scholarly journals Identification of a calcium-binding protein as a calcium-dependent regulator of brain adenylate cyclase.

1975 ◽  
Vol 72 (1) ◽  
pp. 64-68 ◽  
Author(s):  
C. O. Brostrom ◽  
Y. C. Huang ◽  
B. M. Breckenridge ◽  
D. J. Wolff
Keyword(s):  
Adenylate Cyclase ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Calcium Dependent

scholarly journals Regulation of adenylate cyclase from glial tumor cells by calcium and a calcium-binding protein.

1976 ◽  
Vol 251 (15) ◽  
pp. 4744-4750 ◽  
Author(s):  
M A Brostrom ◽  
C O Brostrom ◽  
B M Breckenridge ◽  
D J Wolff
Keyword(s):  
Adenylate Cyclase ◽  
Tumor Cells ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Glial Tumor

scholarly journals Gene structure of calcium-dependent protease retains the ancestral organization of the calcium-binding protein gene

FEBS Letters ◽  
1986 ◽  
Vol 194 (2) ◽  
pp. 249-252 ◽  
Author(s):  
Yasufumi Emori ◽  
Shigeo Ohno ◽  
Masako Tobita ◽  
Koichi Suzuki
Keyword(s):  
Gene Structure ◽  
Calcium Binding ◽  
Protein Gene ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Calcium Dependent ◽  
Binding Protein Gene

Characterization of Cos-7 cells overexpressing the rat secretory pathway Ca2+-ATPase

2004 ◽  
Vol 286 (1) ◽  
pp. C164-C169 ◽  
Author(s):  
Timothy A. Reinhardt ◽  
Ronald L. Horst ◽  
W. Ray Waters
Keyword(s):  
Calcium Binding ◽  
Secretory Pathway ◽  
Storage Proteins ◽  
Binding Protein ◽  
Biological Effects ◽  
Liver Microsomes ◽  
Calcium Binding Protein ◽  
Rat Liver Microsomes ◽  
Calcium Dependent ◽  
Gradient Fractionation

On the basis of sequence similarities to the yeast PMR1 and hSPCA gene, the rat alternatively spliced mRNA has been suggested to be a Golgi secretory pathway Ca2+-ATPase (SPCA). Data in this report lend further support for this hypothesis in that sucrose gradient fractionation of rat liver microsomes resulted in SPCA comigrating with the Golgi calcium binding protein CALNUC, which was well resolved from the endoplasmic reticulum marker calreticulin. Also, in PC-12 cells, antibody to SPCA colocalized with an antibody to the Golgi marker α-mannosidase II. To study the biological effects of SPCA expression, we performed stable overexpression of SPCA in COS-7 cells. Seven clones were selected for further comparison with COS-7 cells containing an empty expression vector. Overexpression of SPCA resulted in a significant reduction of plasma membrane Ca2+-ATPase, sarco(endo)plasmic reticulum Ca2+-ATPase, and calreticulin expression in these clones. In contrast, the expression of the Golgi calcium-binding protein CALNUC increased significantly. The phosphoenzyme intermediate formed using membranes from clone G11/5 was calcium dependent, significantly more intense than in COS-7 cells, and not affected by La3+ treatment. Calcium uptake by G11/5 microsomes was ATP dependent and significantly greater than in microsomes from parent COS-7 cells. The overexpression of SPCA significantly increased the growth rate of these cells compared with COS-7 cells containing only the empty vector. These data demonstrate that overexpression of the rat SPCA results in significant changes in the expression of calcium transport and storage proteins in COS-7 cells.

scholarly journals Hypothermal Effects on Expression of Regucalcin, A Calcium Binding Protein, in Livers of Seawater- and Fresh Water-Acclimated Milkfish, Chanos Chanos

2021 ◽  
Author(s):  
Chia-Hao Chang ◽  
Tsung-Han Lee
Keyword(s):  
Protein Expression ◽  
Fresh Water ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Calcium Dependent ◽  
Protein Levels ◽  
Binding Function ◽  
Mrna And Protein Expression ◽  
Apoptotic Pathways

Abstract Regucalcin (RGN) is a calcium-binding protein mainly expressed in the liver. It functions in regulating activities of several calcium-dependent enzymes related to energy metabolism, antioxidant mechanisms, and apoptotic pathways. Previous proteomics analyses revealed downregulation of regucalcin in milkfish livers when acclimated to low temperature (18°C) from normal temperature (28°C). This study first identified the full-length sequence of milkfish regucalcin from livers with high similarity in the protein structure and calcium-binding function compared to the regucalcin of other animals. The mRNA and protein expression of regucalcin in livers of fresh water (FW)- and seawater (SW)-acclimated milkfish under hypothermal acclimation were further analyzed. In FW milkfish, upregulation of regucalcin was found in mRNA and protein levels from two and four days, respectively, to one week after transfer to 18°C for the two. However, in SW milkfish, upregulation of regucalcin occurred quickly and returned to the basal levels in one (mRNA expression) or two days (protein expression) up until one week after transfer. These results suggested potential roles of regucalcin in maintaining calcium homeostasis and its correlation to differential physiological responses in livers of milkfish when they were acclimated to FW and SW.

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