Aequorin targeted to the endoplasmic reticulum reveals heterogeneity in luminal Ca++ concentration and reports agonist- or IP3-induced release of Ca++

Molecular Biology of the Cell

Volumn 7, Issue 3, 1996, Pages 419-434

  Button, Donald ^a   Eidsath, Alec ^b  

^a NATIONAL INSTITUTE OF MENTAL HEALTH   (United States)

^b NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AEQUORIN; CALCIUM ION; DIGITONIN; INOSITOL TRISPHOSPHATE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2;

ARTICLE; BINDING AFFINITY; CALCIUM MOBILIZATION; CALCIUM TRANSPORT; CHEMOLUMINESCENCE; CHROMATOPHORE; EMBRYO; ENDOPLASMIC RETICULUM; GENETIC HETEROGENEITY; HUMAN; HUMAN CELL; HUMAN TISSUE; MAJOR HISTOCOMPATIBILITY COMPLEX; PRIORITY JOURNAL; PROTEIN BINDING;

AEQUORIN; AMINO ACID SEQUENCE; BASE SEQUENCE; CALCIUM; CELL LINE, TRANSFORMED; CLONING, MOLECULAR; DNA PRIMERS; ENDOPLASMIC RETICULUM; GENE EXPRESSION; GOLGI APPARATUS; HUMANS; INOSITOL 1,4,5-TRISPHOSPHATE; MOLECULAR SEQUENCE DATA; RECOMBINANT FUSION PROTEINS;

EID: 0029872757     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.3.419     Document Type: Article

References (43)

1. Allbritton, N.L., Oancea, E., Kuhn, M.A., and Meyer, T. (1994). Source of nuclear calcium signals. Proc. Natl. Acad. Sci. USA 91, 12458-12462.
2. Aoki, D., Lee, N., Yamaguchi, N., Dubois, C , and Fukuda, M. (1992). Golgi retention of a trans-Golgi membrane protein, galactosyltransferase, requires cysteine and histidine residues within the membrane-anchoring domain. Proc. Natl. Acad. Sci. USA 89, 4319-4323.
3. Badminton, M.N., Kendall, J.M., Sala-Newby, G., and Campbell, A.K. (1995). Nucleoplasmin-targeted aequorin provides evidence for a nuclear calcium barrier. Exp Cell Res. 216, 236-243.
4. Barnstable, C.J., Bodmer, W F., Brown, G., Galfie, G , Milstein, C., Williams, A.F., and Ziegler, A. (1978). Production of monoclonal antibodies to group A erythrocytes, HLA and other human cell surface antigens-new tools for genetic analysis. Cell 14, 9-20.
5. Blinks, J.R., Prendergast, F.G., and Allen, D.G. (1976). Photoproteins as biological indicators. Pharmacol. Rev. 28, 1-93.
6. Bole, D.G., Hendershot, L.M., and Kearney, J.F. (1986). Posttranslational association of immunoglobulin heavy chain binding protein with nascent heavy chains in nonsecreting and secreting hybridomas. J. Cell Biol. 102, 1558-1566.
7. 2+ concentration measured with specifically targeted recombinant aequorin. EMBO. J. 12, 4813-4819.
8. 2+ mobilization. Cell Calcium 14, 663-671.
9. Campbell, A.K., Daw, R.A., Hallett, M.B., and Luzio, J.P. (1981). Direct measurement of the increase in intracellular free calcium ion concentration in response to the action of complement. Biochem. J. 194, 551-560.
10. Chen, C.A., and Okayama, H. (1988). Calcium phosphate-mediated gene transfer: a highly efficient transfection system for stably transforming cells with plasmid DNA. BioTechniques 6, 632-638.
11. Clapham, D.E. (1995). Calcium signaling. Cell 80, 259-268.
12. Cobbold, P.H., and Rink, T.J. (1987). Fluorescence and bioluminescence measurement of cytoplasmic free calcium. Biochem. J. 248, 313-328.
13. Connor, J.A. (1993). Intracellular calcium mobilization by inositol 1,4,5-trisphosphate: intracellular movements and compartmentalization. Cell Calcium 14, 185-200.
14. 2+ oscillations in non-excitable cells. Annu. Rev. Physiol. 55, 427-454.
15. Galione, A. (1993). Cyclic ADP-ribose: a new way to control calcium. Science 259, 325-326.
16. 2+ from the nuclear envelope. Cell 80, 439-444.
17. Hofer, A.M., and Machen, T.E. (1993). Technique for in situ measurement of calcium in intracellular inositol 1,4,5-trisphosphate-sensitive stores using the fluorescent indicator mag-fura-2. Proc. Natl. Acad. Sci. USA 90, 2598-2602.
18. Hsu, V.W., Shah, N., and Klausner, R.D. (1992). A brefeldin A-like phenotype is induced by the overexpression of a human ERD-2-like protein, ELP-1. Cell 69, 625-635.
19. 2+ entry in bullfrog sympathetic neurons. Neuron 12, 1073-1079.
20. Kendall, J.M., Badminton, M.N., Dormer, R.L., and Campbell, A.K. (1994). Changes in free calcium in the endoplasmic reticulum of living cells detected using targeted aequorin. Anal. Biochem. 221, 173-181.
21. Kendall, J.M., Dormer, R.L., and Campbell, A.K. (1992). Targeting aequorin to the endoplasmic reticulum of living cells. Biochem. Biophys. Res. Commun. 189, 1008-1016.
22. 32P]trisphosphate binding to isolated rat liver nuclei: evidence for inositol trisphosphate receptor-mediated calcium release from the nucleus. Proc. Natl. Acad. Sci. USA 87, 9270-9274.
23. 2+ pool in liver nuclei. Proc. Natl. Acad. Sci. USA 57, 6858-6862.
24. 2+-binding photoprotein, aequorin. FEBS Lett. 295, 63-66.
25. Pozzan, T., Rizzuto, R., Volpe, P., and Meldolesi, J. (1994). Molecular and cellular physiology of intracellular calcium stores. Physiol. Rev. 74, 595-636.
26. Ridgway, N.D., Dawson, P.A., Ho, Y.K., Brown, M.S., and Goldstein, J.L. (1992). Translocation of oxysterol binding protein to Golgi apparatus triggered by ligand binding. J. Cell Biol. 116, 307-319.
27. 2+ close to IP3-sensitive channels that are sensed by neighboring mitochondria. Science 262, 744-747.
28. Rizzuto, R., Brini, M., and Pozzan, T. (1994). Targeting recombinant aequorin to specific intracellular organelles. Methods Cell Biol. 40, 339-358.
29. ++ revealed by specifically targeted recombinant aequorin. Nature 358, 325-327.
30. 2+; to supramicromolar levels in a pancreatic β-cell line. J. Biol. Chem 268, 22385-22390.
31. Schutze, M.P., Peterson, P.A., and Jackson, M.R. (1994). An N-terminal double-arginine motif maintains type 11 membrane proteins in the endoplasmic reticulum. EMBO J. 13, 1696-1705
32. Shimomura, O., and Johnson, F.H. (1975). Regeneration of the photoprotein aequorin. Nature 256, 236-238.
33. Sitia, R., and Meldolesi, J. (1992). Endoplasmic reticulum: a dynamic patchwork of specialized subregions. Mol. Biol. Cell 3, 1067-1072.
34. Somlyo, A.P., Somlyo, A.V., Gonzalez-Serratos, H., Shuman, H., and McClellan, G. (1980). The sarcoplasmic reticulum and its composition in resting and in contracting muscle. In: Muscle Contraction: Its Regulatory Mechanisms, ed. S. Ebashi, K. Maruyama, and M Endo, Tokyo, Japan and Berlin, Germany: Japan Science Society Press and Springer-Verlag, 421-433.
35. Strubin, M., Long, E.O., and Mach, B. (1986). Two forms of the Ia antigen-associated invariant chain result from alternative initiations at two in-phase AUGs Cell 47, 619-625.
36. 2+-ATPase. Proc. Natl. Acad. Sci. USA 87, 2466-2470.
37. 2+ osculations. Proc. Natl. Acad. Sci. USA 91, 9750-9754.
38. 2+ with Quin2. Methods Enzymol. 172, 230-262.
39. Tsien, S.W., and Tsien, R.Y. (1990). Calcium channels, stores, and oscillations. Annu. Rev. Cell Biol. 6, 715-760.
40. Volpe, P., and Simon, B.J. (1991). The bulk of calcium released to the myoplasm is free in the sarcoplasmic reticulum and does not unbind from calsequestrin. FEBS Lett. 278, 274-278.
41. (2+)-activated photoprotein aequorin. Biochem. J. 293, 181-185.
42. Yeong-An, S., Kricka, L J., and Pritchett, D.B. (1993). Measurement of intracellular calcium using bioluminescent aequorin expressed in human cells. Anal. Biochem. 209, 343-347.
43. 1 cells. Am. J. Physiol. 268, C1133-C1140.