A proton-led model of fast calcium waves

Cell Calcium

Volumn 36, Issue 1, 2004, Pages 83-87

  Jaffe, Lionel F ^a  

^a MARINE BIOLOGICAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALRETICULIN; CALSEQUESTRIN; CELL EXTRACT; PROTON;

ARTICLE; CALCIUM SIGNALING; CALCIUM TRANSPORT; CYTOSOL; DIFFUSION; ELECTRIC POTENTIAL; ENDOPLASMIC RETICULUM; EUKARYOTIC CELL; MEMBRANE TRANSPORT; PREDICTION; PRIORITY JOURNAL; THEORETICAL MODEL;

EUKARYOTA;

EID: 2542502518     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ceca.2003.12.004     Document Type: Article

References (36)

1. L.F. Jaffe, On the conservation of fast calcium wave speeds, Cell Calcium 32 (2002) 217-229;
2. L.T. Izu, W.G. Wier, C.W. Balke, Evolution of cardiac calcium waves from stochastic calcium sparks, Biophys. J. 80 (2001) 103-120.
3. L.F. Jaffe, The path of calcium in cytosolic calcium oscillations: a unifying hypothesis, Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 9883-9887.
4. L.F. Jaffe, Classes and mechanisms of calcium waves, Cell Calcium 14 (1993) 736-745.
5. 2+ binding effects on protein conformation and protein interactions of canine cardiac calsequestrin, J. Biol. Chem. 263 (1988) 1376-1381.
6. 2+-induced folding and aggregation of skeletal muscle sarcoplasmic reticulum calsequestrin, J. Biol. Chem. 268 (1993) 24635-24641.
7. S. Wang, W.R. Trumble, H. Liao, C.R. Wesson, A.K. Dunker, C.-H. Kang, Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum, Nat. Struct. Biol. 5 (1998) 476-483.
8. E.F. Corbett, K.M. Michalak, K. Oikawa, et al., The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment, J. Biol. Chem. 275 (2000) 27177-27185.
9. M. Endo, Calcium release from the sarcoplasmic reticulum, Physiol. Rev. 57 (1977) 71-108.
10. M. Terasaki, J. Henson, D. Begg, B. Kaminer, C. Sardet, Characterization of sea urchin egg endoplasmic reticulum in cortical preparations, Dev. Biol. 148 (1991) 398-401.
11. R.V. Kristic, Ultrastructure of the Mammalian Cell, Springer-Verlag, Heidelberg, 1979.
12. J.J. Johnson, D. Epel, M. Paul, Intracellular pH and activation of sea urchin eggs after fertilization, Nature 262 (1976) 661-664.
13. M.J. Whitaker, R.A. Steinhardt, Ionic signals at fertilization, in: C.B. Metz, A. Monroy (Eds.), The Fertilization Response of the Egg, vol. 3, Academic Press, New York, 1985, pp. 167-221.
14. S.S. Shen, Direct measurement of intracellular pH during metabolic depression of the sea urchin egg, Nature 272 (1978) 253-254.
15. C.H. Johnson, D. Epel, Intracellular pH of sea urchin eggs measured by the dimethyloxazolidinedione (DMO) method, J. Cell. Biol. 89 (1981) 284-291.
16. C. Hidalgo, P. Donoso, P.H. Rodriguez, Protons induce calsequestrin conformational changes, Biophys. J. 71 (1996) 2130-2137.
17. P. Donoso, M. Beltran, C. Hidalgo, Luminal pH regulates calcium release kinetics in sarcoplasmic reticulum vesicles, Biochemistry 35 (1996) 13419-13425.
18. F. Kamp, P. Donoso, C. Hidalgo, Changes in luminal pH caused by calcium release in sarcoplasmic reticulum vesicles, Biophys. J. 74 (1998) 290-296.
19. D.R. Lide (Ed.), Handbook of Chemistry and Physics, 79th edition, CRC Press, Boca Raton, 1999.
20. C. Heilmann, C. Spamer, in: M.R. Celio et al. (Eds.), Guidebook to the Calcium-Binding Proteins, Sambrook & Tooze, Oxford, 1996, pp. 222-224.
21. H.-J. Park, S. Wu, A.K. Dunker, C.-H. Kang, Polymerization of Calsequestrin, J. Biol. Chem. 278 (2003) 16176-16182.
22. M. Michalak, Loc. Cit., pp. 220-222.
23. N. Ikemoto, B. Antoniu, J.-J. Kang, L.G. Meszaros, M. Ronjat, Intravesicular calcium transient during calcium release from sarcoplasmic reticulum, Biochemistry 30 (1991) 5230-5237.
24. A. Fabiato, Fluorescence and differential light absorption recordings with calcium probes and potential-sensitive dyes in skinned cardiac cells, Can. J. Physiol. Pharmacol. 60 (1982) 556-567.
25. Y. Nakajima, M. Endo, Release of calcium induced by 'depolarization' of the sarcoplasmic reticulum membrane, Nat. New Biol. 246 (1973) 216-218.
26. L.F. Jaffe, The propagation speeds of calcium action potentials are remarkably invariant, Biol. Cell. (Paris) 95 (2003) 343-355.
27. V. Shoshan-Barmatz, N. Hadad, W. Feng, I. Shafir, I. Orr, M. Varsany, L.M.G. Heilmeyer, VDAC/porin in sarcoplasmic reticulum from skeletal muscle, FEBS Lett. 386 (1996) 205-210.
28. H.J. Lin, P. Herman, J.R. Lakowicz, Fluorescence lifetime-resolved pH imaging of living cells, Cytometry 52A (2003) 77-89.
29. M. Guttenberger, Arbuscules of vesicular-arbuscular mycorrhizal fungi inhabit an acidic compartment within plant roots, Planta 211 (2000) 299-304.
30. i with aequorin using a photon imaging detector, Methods Cell Biol. 40 (1994) 305-337.
31. 2+] in the endoplasmic reticulum with aequorin, Cell Calcium 32 (2002) 251-260.
32. A. Fabiato, F. Fabiato, Variations of the membrane potential of the sarcoplasmic reticulum of skinned cells from cardiac and skeletal muscle detected with a potential-sensitive dye, J. Gen. Physiol. 70 (1977) 6a.
33. S. Nakajima, A. Gilai, Radial propagation of muscle action potential along the tubular system examined by potential-sensitive dyes, J. Gen. Physiol. 76 (1980) 751-762.
34. S. Fujii, A. Hirota, K. Kamino, Optical signals from early embryonic chick heart stained with potential sensitive dyes: evidence for electrical activity, J. Physiol. 304 (1980) 503-518.
35. B.M. Salzberg, A.L. Obaid, F. Bezanilla, Microsecond response of a voltage-sensitive merocyanine dye: fast voltage-clamp measurements on squid giant axon, Jpn. J. Physiol. 43 (Suppl. 1) (1993) S37-S41.
36. J.A. Heiny, J. Vergara, Dichroic behavior of the absorbance signals from dyes NK2367 and WW375 in skeletal muscle fibers, J. Gen. Physiol. 84 (1984) g05-g37.