Protoreaction of protoplasm

Cellular and Molecular Biology

Volumn 51, Issue 8, 2005, Pages 715-723

  Matveev, V V ^a  

^a INSTITUTE OF CYTOLOGY   (Russian Federation)

Author keywords

Cell hydrophobicity; Contractile proteins; Cytoskeleton; Dye adsorption; General anesthetics; Ionophore; Limiting proteins; Overton Meyer rule; Protoplasm viscosity; Valinomycin

Indexed keywords

CELL PROTEIN; CONTRACTILE PROTEIN; DYE;

ATOM; CELL STRUCTURE; CELL TYPE; CYTOPLASM; HYDROPHOBICITY; MEMBRANE STEADY POTENTIAL; MUSCLE CELL; PHASE TRANSITION; PHOTOREACTIVITY; PROTEIN FUNCTION; REVIEW; SCHOOL; STANDARDIZATION; TURBIDITY; VISCOSITY;

ANESTHETICS, GENERAL; ANIMALS; CELL PHYSIOLOGY; CELL SIZE; CELLULAR STRUCTURES; COLORING AGENTS; CONTRACTILE PROTEINS; CYTOPLASM; DRUG RESISTANCE; HUMANS; HYDROPHOBICITY; IONOPHORES; MEMBRANE POTENTIALS; MUSCLE, SKELETAL; PHASE TRANSITION;

EID: 29144475423     PISSN: 01455680     EISSN: 1165158X     Source Type: Journal    
DOI: 10.1170/T680     Document Type: Review

References (31)

1. Allison, A.C., The effects of inhalational anesthetics on proteins. In: Molecular Mechanisms in General Anaesthesia, Halsey, M.J., Millar, R.A. and Sutton, J.A. (eds.), Churchill Livingstone, Edinburg, 1974, pp. 164-181.
2. 2+-ATPase. Biochim. Biophys. Acta 1994, 1189: 189-194.
3. Brandts, J.F., Conformational transitions of proteins in water and in aqueous mixtures. In: Structure and Stability of Biological Macromolecules, Timasheft, S.N., and Fasman, G.D. (eds.), Marcel Dekker, New York, 1969, pp. 213-290.
4. Creese, R., D'Silva, J.L. and Northover, J., Effect of insulin on sodium in muscle. Nature 1958, 181: 1278.
5. 2+-ATPase of skeletal muscle sarcoplasmic reticulum. J. Biol. Chem. 1985, 260: 7325-7329.
6. Fox, S.W., Atheory of macromolecular and cellular origins. Nature 1965, 205: 328-340.
7. Franks, N.P. and Lieb, W.R., Seeing the light: protein theories of general anesthesia. Anesthesiology 2004, 101: 235-237.
8. Gulati, J., Ochesenfeld, M.M. and Ling, G.N., Metabolic cooperative control of electrolyte levels by adenosine triphosphate in the frog muscle. Biophys. J. 1971, 11: 973-980.
9. Halsey, M.J., Brown, F.F. and Richards, R.E., Perturbations of model protein systems as a basis for central and peripheral mechanisms of general anaesthesia. In: Molecular Interactions and Activity in Proteins. Porter, R. and Fitzsimons, D.W. (eds.), Excerpta Medica, Amsterdam, 1978, pp. 123-132.
10. Inai, Y., Yabuki, M., Kanno, T., Akiyama, J., Yasuda, T. and Utsumi, K., Valinomycin induces apoptosis of ascites hepatoma cells (AH-130) in relation to mitochondrial membrane potential. Cell Struct. Funct. 1997, 22: 555-563.
11. Katz, Y. and Simon, S.A., Physical parameters of the anesthetic site. Biochim. Biophys. Acta 1977, 471: 1-15.
12. Kovaleva, T.A., Suzdalskaya, I.P., Butiagina, N.V., Stepanova, T.P. and Gnetov, A.V., Enhancing the temperature stability of muscle proteins under the action of chloral hydrate and urea. Fiziol. Zh. SSSR Im. I. M. Sechenova 1991, 77: 159-162. (in Russian)
13. Leo, A., Hansch, C. and Elkins, D., Partition coefficients and their use. Chem. Rev. 1971, 71: 525-616.
14. Ling, G.N., A Physical Theory of the Living State: the Association-Induction Hypothesis, Blaisdell Publ., Waltham, Mass., 1962.
15. Ling, G.N., Life at the Cell and Below-Cell Level. The Hidden History of a Fundamental Revolution in Biology, Pacific Press, New York, 2001.
16. Matveev, V.V., Denaturation time of actomyosin exposed to different chemicals. Tsitologiia 1975, 17: 1278-1282. (in Russian)
17. Matveev, V.V., Enhanced stability of isolated muscles and actomyosin due to action of anesthetics at subnarcotic concentrations. Tsitologiia 1987, 29: 197-201. (in Russian)
18. 2+-sensitivity of the natural one. A possible model for an intracellular signalling system related to actin filaments. Physiol. Chem. Phys. Med. NMR 2000, 32: 167-178. (Full text: http://actomyosin.narod.ru or http://www.actomyosin.spb.ru)
19. Matveev, V.V., Revolution and counter revolution in cell physiology. Cell Biol. Int. 2002, 26: 305-308. (Full text: http://bioparadigma.narod.ru/ reviewonpollack.htm or http://www.bioparadigma.spb.ru/reviewonpollack.htm)
20. Nasonov, D.N., Local Reaction of Protoplasm and Gradual Excitation (English Transl. by Halpern, Y.S.), National Science Foundation, available at Office of Technical Services, US Department of Commerce, Washington, D.C., 1962.
21. Nicholls, P. and He, J., Direct and indirect effects of valinomycin upon cytochrome c oxidase. Arch. Biochem. Biophys. 1993, 301: 305-310.
22. Porter, J., Pickup, R. and Edwards, C., Membrane hyperpolarisation by valinomycin and its limitations for bacterial viability assessment using rhodamine 123 and flow cytometry. FEMS Microbiol Lett. 1995, 132: 259-262.
23. Rosenberg, B., Kemeny, G., Switzer, R.C. and Hamilton, T.C., Quantitative evidence for protein denaturation as the cause of thermal death. Nature 1971, 232: 471-473.
24. Roth, S. and Seeman, P., The membrane concentrations of neutral and positive anesthetics (alcohols, chlorpromazine, morphine) fit the Meyer-Overton rule of anesthesia; negative narcotics do not. Biochim. Biophys. Acta 1972, 255: 207-219.
25. Shapiro, H.M., Cell membrane potential analysis. Meth. Cell Biol. 1994, 41: 121-133.
26. Steverding, D. and Kadenbach, B., Valinomycin binds stoichiometrically to cytochrome c oxidase and changes its structure and function. Biochem. Biophys. Res. Commun. 1989, 160: 1132-1139.
27. +-ionophores nonactin and valinomycin interact differently with the protein of reconstituted cytochrome c oxidase. J. Bioenerg. Biomembr. 1990, 22: 197-205.
28. Suzdalskaya, I.P., Increase in stability of isolated tissues and proteins caused by action of chemical stimulants. Tsitologiia 1977, 19: 839-849. (in Russian)
29. Suzdalskaya, I.P. and Kiro, M.B., Increase in the time of conservation of contractility of glycerinated muscles exposed to subthreshhold concentrations of chemical agents. Tsitologiia 1975, 17: 50-54. (in Russian)
30. Troshin, A.S., Problems of Cell Permeability, (English Transl. by Hell, M.G. and Widdas, W.F.), Pergamon Press, London, 1966.
31. Troshina, V.P., Effect of insulin on natural properties of the frog muscle. Tsitologiia 1964, 6: 751-754. (in Russian)