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Ortega, Claudia Karina (2007) Functional properties of an unusual isoform of the plasma membrane calcium ATPase: PMCA 2. [Ph.D. thesis]

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Abstract (english)

The plasma membrane calcium ATP-ase (PMCA) represents a primary system for the specific extrusion of calcium from eukaryotic cells. Together with Na+/Ca2+ exchangers, it is the major plasma membrane transport system responsible for the long-term regulation of the resting intracellular calcium concentration. The PMCAs contain 10 membrane-spanning segments and the NH2 and COOH termini are both located on the cytosolic side of the membrane. The PMCA pump is the product of 4 separate genes, isoform diversity being further increased by a complex pattern of alternative splicing of the primary transcripts. The four basic gene products (PMCA 1-4) and the numerous splice variants vary in expression level during development, have peculiar distribution in tissues and within
cells, and differ with respect to functional parameters, especially those involving regulation properties. PMCA 1 and 4 are ubiquitously expressed while 2 and 3 are mostly found in the central nervous system and, in lesser amounts, in the striated muscle.
Alternative splicing is peculiarly complex in PMCA2 because it involves the insertion of up to three novel exons at site A (variant w) and of two at site C (variant a). The insert at site C creates instead a novel stop codon, leading to the truncation of the pump. The site-C insertions eliminate approximately half of the calmodulin binding domain; those at site A occur next to a domain that binds activatory acidic phospholipids.
Calcium enters the stereocilia of hair cells through mechanoelectrical transduction channels opened by the deflection of the hair bundle and is exported back to endolymph
by an unusual splicing isoform (wa) of plasma-membrane calcium-pump isoform 2 (PMCA2).
Ablation or missense mutations of the pump cause deafness, as described for the G283S mutation in the deafwaddler (dfw) mouse. A deafness-inducing missense mutation of PMCA2 (G293S) has been identified in a human family. The family also was screened for mutations in cadherin 23, which accentuated hearing loss in a previously described human family with a PMCA2 mutation. The wa variant and their mutations were
overexpressed in Sf9 cells. At variance with the other PMCA2 isoforms, it became activated only marginally when exposed to a Ca2+ pulse. The defect is more pronounced
in the dfw mutant than in the G293S (human) mutant. A third mutation was analyzed: Oblivion mouse mutation (where a Serine is replaced by a Phenylalanine at position 877 in TM6), it was slightly more active than the pumps bearing the 283 and 293 mutations but still much lower that of the wild type wa. The other important aspect studied, it is the regulation mechanism of the PMCA 2 wa variant. Microsomal membranes isolated from CHO cells transfected with PMCA 2 zb, PMCA 2 wb, PMCA 2 wa and PMCA 2 wa (Tommy), where a mutation in the ATP binding site occurs in the valine 586, were assayed. Both PMCA 2 zb and PMCA 2 wb had higher basal activity than PMCA 2 wa. PMCA 2 wa (Tommy) only had about 25 per cent of the activity of PMCA 2 wa. In the presence of Calmodulin, PMCA2 zb and wb showed the highest response to it i.e., the activity of these isoforms was over eight times higher than of PMCA 2 wa. PMCA2 wa had lower affinity for calmodulin than PMCA2 zb and wb, but had still higher affinity than the corresponding Tommy mutant.
The mechanism by which different phospholipids activate the PMCAs is not known. However, given the location of the lipid-binding sequences in the pump, one speculated
that the interaction of acidic phospholipids with the calmodulin binding domain leads to some structural rearrangement that weakens the autoinhibitory intramolecular interactions formed by the COOH-terminal tail. The PMCA 2 zb and wb, when
overexpressed in CHO cells, had the same response to this acidic phospholipids implying that the inserts next to the N-terminal phospholipids binding domain (variant w) was not disturbed by the splicing insert. The PMCA wa was absolutely not stimulated
by phosphatidyl serine apparently, then, no activation by acidic phospholipids can occur when the C-terminal binding site is undisturbed. The response of the PMCA 2 b pumps to PS was 4 fold higher than that of the wa variant.
To investigate whether Calmodulin indeed removes its binding domain from the cytosolic loops of the pump, we have introduced a mutation in one of the two sites that interact with the CaM binding domain in the cytosolic loops of the pump. Prior to this,
the PMCA pump was modeled to decide the residue that should have been mutated. From the model and previous works we decided to mutate the methionine 265 in Alanine (M265A). The activity of the PMCA 2 zb and M265A pumps expressed in transfected CHO cells evaluated as a function of Ca2+ in both the presence and absence of calmodulin shows that the M265A mutant has a response to calmodulin which was the same as that of the wild type at saturating concentrations of calmodulin. The activation by CaM was higher in the M265A pump with respect to wild type pump at 1nM, 5nM and 15 nM calmodulin concentrations. This suggests that the autoinhibitory sequence was bound with less affinity to the intramolecular binding site in the Met265 mutant as less calmodulin was required to relieve the inhibition. Evidently, the inhibition of Met 265 decreased the affinity of the C-terminal autoinhibitory domain, making it
easier for calmodulin to remove it from binding site.

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EPrint type:Ph.D. thesis
Tutor:Carafoli, Ernesto
Supervisor:Carafoli, Ernesto
Ph.D. course:Ciclo 20 > Scuole per il 20simo ciclo > BIOCHIMICA E BIOTECNOLOGIE > BIOCHIMICA E BIOFISICA
Data di deposito della tesi:2007
Anno di Pubblicazione:2007
Key Words:PMCA 2, splicing variant, deafness
Settori scientifico-disciplinari MIUR:Area 05 - Scienze biologiche > BIO/10 Biochimica
Struttura di riferimento:Dipartimenti > pre 2012 Dipartimento di Chimica Biologica
Codice ID:148
Depositato il:21 Oct 2008
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Le url contenute in alcuni riferimenti sono raggiungibili cliccando sul link alla fine della citazione (Vai!) e tramite Google (Ricerca con Google). Il risultato dipende dalla formattazione della citazione.

1. Ringer, S. (1883) J. Physiol. 4, 29-43 Cerca con Google

2. Brown, E.M., Quinn, S.M. and Vassilev, P.M. (1999) in E. Carafoli and C.B. Klee (Eds) Oxford University Press, pp. 295-310 Cerca con Google

3. Kifor, O., Moore, F.D., Jr., Wang, P., Goldstein, M., Vassilev, P., Kifor, I., Hebert, S.C. and Brown, E.M. (1996) J. Clin. Endocrinol. Metab. 81, 1598-1606 Cerca con Google

4. Carafoli E and Penniston J. T. (1985) The calcium signal. Sci Am. 253(5), 70-78 5. Pedersen, P.L. and Carafoli, E. (1987) Trends Biochem. Sci. 12,186-189 Cerca con Google

6. Kretsinger, R. H. & Nockholds, C. E. (1973) J. Biol. Chem. 248, 3313-3326 Cerca con Google

7. Jurado, L. A., Chockalingam, P. S. & Jarrett, H. W. (1999) Physiol. Rev. 79, 661-682 Cerca con Google

8. Moldoveanu, T. et al. (2002) Cell 108, 649-660 Cerca con Google

9. Ebashi, S. & Kodama, K. (1968) J. Biochem. 58, 107-108 Cerca con Google

10. Lewis RS (2007) Nature 15, 284-287 Cerca con Google

11.Berggard, T. et al. (2002) J. Biol. Chem. 277, 41954-41959 Cerca con Google

12. Tsien, R. W. et al. (1987) Soc. Gen. Physiol. Ser. 41, 167-187 Cerca con Google

13. Fleckenstein, A. (1964) Inn. Med. 70, 81-99 (in German) Cerca con Google

14. Watkins J. C. (1989) in eds Watkins, J. C. & Collingridge, G. L. Oxford Univ. Press, New York, 1-17 Cerca con Google

15. Endo, M. et al. (1970) Nature 228, 34-36 Cerca con Google

16. Streb, H. et al. (1983) Nature 306, 67-69 Cerca con Google

17. Lee, H. C (1997). Physiol. Rev. 77, 1133—1164 Cerca con Google

18. Franco, L. et al. (1998) FASEB J. 12, 1507-1520 Cerca con Google

19. Perraud A. L. et al. (2001) Nature 411, 542-543 Cerca con Google

20. Reuter, H. & Seitz, N. (1968) J. Physiol. 195, 451-470 Cerca con Google

21. Baker, P. F. et al. (1969) J. Physiol. 200, 459-496 Cerca con Google

22. Carafoli, E. et al. (1974) J. Mol. Cell. Cardiol. 6, 361-371 Cerca con Google

23. Toyoshima, C. et al. (2000) Nature 405, 647-655 Cerca con Google

24. Toyoshima, C. & Nomura, H. (2002) Nature 418, 605- 611 Cerca con Google

25. James, P. et al. (1989) Nature 342, 90-92 Cerca con Google

26. Van Baelen K, Dode L, Vanoevelen J, Callewaert G, De Smedt H, Missiaen L, Parys JB, Raeymaekers L, Wuytack F. ( 2004) Biochim Biophys Acta. 1742, 103-112 Cerca con Google

27. Ton VK, Rao R. (2004) Am J Physiol Cell Physiol 287, C 580- 589 Cerca con Google

28. Schatzmann, H.J. (1966) Experientia 22(6),364- 365 Cerca con Google

29. Vincenzi ,F.F. Schatzmann HJ. (1967) Helv. Physiol. Pharmacol. Acta 25(2),CR233- Cerca con Google

30. Pedersen, P.L. and Carafoli, E. (1987) Trends Biochem. Sci .12,146-150 Cerca con Google

31. Niggli, V., Sigel E., Carafoli, E. (1982) J. Biol. Chem .10, 2350-2356 Cerca con Google

32. Hao, L., Rigaud, J.L., Inesi, G. ( 1994) J. Biol. Chem. 269, 14268-14275 Cerca con Google

33. Barrabin, H., Garrahan, P.J., Rega, A.F. (1980) Biochim. Biophys. Acta 600, 796-80 Cerca con Google

34. Scott, T.L., (1984) J. Biol .Chem. 259, 4035-4037. Cerca con Google

35. Squier, T.C., Bigelow, D.J., Fernandez-Belda, F.J., deMeis, L., Inesi, G. (1990) J. Biol. Chem. 265, 13713-13720 Cerca con Google

36. Asturias et al. (1994) Biophys. J. 66, 1665-1677 Cerca con Google

37. Szasz, I., Sarkadi, B., Schubert, A., Gardos, G. (1978) Biochim. Biophys. Acta 512(2):331-340 Cerca con Google

38. Chaudhary, J., Walia, M., Matharu, J., Escher, E., Grover, A.K. (2001) Am. J. Physiol. Cell. Physiol. 280, C1027-1030 Cerca con Google

39. Pande, J., Mallhi, K.K., Grover, A.K. (2005) Eur. J. Pharmacol. 508, 1-6. Cerca con Google

40. Stauffer, T.P., Guerini, D., Carafoli, E., (1995) J. Biol. Chem. 270,12184-12190 Cerca con Google

41. Niggli, V., Penniston, J.T., Carafoli, E., (1979) J. Biol. Chem. 254, 9955-9958 Cerca con Google

42. Jarrett, H.W., Penniston, J.T. (1978) J. Biol. Chem. 253,4676-4682 Cerca con Google

43. Gopinath, R.M., Vincenzi, F.F. (1979) Am. J. Hematol. 7, 303-312. Cerca con Google

44. James, P., Vorherr, T., Krebs, J., Morelli, A., Castello, G., McCormick, D.J., Penniston, J.T., De Flora, A., Carafoli, E. (1989) J. Biol. Chem. 264, 8289-8296 Cerca con Google

45. Falchetto, R., Vorherr, T., Brunner, J., Carafoli, E. (1991) J. Biol. Chem. 266, 2930-2936 Cerca con Google

46. Falchetto, R., Vorherr, T., Carafoli, E. (1992) Protein Sci. 12:1613-1621. Cerca con Google

47. Salamino, F., Sparatore, B., Melloni, E., Michetti, M., Viotti, P.L., Pontremoli, S., Carafoli, E. (1994) Cell Calcium 15, 28-35 Cerca con Google

48. Shull, G.E. and Greeb, J. (1988) J. Biol. Chem. 263, 8646-8657 Cerca con Google

49. Verma, A.K., Filoteo, A.G., Stanford, D.R., Wieben, E.D., Penniston, J.T., Strehler, E.E., Fischer, R., Heim, R., Vogel, G., Mathews, S., et al. (1988) J Biol Chem. 263,14152-14159 Cerca con Google

50. Toyoshima, C., Nakasako, M., Nomura, H., Ogawa, H. (2000) Nature 405, 647-655 Cerca con Google

51. Zvaritch, E., James, P., Vorherr, T., Falchetto, R., Modyanov, N., Carafoli, E. (1990) Biochemistry. 29, 8070-8076. Cerca con Google

52. James, P., Maeda, M., Fischer, R., Verma, A.K., Krebs, J., Penniston, J.T., Carafoli, E. (1988) J. Biol. Chem. 263, 2905-2910 Cerca con Google

53. Enyedi, A., Vorherr , T., James, P., McCormick, D.J., Filoteo, A.G., Carafoli, E., Penniston, J.T. (1989) J. Biol. Chem. 264, 12313-12321 Cerca con Google

54. Goldberg, J., Nairn, A.C., Kuriyan, J. (1996) Cell. 84, 875-87 Cerca con Google

55. James, P.H., Pruschy, M., Vorherr, T.E., Penniston, J.T., Carafoli, E. (1989) Biochemistry 28, 4253-4258 Cerca con Google

56. Smallwood, J.I., Gugi, B., Rasmussen, H. (1988) J. Biol. Chem. 263, 2195-2202 Cerca con Google

57. Furukawa, K., Tawada, Y., Shigekawa, M. (1989) J. Biol. Chem. 264, 4844-4849 Cerca con Google

58. Ogurusu, T., Wakabayashi, S., Furukawa, K., Tawada-Iwata, Y., Imagawa, T., Shigekawa, M. (1990) Biochem. (Tokyo) 108, 222-229 Cerca con Google

59. Fukuda, T., Ogurusu, T., Furukawa, K., Shigekawa, M. (1990) Biochem. (Tokyo) 108, 629-634 Cerca con Google

60. Kuo, T.H., Wang, K.K., Carlock, L., Diglio, C., Tsang, W. (1991) Biol. Chem. 266, 2520-2525 Cerca con Google

61. Qu, Y., Torchia, J., Sen, A.K. (1992) Can.J. Physiol. Pharmacol. 70, 1230-1235 Cerca con Google

62. Wright, L.C., Chen, S., Roufogalis, B.D. (1993) Arch. Biochem. Biophys. 306, 277- 284 Cerca con Google

63. Wang, K.K., Wright, L.C., Machan, C.L., Allen, B.G., Conigrave, A.D., Roufogalis, B.D. (1991) J. Biol. Chem. 266, 9078-9085 Cerca con Google

64. Hofmann, F., Anagli, J., Carafoli, E., Vorherr, T. (1994) J Biol. Chem 269, 24298-24303 Cerca con Google

65. Farrar,Y.J., Vanaman, T.C., Slevin, J.T. (1994) FASEB J. 8, A1390 Cerca con Google

66. Enyedi, A., Flura, M., Sarkadi, B., Gardos, G., Carafoli, E. (1987) J Biol Chem 262, 6425-6430 Cerca con Google

67. Brodin, P., Falchetto, R., Vorherr, T., Carafoli, E. (1992) Eur. J. Biochem .204, 939-946 Cerca con Google

68. Niggli, V., Adunyah, E.S., Carafoli, E. (1981) J. Biol. Chem. 256, 8588-8592 Cerca con Google

69. Penniston, J.T. (1982) Ann. N. Y. Acad. Sci. 402, 296-303 Cerca con Google

70. Wang, K.K., Villalobo, A., Roufogalis, B.D. (1992) Trends Cell Biol. 2,46-52 Cerca con Google

71. Hofmann, F., James, P., Vorherr, T., Carafoli, E. (1993) J Biol. Chem. 268, 10252-10259 Cerca con Google

72. Kosk-Kosicka, D., Bzdega, T. (1988) J. Biol. Chem. 263, 18184-18189 Cerca con Google

73. Kosk-Kosicka, D., Bzdega, T., Johnson, J.D. (1990) Biochemistry 29,1875-1879 Cerca con Google

74. Vorherr, T., Kessler, T., Hofmann, F., Carafoli, E. (1991) J. Biol. Chem. 266, 22-27 Cerca con Google

75. Bredeston, L.M., Rega, A.F. (1999) Biochim. Biophys. Acta 1420, 57-62 Cerca con Google

76. Levi,V., Rossi, J.P., Castello, P.R., Gonzalez Flecha, F.L. (2000) FEBS Lett. 483, 99-103 Cerca con Google

77. Olson, S., Wang, M.G., Carafoli, E., Strehler, E.E. , McBride, O.W. (1991) Genomics 9, 629-641 Cerca con Google

78. Brandt, P., Ibrahim, E., Bruns, G.A.P., Neve, R.L. (1992) Genomics 14, 484-487 Cerca con Google

79. Latif, F., Duh, F.M., Gnarra, J., Tory, K., Kuzmin, I., Yao, M., Stackhouse, T. Modi, W., Geil, L., Schmidt, L., Li, H., Orcutt, M.L., Maher, E., Richards, F., Phipps, M., Ferguson-Smith, M., Le Paslier, D., Linehan, W.M., Zbar, B., Lerman MI. (1993) Cancer Res. 53, 861-867 Cerca con Google

80. Wang, M.G., Yi, H., Hilfiker, H., Carafoli, E., Strehler, E.E., McBride, O.W. (1994) Cytogenet. Cell Genet. 67, 41-45 Cerca con Google

81. Brandt, P., Neve, R.L., Kammesheidt, A., Rhoads, R.E., Vanaman, T.C. (1992) J. Biol. Chem. 267, 4367-4385 Cerca con Google

82. Heim, R., Hug, M., Iwata, T., Strehler, E.E., Carafoli, E. (1992) Eur. J.Biochem. 205, 333-340 Cerca con Google

83. Kuzmin, I., Stackhouse, T., Latif, F., Duh, F.M., Geil, L., Gnarra, J., Yao, M., Li, H., Tory, K., Le Paslier, D., Chumakov, I., Cohen, D., Chinault, A.C., Linehan, W.M., Lerman, M.I., Zbar, B. (1994) Cancer Res. 54, 2486-2491 Cerca con Google

84. Brown, B.J., Hilfiker, H., DeMarco, S.J., Zacharias, D.A., Greenwood, T.M., Guerini, D., Strehler, E.E. (1996) Biochim. Biophys. Acta 1283, 10-13 Cerca con Google

85. Furuta, H., Luo, L., Hepler, K., Ryan, A.F. (1998) Hear. Res. 123,10-26 Cerca con Google

86. Street, V.A., McKee-Johnson, J.W., Fonseca, R.C., Tempel, B.L., Noben-Trauth, K. (1998) Nature Genet. 19, 390-394, Cerca con Google

87. Stahl,W.L., Eakin, T.J., Owens, J.W.M., Breininger, J.F., Filuk, P.E., Anderson, W.R. (1992) Mol. Brain Res. 16,223-231 Cerca con Google

88. Stauffer, T.P., Guerini, D., Celio, M.R., Carafoli, E. (1997) Brain Res. 748, 21-29 Cerca con Google

89. Greeb, J., Shull, G.E. (1989) J. Biol. Chem. 264, 18569-18576 Cerca con Google

90. Zacharias, D.A., Kappen, C. (1999) Biochim. Biophys. Acta 1428, 397-405 Cerca con Google

91. Guerini, D., Pan, B., Carafoli, E. (2003) J. Biol. Chem. 278, 38141-38148 Cerca con Google

92. Brini, M., Coletto, L., Pierobon, N., Kraev, N., Guerini, D., Carafoli, E. (2003) J. Biol. Chem. 278, 24500-24508 Cerca con Google

93. Strehler, E.E., Strehler-Page, M.A., Vogel, G., Carafoli, E. (1989) Proc. Natl. Acad. Sci. USA 86,6908-6912 Cerca con Google

94. Burk, S.E., Shull, G.E. (1992) J. Biol. Chem. 267, 19683-19690 Cerca con Google

95. Stauffer, T.P., Hilfiker, H., Carafoli, E., Strehler, E.E. (1993) J. Biol. Chem. 268, 25993-26003 Cerca con Google

96. Keeton, T. P., Shull, G.E. (1995) Biochem J 306, 779-785 Cerca con Google

97. Zacharias, D.A., Dalrymple, S.J, Strehler, E.E.. (1995) Mol. Brain Res. 28, 263-272 Cerca con Google

98. Dumont, R.A., Lins, U., Filoteo, A.G., Penniston, J.T., Kachar, B., Gillespie, P.G. (2001) J. Neurosci. 21, 5066-5078 Cerca con Google

99. Carafoli, E. (1994) FASEB J. 8, 993-1002 Cerca con Google

100. Keeton, T.P, Burk, S.E., Shull, G.E. (1993) J Biol Chem 268, 2740-2748 Cerca con Google

101. Chicka, M., Strehler E. E. (2003) J. Biol. Chem. 278, 18464-18470 Cerca con Google

102. Hill, J.K., Williams, D.E., LeMasurier, M., Dumont, R.A., Strehler, E.E., Gillespie, P.G. (2006) J. Neurosci. 26, 6172-6180 Cerca con Google

103. Grati, M., Aggarwal, N., Strehler, E.E., Wenthold, R.J. (2006) J. Cell. Sci. 119, 2995-3007. Cerca con Google

104. Schuh, K., Uldrijan, S., Gambaryan, S., Roethlein, N., Neyes, L. (2003) J. Biol. Chem. 278, 9778-9783 Cerca con Google

105.Kim, E., DeMarco, S.J., Marfatia, S.M., Chishti, A.H., Sheng, M., Strehler, E.E. (1998) J. Biol. Chem. 273,1591-1595 Cerca con Google

106.Williams, J.C., Armesilla, A.L., Mohamed, T.M.A., Hagarty, C.L., McIntyre, F.H., Schomburg, S., Zaki, A.O., Oceandy, D., Cartwright, E.J., Buch, M.H., Emerson, M., Neyes, L (2006) J. Biol. Chem. Epub. ahead of print Cerca con Google

107.Armesilla, A.L., Williams, J.C., Buch, M.H., Pickard, A., Emerson, M., Cartwright, E.J., Oceandy, D., Vos Michele, D., Gillies, S., Clark, G.J., Neyses, L. 2004 J. Biol. Chem. 279, 31318-31328 Cerca con Google

108.Buch, M.H., Pickard, A., Rodriguez, A., Gillies, S., Maass, A.H., Emeron, M., Cartwright, E.J., Williams, J.C., Oceandy, D., Redondo, J.M., Neyes, L., Armesilla, A.L., (2005) J. Biol. Chem. 280, 29479-29487 Cerca con Google

109.Rimessi, A., Coletto, L., Pinton, P., Rizzato, R., Brini, M., Carafoli, E. (2005) J. Biol. Chem., 280, 37195-37203 Cerca con Google

110.Goellner, G.M., DeMarco, S.J., Strehler, E.E. (2003) Ann. N.Y. Acad. Sci. 986, 461-471 Cerca con Google

111.Steven, J., DeMarco, S.J., Strehler, E. (2001) J. Biol. Chem. 276, 21594-21600 Cerca con Google

112.Steven, J., DeMarco, S.J., Chicka, M.C., Strehler, E. (2002) J. Biol. Chem. 277, 10506-10511 Cerca con Google

113.Sgambato-Faure, V., Xiong, Y., Berke, J.D., Hyman, S.E., Strehler, E.E. (2006) Biochem. Biophys. Res. Commun. 343,630-637 Cerca con Google

114.Okunade, G.W., Miller, M.L., Pyne, G.J., Sutliff, R.L., O’Connor, K.T., Neumann, J.C., Andringa, A., Miller, D.A., Prasad, V., Doetschman, T., Paul, R.J., Shull, G.E. (2004) J. Biol. Chem. 279, 33742-33750 Cerca con Google

115.Schuh, K., Cartwright, E.J., Jankevics, E., Bundschu, K., Liebermann, J., Williams, J.C., Armesilla, A.L., Emerson, M., Oceandy, D., Knobeloch, K.P., Neyses, L. (2004) J. Biol. Chem. 279, 28220-28229 Cerca con Google

116.Ren, D., Navarro, B., Perez, G., Jackson, A.C., Hsu, S., Shi, Q., Tilly, J.L., Clapham, D.E. (2001) Nature 413, 603-609 Cerca con Google

117.Chen, J., McLean, P.A., Neel, B.G., Okunade, G., Shull, G. E., Wortis, H.H. (2004) Nature Immunol. 5, 651-657 Cerca con Google

118.Kozel, P.J., Friedman, R.A., Erway, L.C., Yamoah E.N., Liu L.H., Riddle, T., Duffy, J.J., Doetschman, T., Miller, M.L., Cardell, E.L., Shull, G.E., (1998) J. Biol. Chem. 273, 18693-18696 Cerca con Google

119.Takahashi, K., Kitamura, K. (1999) Biochem. Biophys. Res. Commun. 261, 773-778 Cerca con Google

120. Lethotsky, J., Kaplan, P., Murin, R., Raeymaekers, L. (2002) Frontieres in Bioscience 7, d53-84 Cerca con Google

121.Schultz, J.M., Yang, Y., Caride, A .J., Filoteo, A., Penheither, A.R., Lagziel, A., Morell, R.J., Mohiddin, S.A., Fananapazir, L., Madeo, A.C., Penniston, J.T., Griffith, A. (2005) N. Engl. J. Med. 352, 1557-1564 Cerca con Google

122.Ficarella R., Di Leva F., Bortolozzi M., Ortolano S., Donaudy F., M. Petrillo, Melchionda S., Lelli A., Domi T. Fedrizzi L,, Lim D., Shull G. E.,. Gasparini P, Brini M., Mammano F., and Carafoli E. (2007) PNAS 104, 1516-1521 Cerca con Google

123.Berridge, M.J., Bootman, M.D., Lipp, P. (1998) Nature 395, 645-648 Cerca con Google

124.Guerini, D., Garcia-Martin, E., Gerber, A., Volbracht, C., Leist, M., Merino, C.G., Carafoli, E. (1999) J. Biol. Chem. 274, 1667-1676 Cerca con Google

125.Usachev, Y.M., Toutenhoofd, S.L., Goellner, G.M., Strehler, E.E., Thayer, S.A. (2001) J. Neurochem. 76, 1756-1765 Cerca con Google

126.Guerini, D., Wang, X., Li, L., Genazzani, A., Carafoli, E. (2000) J. Biol. Chem. 275, 3706-3712 Cerca con Google

127.Brandt, P.C., Vanaman, T.C. (2000) J. Biol. Chem. 275, 24534-24539 Cerca con Google

128.Mark, R.J., Hensley, K., Butterfield, D.A., Mattson, M.P. (1995) J. Neurosci. 15, 6239-6249 Cerca con Google

129.Nakanishi, H., Makino, N., Hata, T., Matsui, H., Yano, K., Yanaga, T. (1989) Am. J. Physiol. 257, H349-356 Cerca con Google

130.Afroze, T., Husain, M. (2000) J. Biol. Chem. 275, 9062-9069 Cerca con Google

131.Garcia, M.E., Del Zotto, H., Caride, A.J., Filoteo A.G., Penniston J.T., Rossi, J.P., Gagliardino, J.J. (2002) J. Membr. Biol. 185,17-23 Cerca con Google

132.Kamagate, A., Herchuelz, A. Bollen, A., Van Eylen, F. (2000) Cell Calcium 4, 231-246. Cerca con Google

133.Ximenes, H.M., Kamagate, A., Van Eylen, F., Carpinelli, A., Herchuelz, A. (2003) J. Biol. Chem. 278, 22956-22963 Cerca con Google

134.Glendenning, P.T., Ratajczak, Dick, I.M., Prince, R.L. (2000) Arch. Biochem. Biophys. 380, 126-132 Cerca con Google

135.Caride, A.J., Chini, E.N., Penniston, J.T., Dousa, T.P. (1999) Kidney 56, 1818-1825, Cerca con Google

136.Donahue, H.J., Penniston, J.T., Heath, H.J. (1989) J. Clin. Endocrinol. Metab. 68, 893-898 Cerca con Google

137.Lee, W.J., Roberts-Thomson, S.J., Montheith, G.R., Biochem. Biophys. Res. Commun. (2005) 337, 779-83 Cerca con Google

138. Carafoli E, Santella L, Branca D, Brini M. (2001) Crit Rev Biochem Mol Biol. 36,107-260 Cerca con Google

139. Elwess NL, Filoteo AG, Enyedi A, Penniston JT. (1997) J Biol Chem. 272,17981-17986 Cerca con Google

140. Niggli V, Adunyah ES, Penniston JT, Carafoli E. (1981) J Biol Chem.256, 395-401 Cerca con Google

141. Crouch JJ, Schulte BA. (1996) Hear. Res.101, 55-61 Cerca con Google

142. Lowry, O. H.,. Rosebrough N. J,. Farr A.L and Randall R. J., (1951) J. Biol. Chem. 193, 265-275 Cerca con Google

143. Enyedi, A., Verma, A. K., Filoteo, A. G., and Penniston, J. T. (1993) J. Biol. Chem. 268, 10621-10626 Cerca con Google

144. Xu C, Ma H, Inesi G, Al-Shawi MK, Toyoshima C. (2004) J Biol Chem. 279,17973-17979 Cerca con Google

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