Calcium binding proteins in the sarcoplasmic/endoplasmic reticulum of muscle and nonmuscle cells

1992 ◽  
Vol 112 (1) ◽  
Author(s):  
RachelE. Milner ◽  
KonradS. Famulski ◽  
Marek Michalak
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Nonmuscle Cells

Endoplasmic Reticulum and Calcium-Binding Proteins inLiriodendron TulipiferaL. (Magnoliaceae) Pollen

1994 ◽  
Vol 128 (1) ◽  
pp. 295-295 ◽  
Author(s):  
L. Navazio ◽  
L. Sponga ◽  
F. Guzzo ◽  
B. Baldan ◽  
P. Mariani ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins

Identification of a set of calcium-binding proteins in reticuloplasm, the luminal content of the endoplasmic reticulum

1988 ◽  
Vol 91 (1) ◽  
pp. 61-70 ◽  
Author(s):  
D.R. Macer ◽  
G.L. Koch
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Binding Capacity ◽  
Equilibrium Dialysis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Calcium Ionophore ◽  
Binding Activity ◽  
Calcium Binding Proteins ◽  
Molecular Weights

A procedure was developed for the isolation of reticuloplasm, the luminal material of the endoplasmic reticulum (ER). A reticuloplasm-rich extract was prepared from a murine plasmacytoma cell line that contains large amounts of ER, by first extracting the cytoplasmic contents using hypotonic lysis to yield ER-rich ‘shells’ followed by mechanical lysis to release the ER contents. The extract contains five major proteins with apparent molecular weights of 100, 75, 60, 58 and 55 (X 10(3] Mr by SDS-polyacrylamide gel electrophoresis. The 100, 75 and 58 (X 10(3] Mr species were identified as the known ER proteins endoplasmin, BiP and PD1, respectively. The ER association of the 60 and 55 (X 10(3] Mr proteins was confirmed by confocal fluorescence microscopy with affinity-purified antibodies. Equilibrium dialysis with isolated reticuloplasm gave a calcium-binding capacity of 300 nmoles calcium per mg protein with half-maximal binding at 3 mM-Ca2+. Purified endoplasmin bound 280 nmoles calcium per mg protein at a calcium concentration of 5 mM-Ca2+. A calcium overlay test revealed that, in addition to endoplasmin, reticuloplasm contained at least three other calcium-binding proteins: i.e. BiP, PDI and the 55 X 10(3) Mr protein, respectively, with endoplasmin and the 55 X 10(3) Mr protein (CRP55) accounting for the major proportion of the calcium-binding activity. Treatment of cells with calcium ionophore led to the specific over-expression of the major calcium-binding reticuloplasmins endoplasmin, BiP and CRP55. These studies show that the lumen of the ER contains a family of proteins with the capacity to bind significant amounts of calcium in the millimolar range and thereby to confer upon the ER the ability to perform a calcium storage function analogous to that of the sarcoplasmic reticulum in muscle cells.

scholarly journals SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane.

1991 ◽  
Vol 266 (29) ◽  
pp. 19599-19610 ◽  
Author(s):  
I. Wada ◽  
D. Rindress ◽  
P.H. Cameron ◽  
W.J. Ou ◽  
J.J. Doherty ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Endoplasmic Reticulum Membrane

How Important are S100A8/S100A9 Calcium Binding Proteins for the Activation of Phagocyte NADPH Oxidase, Nox2

2009 ◽  
Vol 8 (4) ◽  
pp. 282-289 ◽  
Author(s):  
Sylvie Berthier ◽  
Athan Baillet ◽  
Marie-Helene Paclet ◽  
Philippe Gaudin ◽  
Francoise Morel
Keyword(s):  
Nadph Oxidase ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Phagocyte Nadph Oxidase
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