Apoptosis-Inducing Activity of the S100A8/A9 Heterodimer

ISSN: 1875-614X (Online)
ISSN: 1871-5230 (Print)


Volume 15, 3 Issues, 2016


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Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry

Formerly: Current Medicinal Chemistry - Anti-Inflammatory and Anti-Allergy Agents

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Editor-in-Chief:
Claudiu T. Supuran
Neurofarba Department
University of Florence
Florence
Italy


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Apoptosis-Inducing Activity of the S100A8/A9 Heterodimer



Anti-Inflammatory & Anti-Allergy Agents in Medicinal Chemistry, 8(4): 318-328.

Author(s): Mohammad Hashemi, Seth Chitayat, Sudharsana Rao Ande and Walter J Chazin.

Affiliation: Clinical Biochemistry, Department of Clinical Biochemistry, School of Medicine, Zahedan University of Medical Sciences, Zahedan, I.R. Iran.

Abstract

The S100A8/S100A9 heterodimer, commonly referred to as calprotectin (CP), is a member of the S100 subfamily of EF-hand calcium binding proteins that is largely expressed in activated monocytes and macrophages and has well-defined functions in acute and chronic inflammation. Indeed, certain S100 proteins including S100A8/A9 are exported from cells by an as-yet unknown mechanism. Once outside the cell, S100A8/A9 activates cell surface receptors such as the receptor for advanced glycation end products (RAGE) and has also been shown to inhibit the growth of pathogenic bacteria through the chelation of trace metal ions such as zinc (Zn2+) and manganese (Mn2+). The binding of these metal ions by S100A8/A9 has also been shown to induce apoptosis in various tumor cell lines. However, several lines of evidence have suggested that S100A8/A9-dependent apoptosis is not solely due to its ability to sequester Zn2+ from cells. Rather, it appears that trace metal binding to S100A8/A9 triggers a novel conformational switch in the protein, which promotes binding to specific sites on the surface of cells or through interaction with yet unidentified cell surface receptors. This review summarizes what is currently known regarding the molecular mechanisms by which S100A8/A9 performs its role as a novel apoptotic agent.

Keywords:

S100A8/A9, calprotectin, apoptosis, zinc.



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Article Details

Volume: 8
Issue Number: 4
First Page: 318
Last Page: 328
Page Count: 11
DOI: 10.2174/187152309789838993
Price: $58
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