Calreticulin inhibits repetitive intracellular Ca2+ waves
作者： Patricia Camacho , James D Lechleiter
DOI: 10.1016/0092-8674(95)90473-5
关键词:
摘要: Inositol 1,4,5-trisphosphate (IP3)-mediated calcium (Ca2+) signaling is subject to cytosolic and luminal regulatory mechanisms. In Xenopus oocytes, Ca(2+)-sensitive gating of the IP3 receptor (IP3R) produces repetitive waves Ca2+ release. We examined role Ca(2+)-binding protein calreticulin (CRT) in IP3-mediated by using wave activity as a sensitive release assay. Overexpression CRT inhibited IP3-induced waves. Deletion mutagenesis demonstrated that inhibition was mediated high affinity-low capacity domain, which contributes little storage. This novel function intracellular may be regulated occupancy affinity binding site.
core.ac.uk
elsevier.com
sci-hub.se 参考文章(41)
H. R. Pelham, Evidence that luminal ER proteins are sorted from secreted proteins in a post-ER compartment. The EMBO Journal. ,vol. 7, pp. 913- 918 ,(1988) , 10.1002/J.1460-2075.1988.TB02896.X
Janice P. Evans, Brian K. Kay, Chapter 7 Biochemical Fractionation of Oocytes Methods in Cell Biology. ,vol. 36, pp. 133- 148 ,(1991) , 10.1016/S0091-679X(08)60275-7
S.K. Nigam, A.L. Goldberg, S. Ho, M.F. Rohde, K.T. Bush, Myu Sherman, A set of endoplasmic reticulum proteins possessing properties of molecular chaperones includes Ca(2+)-binding proteins and members of the thioredoxin superfamily. Journal of Biological Chemistry. ,vol. 269, pp. 1744- 1749 ,(1994) , 10.1016/S0021-9258(17)42090-4
L Fliegel, K Burns, D H MacLennan, R A Reithmeier, M Michalak, Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum. Journal of Biological Chemistry. ,vol. 264, pp. 21522- 21528 ,(1989) , 10.1016/S0021-9258(20)88216-7
A M Gunteski-Hamblin, J Greeb, G E Shull, A novel Ca2+ pump expressed in brain, kidney, and stomach is encoded by an alternative transcript of the slow-twitch muscle sarcoplasmic reticulum Ca-ATPase gene. Identification of cDNAs encoding Ca2+ and other cation-transporting ATPases using an oligonucleotide probe derived from the ATP-binding site. Journal of Biological Chemistry. ,vol. 263, pp. 15032- 15040 ,(1988) , 10.1016/S0021-9258(18)68142-6
A.M. Katz, R.B. Jennings, E. Haber, H.A. Fozzard, The heart and cardiovascular system New York, NY; Raven Press. ,(1986)
S. Baksh, M. Michalak, Expression of calreticulin in Escherichia coli and identification of its Ca2+ binding domains. Journal of Biological Chemistry. ,vol. 266, pp. 21458- 21465 ,(1991) , 10.1016/S0021-9258(18)54661-5
N Liu, R E Fine, E Simons, R J Johnson, Decreasing calreticulin expression lowers the Ca2+ response to bradykinin and increases sensitivity to ionomycin in NG-108-15 cells. Journal of Biological Chemistry. ,vol. 269, pp. 28635- 28639 ,(1994) , 10.1016/S0021-9258(19)61952-6
J.B. Parys, S.W. Sernett, S DeLisle, P.M. Snyder, M.J. Welsh, K.P. Campbell, Isolation, characterization, and localization of the inositol 1,4,5-trisphosphate receptor protein in Xenopus laevis oocytes. Journal of Biological Chemistry. ,vol. 267, pp. 18776- 18782 ,(1992) , 10.1016/S0021-9258(19)37028-0
R E Milner, S Baksh, C Shemanko, M R Carpenter, L Smillie, J E Vance, M Opas, M Michalak, Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum. Journal of Biological Chemistry. ,vol. 266, pp. 7155- 7165 ,(1991) , 10.1016/S0021-9258(20)89624-0