scholarly journals Neuroprotective Effect of Ginseng against Alteration of Calcium Binding Proteins Immunoreactivity in the Mice Hippocampus after Radiofrequency Exposure

2013 ◽  
Vol 2013 ◽  
pp. 1-12 ◽  
Author(s):  
Dhiraj Maskey ◽  
Jin-Koo Lee ◽  
Hak Rim Kim ◽  
Hyung-Gun Kim
Keyword(s):  
Calcium Binding ◽  
Binding Proteins ◽  
Granule Cells ◽  
Neuroprotective Effect ◽  
Staining Intensity ◽  
Treated Group ◽  
Calcium Binding Proteins ◽  
Significant Difference ◽  
Cornu Ammonis ◽  
Intracellular Ca

Calcium binding proteins (CaBPs) such as calbindin D28-k, parvalbumin, and calretinin are able to bind Ca2+with high affinity. Changes in Ca2+concentrations via CaBPs can disturb Ca2+homeostasis. Brain damage can be induced by the prolonged electromagnetic field (EMF) exposure with loss of interacellular Ca2+balance. The present study investigated the radioprotective effect of ginseng in regard to CaBPs immunoreactivity (IR) in the hippocampus through immunohistochemistry after one-month exposure at 1.6 SAR value by comparing sham control with exposed and ginseng-treated exposed groups separately. Loss of dendritic arborization was noted with the CaBPs in the Cornu Ammonis areas as well as a decrease of staining intensity of the granule cells in the dentate gyrus after exposure while no loss was observed in the ginseng-treated group. A significant difference in the relative mean density was noted between control and exposed groups but was nonsignificant in the ginseng-treated group. Decrease in CaBP IR with changes in the neuronal staining as observed in the exposed group would affect the hippocampal trisynaptic circuit by alteration of the Ca2+concentration which could be prevented by ginseng. Hence, ginseng could contribute as a radioprotective agent against EMF exposure, contributing to the maintenance of Ca2+homeostasis by preventing impairment of intracellular Ca2+levels in the hippocampus.

scholarly journals An updated investigation on the dromedary camel cerebellum (Camelus dromedarius) with special insight into the distribution of calcium-binding proteins

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Abdelraheim H. Attaai ◽  
Ahmed E. Noreldin ◽  
Fatma M. Abdel-maksoud ◽  
Manal T. Hussein
Keyword(s):  
Purkinje Cells ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Granular Layer ◽  
Granule Cells ◽  
Molecular Layer ◽  
Calcium Binding Proteins ◽  
Dromedary Camel ◽  
Cell Layers ◽  
Calbindin D

AbstractStudying the cerebella of different animals is important to expand the knowledge about the cerebellum. Studying the camel cerebellum was neglected even though the recent research in the middle east and Asia. Therefore, the present study was designed to achieve a detailed description of the morphology and the cellular organization of the camel cerebellum. Because of the high importance of the calcium ions as a necessary moderator the current work also aimed to investigate the distribution of calcium binding proteins (CaBP) such as calbindin D-28K (CB), parvalbumin (PV) and calretinin (CR) in different cerebellar cells including the non-traditional neurons. The architecture of camel cerebellum, as different mammals, consists of the medulla and three layered-cortex. According to our observation the cells in the granular layer were not crowded and many spaces were observed. CB expression was the highest by Purkinje cells including their dendritic arborization. In addition to its expression by the inhibitory interneurons (basket, stellate and Golgi neurons), it is also expressed by the excitatory granule cells. PV was expressed by Purkinje cells, including their primary arborization, and by the molecular layer cells. CR immunoreactivity (-ir) was obvious in almost all cell layers with varying degrees, however a weak or any expression by the Purkinje cells. The molecular layer cells and the Golgi and the non traditional large neurons of the granular layer showed the strongest CR-ir. Granule neurons showed moderate immunoreactivity for CB and CR. In conclusion, the results of the current study achieved a complete map for the neurochemical organization of CaBP expression and distribution by different cells in the camel cerebellum.

scholarly journals Purification, immunological and biochemical characterization of rat 28 kDa cholecalcin (cholecalciferol-induced calcium-binding proteins). Identity between renal and cerebellar cholecalcins

1985 ◽  
Vol 231 (1) ◽  
pp. 89-95 ◽  
Author(s):  
S Intrator ◽  
J Elion ◽  
M Thomasset ◽  
A Brehier
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Biochemical Characterization ◽  
Structural Characteristics ◽  
Single Species ◽  
Calcium Binding Proteins ◽  
Significant Difference ◽  
High Concentrations

The cholecalcins are intracellular vitamin D-dependent calcium-binding proteins. High concentrations of 28 kDa cholecalcins have been found in the kidneys and cerebella of birds and mammals. However, whereas the synthesis of the renal protein is vitamin D-dependent, that of the cholecalcin in the cerebella of young growing chicks and rats is apparently not. In the present study a range of immunological, physicochemical and structural characteristics of renal and cerebellar cholecalcins isolated from a single species, the rat, has been examined to ascertain what, if any, differences there are between them, other than the vitamin D-dependence. Both proteins behaved in exactly the same way during purification and showed complete immunocross-reactivity in Ouchterlony double immunodiffusion and radioimmunoassay. No difference could be detected between them on electrophoresis under denaturing conditions or on two-dimensional isoelectric focusing/electrophoresis. Their amino acid compositions were very similar, as were their u.v.-absorption spectra and their chymotryptic and tryptic peptide maps. The N-terminal sequence was found to be Gly-Gly-Val-Ser... for both cholecalcins. We have thus been unable to show any significant difference between the two proteins and suggest that the 28 kDa cholecalcins of the rat cerebellum and kidney are extremely similar, if not identical.

Differential expression of calcium-related genes in gastric cancer cells transfected with cellular prion protein

2007 ◽  
Vol 85 (3) ◽  
pp. 375-383 ◽  
Author(s):  
Jie Liang ◽  
Guanhong Luo ◽  
Xiaoxuan Ning ◽  
Yongquan Shi ◽  
Huihong Zhai ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Cancer Cells ◽  
Prion Protein ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins ◽  
Cellular Prion Protein ◽  
Primary Role ◽  
Gastric Cancer Cells ◽  
Intracellular Ca

The prion protein (PrPC) has a primary role in the pathogenesis of transmissible spongiform encephalopathies, which causes prion disorders partially due to Ca2+ dysregulation. In our previous work, we found that overexpressed PrPC in gastric cancer was involved in apoptosis, cell proliferation, and metastasis of gastric cancer. To better understand how PrPC acts in gastric cancer, a human microarray was performed to select differentially regulated genes that correlate with the biological function of PrPC. The microarray data were analyzed and revealed 3798 genes whose expression increased at least 2-fold in gastric cancer cells transfected with PrPC. These genes encode proteins involved in several aspects of cell biology, among which, we specially detected molecules related to calcium, especially the S100 calcium-binding proteins, and found that PrPC upregulates S100A1, S100A6, S100B, and S100P but downregulates CacyBP in gastric cancer cells. We also found that intracellular Ca2+ levels in cells transfected with PrPC increased, whereas these levels decreased in knockdowns of these cells. Taken together, PrPC might increase intracellular Ca2+, partially through calcium-binding proteins, or PrPC might upregulate the expression of S100 proteins, partially through stimulating the intracellular calcium level in gastric cancer. Though the underlying mechanisms need further exploration, this study provides a new insight into the role of PrPC in gastric cancer and enriches our knowledge of prion protein.

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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