. CrossRefGoogle Scholar
  10. 10.
    Nicoll, D.A., Longoni, S., Philipson, K.D., 1990, Molecular Science 250:78. CrossRefGoogle Scholar
  11. 11.
    Rakowska, M.., Jasirska, R., Lenard, J., Komamska, I., Makowski, R., Dygas, A., Pikula, S., 1997, Membrane Mol.Cell.Biochem. 168(1–2):163. PubMedCrossRefGoogle Scholar
  12. 12.
    Senchuk, V.V., Pikulev, A.T., Dashkevich, I.N., 1990, Study Biokhimia 55(9):1648. Google Scholar
  13. 13.
    Takahashi, H., Yamaguechi, H., 1999, Role J.Cell Biochem. 74(4):663 CrossRefGoogle Scholar
  14. 14.
    Torchinskij, Yu.M.,.1977 Sulfur In Proteins Nauka, Moskow.Google Scholar
  15. 15.
    Valenzuela, Bender, 1971, Ref. Lenindger, A., 1974 Biochemistry Mir Moskow.Google Scholar
  16. 16.
    Viarengo, A., Nicotera, P., 1991, Possible… Comp. Biochem. Physiol.C. 100(1–2):81. PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Nataly V. Fedirko
    • 1
  • Myron Yu. Klevets
    • 1
  • Volodymyr V. Manko
    • 1
  1. 1.Ivan Franko National University of LvivLvivUkraine

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