Biochemical and immunohistochemical correlates of kindling-induced epilepsy: role of calcium binding protein

1983 ◽  
Vol 278 (1-2) ◽  
pp. 322-326 ◽  
Author(s):  
J.J. Miller ◽  
K.G. Baimbridge
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein

scholarly journals Calretinin expression in the mammalian neocortex: a review

2010 ◽  
pp. 665-677
Author(s):  
F Barinka ◽  
R Druga
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Actual Knowledge ◽  
Neuronal Homeostasis ◽  
Physiological Properties ◽  
Cortical Interneurons

In the mammalian neocortex, the calcium-binding protein calretinin is expressed in a subset of cortical interneurons. In the recent years, research on interneurons is one of the most rapidly growing fields in neuroscience. This review summarizes the actual knowledge of the functions of calretinin in neuronal homeostasis and particularly of the distribution, connectivity and physiological properties of calretinin expressing interneurons in the neocortex of rodents and primates, including humans. The possible neuroprotective role of calretinin and the presumed “resistance” of calretinin-expressing interneurons to various pathological processes are also discussed.

scholarly journals Calcium-binding protein of the chick chorioallantoic membrane. I. Immunohistochemical localization

1978 ◽  
Vol 77 (3) ◽  
pp. 743-751 ◽  
Author(s):  
RS Tuan ◽  
WA Scott ◽  
ZA Cohn
Keyword(s):  
Calcium Binding ◽  
Calcium Transport ◽  
External Surface ◽  
Binding Protein ◽  
Chorioallantoic Membrane ◽  
Immunohistochemical Localization ◽  
Calcium Binding Protein ◽  
Transport Function ◽  
Chick Chorioallantoic Membrane

The preparation of a specific antiserum (anti-CaBP) against the calcium-binding protein (CaBP) of the chorioallantoic membrane (CAM) is described. The anti-CaBP appeared to be specific for the CaBP by immunodiffusion and immunoelectrophoresis. Application of the anti-CaBP in immunofluorescence histochemistry revealed that the CaBP is present in the CAM only at developmental ages corresponding with the expression of the calcium transport function of the membrane. Furthermore, the CaBP is localized to the ectoderm of the CAM, appears to be exposed to the entire external surface of the ectoderm, and can be shown to be associated with cells enzymatically dissociated from the CAM. These results are consistent with a functional role of the CaBP in the CAM calcium transport process.

scholarly journals Role of the calcium-binding protein parvalbumin in short-term synaptic plasticity

2000 ◽  
Vol 97 (24) ◽  
pp. 13372-13377 ◽  
Author(s):  
O. Caillard ◽  
H. Moreno ◽  
B. Schwaller ◽  
I. Llano ◽  
M. R. Celio ◽  
...  
Keyword(s):  
Synaptic Plasticity ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Short Term

scholarly journals Downregulation of S100 Calcium Binding Protein A12 inhibits the growth of glioma cells

2020 ◽  
Author(s):  
Chunhe Lu ◽  
Jia Liu ◽  
Mingze Yao ◽  
Lun Li ◽  
Guangyu Li
Keyword(s):  
Cell Apoptosis ◽  
Calcium Binding ◽  
Binding Protein ◽  
S100 Protein ◽  
Glioma Cells ◽  
Calcium Binding Protein ◽  
Migration And Invasion ◽  
S100 Calcium Binding Protein ◽  
Tumorigenesis And Progression

Abstract Introduction: S100 Calcium Binding Protein A12 (S100A12) is a member of the S100 protein family and is widely expressed in neutrophil and low expressed in lymphocytes and monocyte. However, the role of S100A12 in glioma has not yet been identified. Methods: In the present study, we carried out immunohistochemical investigation of S100A12 in 81 glioma tissues to determine the expression of s100A12 in glioma cells, and evaluate the clinical significance of S100A12 in glioma patients. Futher we knockdown the S100A12 by ShRNA, and evaluated cell proliferation, cell migration and cell apoptosis by MTT,clony formation assay, transwell assay ,flow cytometry assa and westernblot. Results: We found that S100A12 was upregulated in tissues of glioma patients and the expression was correlated to WHO stage and tumor size. Further, we found that knockdown S100A12 inhibits the proliferation, migration and invasion of glioma cells through regulating cell apoptosis and EMT. Conclusions: These findings demonstrated a novel function for S100A12 in glioma progression and suggested that S100A12 may be served as a new marker in the tumorigenesis and progression of glioma.

scholarly journals Downregulation of S100 Calcium Binding Protein A12 inhibits the growth of glioma cells

2020 ◽  
Author(s):  
Chunhe Lu ◽  
Jia Liu ◽  
Mingze Yao ◽  
Lun Li ◽  
Guangyu Li
Keyword(s):  
Cell Apoptosis ◽  
Calcium Binding ◽  
Binding Protein ◽  
S100 Protein ◽  
Glioma Cells ◽  
Calcium Binding Protein ◽  
Migration And Invasion ◽  
Transwell Assay ◽  
S100 Calcium Binding Protein

Abstract Background: S100 Calcium Binding Protein A12 (S100A12) is a member of the S100 protein family and is widely expressed in neutrophil and low expressed in lymphocytes and monocyte. However, the role of S100A12 in glioma has not yet been identified. Methods: In the present study, we carried out immunohistochemical investigation of S100A12 in 81 glioma tissues to determine the expression of s100A12 in glioma cells, and evaluate the clinical significance of S100A12 in glioma patients. Futher we knockdown the S100A12 by ShRNA, and evaluated cell proliferation, cell migration and cell apoptosis by MTT, clony formation assay, transwell assay ,flow cytometry assa and western blot. Results: We found that S100A12 was upregulated in tissues of glioma patients and the expression was correlated to WHO stage and tumor size. Further, we found that knockdown S100A12 inhibits the proliferation, migration and invasion of glioma cells through regulating cell apoptosis and EMT. Background: S100 Calcium Binding Protein A12 (S100A12) is a member of the S100 protein family and is widely expressed in neutrophil and low expressed in lymphocytes and monocyte. However, the role of S100A12 in glioma has not yet been identified. Methods: In the present study, we carried out immunohistochemical investigation of S100A12 in 81 glioma tissues to determine the expression of s100A12 in glioma cells, and evaluate the clinical significance of S100A12 in glioma patients. Futher we knockdown the S100A12 by ShRNA, and evaluated cell proliferation, cell migration and cell apoptosis by MTT, clony formation assay, transwell assay ,flow cytometry assa and western blot. Results: We found that S100A12 was upregulated in tissues of glioma patients and the expression was correlated to WHO stage and tumor size. Further, we found that knockdown S100A12 inhibits the proliferation, migration and invasion of glioma cells through regulating cell apoptosis and EMT.

Upregulation of S100 Calcium-Binding Protein A9 levels in the lungs of patients with idiopathic pulmonary fibrosis

2020 ◽  
Author(s):  
Jong-Uk Lee ◽  
Jong-Sook Park ◽  
Myung-Shin Kim ◽  
Jai-Seong Park ◽  
Eun-Suk Go ◽  
...  
Keyword(s):  
Idiopathic Pulmonary Fibrosis ◽  
Pulmonary Fibrosis ◽  
Calcium Binding ◽  
Binding Protein ◽  
Survival Rates ◽  
Surrogate Marker ◽  
Calcium Binding Protein ◽  
S100 Calcium Binding Protein ◽  
Neutrophil Percentage

Abstract Background: Neutrophilic inflammation is a predominant characteristic of idiopathic pulmonary fibrosis (IPF). S100 Calcium-Binding Protein A9 (S100A9) is a neutrophil-derived protein and is involved in the development of neutrophil-related chronic inflammatory disorders. However, the role of S100A9 in IPF has not been evaluated.Methods : S100A9 concentrations were measured by ELISA in the BAL fluid obtained from NCs (n = 33) and patients with IPF (n = 87), NSIP (n = 22), HP (n = 19), or sarcoidosis (n = 10).Results: The S100A9 levels in BALF were significantly higher in patients with IPF than in those with NC (0.4 [0.18–0.9] vs. 0 [0–0.5] ng/mL, p < 0.001), HP (0.19 [0.07–0.33] ng/mL, p = 0.043), or sarcoidosis (0.06 [0–0.11] ng/mL, p < 0.001) patients. A S100A9 level of 0.093 ng/mL had discriminating powers of 78.79% for specificity and 81.61% for sensitivity between IPF patients and NCs. S100A9 levels were also correlated with neutrophil numbers (r = 0.356, p = 0.0007) and S100A9 was expressed on neutrophils and macrophages in the BALF of IPF patients. Patients with S100A9 levels above 0.5535 ng/mL or a neutrophil percentage above 49.09% (n = 43) had significantly lower survival rates than those with S100A9 levels at or below 0.5535 ng/mL and a neutrophil percentage at or below 49.09% (n = 41) (HR, 9.28; p = 0.0004).Conclusion: S100A9 may participate in the development and progression of IPF. The levels of S100A9 in BALF may be a surrogate marker for diagnosing IPF and predicting its prognosis.

scholarly journals Neutrophilic Cell-Free Exudate Induces Antinociception Mediate by the Protein S100A9

2006 ◽  
Vol 2006 ◽  
pp. 1-6 ◽  
Author(s):  
Rosana L. Pagano ◽  
Mario Mariano ◽  
Renata Giorgi
Keyword(s):  
Monoclonal Antibody ◽  
Calcium Binding ◽  
Inflammatory Pain ◽  
Initial Phase ◽  
Binding Protein ◽  
Antinociceptive Effect ◽  
Calcium Binding Protein ◽  
Nociceptive Response ◽  
Endogenous Control

Calcium-binding protein S100A9 (MRP-14) induces antinociceptive effect in an experimental model of painful sensibility and participates of antinociception observed during neutrophilic peritonitis induced by glycogen or carrageenan in mice. In this study, the direct antinociceptive role of the protein S100A9 in neutrophilic cell-free exudates obtained of mice injected with glycogen was investigated. Mice were intraperitoneally injected with a glycogen solution, and after4,8,24, and48hours, either the pattern of cell migration of the peritoneal exudate or the nociceptive response of animals was evaluated. The glycogen-induced neutrophilic peritonitis evoked antinociception4and8hours after inoculation of the irritant. Peritoneal cell-free exudates, collected in different times after the irritant injection, were transferred to naive animals which were submitted to the nociceptive test. The transference of exudates also induced antinociceptive effect, and neutralization of S100A9 activity by anti-S100A9 monoclonal antibody totally reverted this response. This effect was not observed when experiments were made24or48hours after glycogen injection. These results clearly indicate that S100A9 is secreted during glycogen-induced neutrophilic peritonitis, and that this protein is responsible by antinociception observed in the initial phase of inflammatory reaction. Thus, these data reinforce the hypothesis that the calcium-binding protein S100A9 participates of the endogenous control of inflammatory pain.

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