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.

Differential expression of the EF-hand calcium-binding protein calsensin in the central nervous system of hirudinid leeches

1996 ◽  
Vol 286 (3) ◽  
pp. 357-364 ◽  
Author(s):  
Mark Veldman ◽  
Yueqiao Huang ◽  
John Jellies ◽  
Kristen M. Johansen ◽  
Jørgen Johansen
Keyword(s):  
Central Nervous System ◽  
Nervous System ◽  
Differential Expression ◽  
Calcium Binding ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Ef Hand ◽  
The Central Nervous System

NMR Derived Solution Structure of an EF-Hand Calcium-Binding Protein fromEntamoeba Histolytica†

Biochemistry ◽  
2001 ◽  
Vol 40 (48) ◽  
pp. 14392-14403 ◽  
Author(s):  
H. S. Atreya ◽  
S. C. Sahu ◽  
A. Bhattacharya ◽  
Girjesh Govil
Keyword(s):  
Calcium Binding ◽  
Solution Structure ◽  
Binding Protein ◽  
Calcium Binding Protein ◽  
Ef Hand

scholarly journals Isolation and characterization of grancalcin, a novel 28 kDa EF-hand calcium-binding protein from human neutrophils

1992 ◽  
Vol 286 (2) ◽  
pp. 549-554 ◽  
Author(s):  
C G Teahan ◽  
N F Totty ◽  
A W Segal
Keyword(s):  
Sequence Analysis ◽  
Calcium Binding ◽  
Binding Protein ◽  
Sequence Similarity ◽  
Gel Filtration ◽  
Calcium Binding Protein ◽  
Peptide Sequence ◽  
Human Neutrophils ◽  
Isolation And Characterization ◽  
Ef Hand

A novel 28 kDa protein, which we have named ‘grancalcin’, has been identified in human neutrophils. The protein was isolated from the cytosol and found to be a homodimer, with an apparent molecular mass of 55 kDa on gel filtration. Polyclonal antibodies were raised to the native protein. N-Terminal sequence analysis and tryptic-peptide sequence analysis was performed. The protein exhibits sequence similarity to sorcin, a 24 kDa calcium-binding protein over-expressed in certain multi-drug-resistant cell lines. It appears to be a member of the EF-hand family of calcium-binding proteins. The association of a high proportion of this protein with the membranes and granules in the presence of physiological concentrations of calcium may indicate a role in granule-membrane fusion and degranulation.

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