scholarly journals Increased Susceptibility to Isoproterenol-Induced Cardiac Hypertrophy and Impaired Weight Gain in Mice Lacking the Histidine-Rich Calcium-Binding Protein

2006 ◽  
Vol 26 (24) ◽  
pp. 9315-9326 ◽  
Author(s):  
Eric J. Jaehnig ◽  
Analeah B. Heidt ◽  
Stephanie B. Greene ◽  
Ivo Cornelissen ◽  
Brian L. Black
Keyword(s):  
Weight Gain ◽  
Cardiac Hypertrophy ◽  
Knockout Mice ◽  
Calcium Binding ◽  
Calcium Release ◽  
Binding Protein ◽  
Critical Role ◽  
Calcium Binding Protein ◽  
Calcium Handling

ABSTRACT The sarcoplasmic reticulum (SR) plays a critical role in excitation-contraction coupling by regulating the cytoplasmic calcium concentration of striated muscle. The histidine-rich calcium-binding protein (HRCBP) is expressed in the junctional SR, the site of calcium release from the SR. HRCBP is expressed exclusively in muscle tissues and binds calcium with low affinity and high capacity. In addition, HRCBP interacts with triadin, a protein associated with the ryanodine receptor and thought to be involved in calcium release. Its calcium binding properties, localization to the SR, and interaction with triadin suggest that HRCBP is involved in calcium handling by the SR. To determine the function of HRCBP in vivo, we inactivated HRC, the gene encoding HRCBP, in mice. HRC knockout mice exhibited impaired weight gain beginning at 11 months of age, which was marked by reduced skeletal muscle and fat mass, and triadin protein expression was upregulated in the heart of HRC knockout mice. In addition, HRC null mice displayed a significantly exaggerated response to the induction of cardiac hypertrophy by isoproterenol compared to their wild-type littermates. The exaggerated response of HRC knockout mice to the induction of cardiac hypertrophy is consistent with a regulatory role for HRCBP in calcium handling in vivo and suggests that mutations in HRC, in combination with other genetic or environmental factors, might contribute to pathological hypertrophy and heart failure.

Calcium absorption and intestinal calcium-binding protein: quantitative relationship.

1979 ◽  
Vol 236 (5) ◽  
pp. E556 ◽  
Author(s):  
J J Feher ◽  
R H Wasserman
Keyword(s):  
Vitamin D ◽  
Vitamin D3 ◽  
Calcium Binding ◽  
Calcium Absorption ◽  
Binding Protein ◽  
Quantitative Relationship ◽  
Calcium Binding Protein ◽  
Vitamin D Status ◽  
Loop Technique

The concentration of the vitamin D-induced calcium-binding protein (CaBP) and calcium absorption from the duodenum were investigated in chicks with an in vivo ligated-loop technique. The relation between CaBP and calcium absorption was dependent on a) source of vitamin D activity (either vitamin D3 or 1,25-dihydroxycholecalciferol); b) dosage of vitamin D3; c) time after administration of vitamin D3 to rachitic animals. To aid in the interpretation of these results, a phenomenological model was developed in which CaBP was viewed as being linearly related to a portion of calcium absorption. The model, when applied to the data, suggests that there is a "nonfunctional" pool of CaBP the size of which is determined by the vitamin D status of the animal. After correction for this nonfunctional pool, the proportionality between CaBP and calcium absorption is independent of the vitamin D status of the animal.

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.

scholarly journals Ablation of Histidine-Rich Calcium Binding Protein (HRC) Results in Severe Cardiac Hypertrophy and Dysfunction in Pressure Overload Model

2012 ◽  
Vol 102 (3) ◽  
pp. 555a
Author(s):  
Chang Sik Park ◽  
Hyeseon Cha ◽  
Sora Jin ◽  
Woo Jin Park ◽  
Jung Hee Cho ◽  
...  
Keyword(s):  
Cardiac Hypertrophy ◽  
Calcium Binding ◽  
Binding Protein ◽  
Pressure Overload ◽  
Calcium Binding Protein

scholarly journals Calcium Binding Protein S100A16 Expedites Proliferation, Invasion and Epithelial-Mesenchymal Transition Process in Gastric Cancer

2021 ◽  
Vol 9 ◽  
Author(s):  
Xiaoying You ◽  
Min Li ◽  
Hongwei Cai ◽  
Wenwen Zhang ◽  
Ye Hong ◽  
...  
Keyword(s):  
Gastric Cancer ◽  
Calcium Binding ◽  
Epithelial Mesenchymal Transition ◽  
Malignant Tumors ◽  
Binding Protein ◽  
Transition Process ◽  
Calcium Binding Protein ◽  
Mesenchymal Transition

Gastric cancer (GC) is one of the most common malignant tumors of the digestive system, listed as the second cause of cancer-related deaths worldwide. S100 Calcium Binding Protein A16 (S100A16) is an acidic calcium-binding protein associated with several types of tumor progression. However, the function of S100A16 in GC is still not very clear. In this study, we analyzed S100A16 expression with the GEPIA database and the UALCAN cancer database. Meanwhile, 100 clinical GC samples were used for the evaluation of its role in the prognostic analysis. 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 cell proliferation and migration both in vivo and in vitro; by contrast, S100A16 knockdown restricts the speed of GC cell growth and mobility. Proteomic analysis results reveal a large S100A16 interactome, which includes ZO-2 (Zonula Occludens-2), a master regulator of cell-to-cell tight junctions. Mechanistic assay results indicate that excessive S100A16 instigates GC cell invasion, migration, and epithelial-mesenchymal transition (EMT) via ZO-2 inhibition, which arose from S100A16-mediated ZO-2 ubiquitination and degradation. 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 to prevent ZO-2 loss and suppress GC metastasis and progression.

scholarly journals Calcium-binding protein of the chick chorioallantoic membrane. II. Vitamin K-dependent expression

1978 ◽  
Vol 77 (3) ◽  
pp. 752-761 ◽  
Author(s):  
RS Tuan ◽  
WA Scott ◽  
ZA Cohn
Keyword(s):  
Vitamin D ◽  
Vitamin K ◽  
Calcium Binding ◽  
Binding Protein ◽  
Vitamin K Antagonists ◽  
Chorioallantoic Membrane ◽  
Calcium Binding Protein ◽  
Simple Method ◽  
Chick Chorioallantoic Membrane

A simple method was devised for the maintenance of the chorioallantoic membrane (CAM) of chick embryos in organ culture. Explants of CAM survived for up to 5 days in this system and retained the characteristic three-layered morphology (ectoderm, mesoderm, and endoderm). Induction of the CAM calcium-binding protein (CaBP) by effectors of calcium metabolism was studied in these organ cultures. Vitamin K was found to elicit a seven- to eightfold increase in CaBP, whereas no increase in CaBP activity occurred on supplementation with vitamin A, parathyroid hormone, an analogue of vitamin D, vitamin D and its hydroxylated metabolites, or with elevated calcium levels. The vitamin K-mediated induction of CaBP was dose-dependent, inhibited by the vitamin K antagonists warfarin and dicoumarol, selective for vitamin K5, and maximal at the developmental stage (13-15 days of incubation) corresponding to the onset of calcium transport by the CAM in vivo. CaBP levels increased after 60-70 h in cultures of 13-15 day CAM supplemented with vitamin K and reached maximal levels around 80-90 h of culture. The CAM ectoderm underwent extensive proliferation and often assumed a villuslike morphology in the vitamin K cultures.

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