scholarly journals Clinical Significance and Prognostic Value of Human Soluble Resistance-Related Calcium-Binding Protein: A Pan-Cancer Analysis

2021 ◽  
Vol 8 ◽  
Author(s):  
Jinguo Zhang ◽  
Jian Chen ◽  
Benjie Shan ◽  
Lin Lin ◽  
Jie Dong ◽  
...  
Keyword(s):  
Immune Cells ◽  
Calcium Binding ◽  
Drug Sensitivity ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
The Cancer Genome Atlas ◽  
Aberrant Expression ◽  
Mesenchymal Transition ◽  
Pan Cancer

The soluble resistance-related calcium-binding protein (sorcin, SRI) serves as the calcium-binding protein for the regulation of calcium homeostasis and multidrug resistance. Although the mounting evidence suggests a crucial role of SRI in the chemotherapeutic resistance of certain types of tumors, insights into pan-cancer analysis of SRI are unavailable. Therefore, this study aimed to probe the multifaceted properties of SRI across the 33 cancer types. The SRI expression was analyzed via The Cancer Genome Atlas (TCGA) and Genotype Tissue-Expression (GTEX) database. The SRI genomic alterations and drug sensitivity analysis were performed based on the cBioPortal and the CellMiner database. Furthermore, the correlations among the SRI expression and survival outcomes, clinical features, stemness, tumor mutation burden (TMB), microsatellite instability (MSI), and immune cells infiltration were analyzed using TCGA data. The differential analysis showed that SRI was upregulated in 25 tumor types compared with the normal tissues. Aberrant expression of SRI was able to predict survival in different cancers. Further, the most frequent alteration of SRI genomic was amplification. Moreover, the aberrant SRI expression was related to stemness score, epithelial-mesenchymal-transition (EMT)-related genes, MSI, TMB, and tumor immune microenvironment in various types of cancer. TIMER database mining further found that the SRI expression was significantly correlated with the infiltration levels of various immune cells in certain types of cancer. Intriguingly, the SRI expression was negatively correlated with drug sensitivity of fluorouracil, paclitaxel, docetaxel, and isotretinoin. Our findings highlight the predictive value of SRI in cancer and provide insights for illustrating the role of SRI in tumorigenesis and drug resistance.

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.

scholarly journals Calcium Binding Protein S100A16 Expedites Proliferation, Invasion and EMT Process in Gastric Cancer

2021 ◽  
Author(s):  
Xiaoying You ◽  
Min Li ◽  
Hongwei Cai ◽  
Wenwen Zhang ◽  
Ye Hong ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Molecular Mechanism ◽  
Calcium Binding ◽  
Malignant Tumors ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Tumor Formation ◽  
Mesenchymal Transition

Abstract Background: Gastric cancer (GC) is one of the most common malignant tumors of the digestive system, which has been the second cause of cancer-related deaths worldwide. The distant metastasis is one of the main reasons for the high recurrence and mortality rate of GC patients. Hence, it is necessary to investigate the molecular mechanism underlying gastric carcinogenesis and progression, especially the key genes and signaling pathways that promote GC cells proliferation, invasion, and metastasis. Methods: Using bioinformatics and clinicopathological analysis, in vivo tumor formation assays, mass spectrometry and so on, we characterized the role and molecular mechanism of S100 Calcium Binding Protein A16 (S100A16) in promoting GC tumor growth, migration, invasion and epithelial-to-mesenchymal transition (EMT), and investigated how Zonula Occludens-2 (ZO-2) inhibition mediates S100A16-induced metastasis and progression in GC.Results: We analyzed S100A16 expression with the GEPIA database and the UALCAN cancer database, and the prognostic analysis was performed using 100 clinical GC samples. We found that S100A16 is significantly upregulated in GC tissues and closely correlated with poor prognosis in GC patients. Functional studies reveal that S100A16 overexpression triggers GC cells proliferation and migration both in vivo and in vitro; by contrast, S100A16 knockdown restricts the speed of GC cells growth and mobility. Proteomic analysis results reveal a large S100A16 interactome, which includes ZO-2, a master regulator of cell-to-cell tight junctions. Mechanistic assay results indicate that excessive S100A16 instigates GC cell invasion, migration and EMT via ZO-2 inhibition, which arose from S100A16-mediated ZO-2 ubiquitination and degradation. Conclusions: Our results not only reveal that S100A16 is a promising candidate biomarker in GC early diagnosis and prediction of metastasis, but also establish the therapeutic importance of targeting S100A16 in order to prevent ZO-2 loss and suppress GC metastasis and progression.

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.

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