scholarly journals Effect of monovalent ion binding on molecular dynamics of the S100‐family calcium‐binding protein calbindin D 9k

2019 ◽  
Vol 40 (22) ◽  
pp. 1936-1945
Author(s):  
Mahendra Thapa ◽  
Eric Johnson ◽  
Mark Rance
Keyword(s):  
Molecular Dynamics ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Ion Binding ◽  
S100 Family ◽  
Monovalent Ion ◽  
Calbindin D

Ontogeny of the calcium binding protein calbindin D-28k in the rat nervous system

1987 ◽  
Vol 177 (1) ◽  
pp. 15-28 ◽  
Author(s):  
Susann Enderlin ◽  
A. W. Norman ◽  
Marco R. Celio
Keyword(s):  
Nervous System ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Calbindin D

Endocrine control of plasma concentrations of calcium-binding protein in the pig

1987 ◽  
Vol 115 (1) ◽  
pp. 121-128
Author(s):  
E. M. W. Maunder ◽  
A. V. Pillay ◽  
A. D. Care
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Plasma Concentrations ◽  
Significant Rise ◽  
Calcium Binding Protein ◽  
Adrenergic Stimulation ◽  
Adrenergic Agonist ◽  
Endocrine Control ◽  
Adrenergic Blocker ◽  
Calbindin D

ABSTRACT The aetiology of the rise in plasma calbindin-D9k (vitamin D-induced calcium-binding protein; CaBP), following insulin-induced hypoglycaemia, was studied in the pig. ACTH led to a rise in plasma concentrations of both CaBP and cortisol. Metyrapone, which blocks cortisol synthesis, abolished the increases in plasma concentrations of CaBP and cortisol normally observed in response to insulin-induced hypoglycaemia. However, there was no significant rise in plasma concentrations of CaBP in response to pharmacological or physiological doses of cortisol. Injection of clonidine, an α2-adrenergic agonist, led to a rise in plasma concentrations of CaBP, whereas phenylephrine, an α1-adrenergic agonist, tended to exert an inhibitory effect. Also, administration of phentolamine (an α-adrenergic blocker) before injection of insulin abolished the usual increase in plasma concentrations of CaBP, whereas propranolol (a β-adrenergic blocker) enhanced the normal increase in plasma concentrations of CaBP in response to insulin-induced hypoglycaemia. Isoproterenol, a β-adrenergic agonist, was without effect on plasma CaBP. Neither GH nor glucagon appear to be involved in the rise in plasma CaBP following insulin-induced hypoglycaemia. Although atropine abolished the effect of acute hypoglycaemia on plasma CaBP, carbamylcholine was without effect on plasma CaBP concentration. It is concluded that the increases in plasma CaBP induced by either ACTH or α2-adrenergic stimulation may be interrelated since the administration of ACTH can lead to raised plasma concentrations of catecholamines. J. Endocr. (1987) 115, 121–128

scholarly journals The Calcium Binding Protein S100A11 and Its Roles in Diseases

2021 ◽  
Vol 9 ◽  
Author(s):  
Linqiang Zhang ◽  
Tingting Zhu ◽  
Huilai Miao ◽  
Bin Liang
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Biological Activities ◽  
Neurological Diseases ◽  
Structural Features ◽  
Calcium Binding Protein ◽  
S100 Family ◽  
Helix Loop Helix ◽  
Ef Hand ◽  
External Stimuli

The calcium binding protein S100 family in humans contains 21 known members, with each possessing a molecular weight between 10 and 14 kDa. These proteins are characterized by a unique helix-loop-helix EF hand motif, and often form dimers and multimers. The S100 family mainly exists in vertebrates and exerts its biological functions both inside cells as a calcium sensor/binding protein, as well as outside cells. S100A11, a member of the S100 family, may mediate signal transduction in response to internal or external stimuli and it plays various roles in different diseases such as cancers, metabolic disease, neurological diseases, and vascular calcification. In addition, it can function as chemotactic agent in inflammatory disease. In this review, we first detail the discovery of S100 proteins and their structural features, and then specifically focus on the tissue and organ expression of S100A11. We also summarize its biological activities and roles in different disease and signaling pathways, providing an overview of S100A11 research thus far.

scholarly journals The 28-kDa calbindin-D is a major calcium-binding protein in the basilar papilla of the chick.

1988 ◽  
Vol 85 (10) ◽  
pp. 3387-3390 ◽  
Author(s):  
J. C. Oberholtzer ◽  
C. Buettger ◽  
M. C. Summers ◽  
F. M. Matschinsky
Keyword(s):  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Basilar Papilla ◽  
Calbindin D
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