Skin calcium-binding protein: distribution in other tissues

1983 ◽  
Vol 244 (1) ◽  
pp. C50-C57 ◽  
Author(s):  
J. H. Pavlovitch ◽  
L. Didierjean ◽  
M. Rizk ◽  
S. Balsan ◽  
J. H. Saurat
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Mechanical Damage ◽  
Physiological Role ◽  
Calcium Binding Protein ◽  
Nerve Tissue ◽  
Rat Tissues ◽  
Protein Distribution ◽  
Calcium Dependent ◽  
Dependent Processes

The distribution of epidermal calcium-binding protein was examined in rat tissues using immunodiffusion and immunofluorescence techniques to investigate its possible physiological role. Epidermal calcium-binding protein was demonstrated in the basal proliferative cell layer of all Malpighian epithelia and related tissues (epidermis, sebaceous glands, cornea, esophagus, and vagina) as well as in ependyma of brain and in the epithelia of the lens. No immunoreactivity for epidermal calcium-binding protein was found in other tissues including dermis, muscle, cartilage, blood vessels, nerve tissue, liver, endocrine glands, urogenital tract, and intestinal and respiratory epithelium. The presence of a protein immunologically indistinguishable from epidermal calcium-binding protein in proliferative cells suggests that it may be involved in the control of calcium-dependent processes perhaps related to mechanical damage and continued proliferation.

Calcium-binding protein distribution in the rat brain

1982 ◽  
Vol 239 (2) ◽  
pp. 519-525 ◽  
Author(s):  
K.G. Baimbridge ◽  
J.J. Miller ◽  
C.O. Parkes
Keyword(s):  
Rat Brain ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Protein Distribution

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

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

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.

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