Abstract
p38 mitogen-activated protein kinases (p38 MAPK, p38) consist of 4 subunits: p38α, p38β, p38γ and p38δ. They play a well-recognized role in regulating intracellular signaling transduction in mammalian cells. p38 MAPK induces a variety of intracellular responses associated with neuropathic pain and other chronic pain. Thus, specific targeting p38 MAPK molecule and its signaling pathway represent potential therapeutic strategies for pain management. Based on the understanding of the crystal structure, biological functions and its signaling pathway of p38 MAPK, chemically synthesized p38 MAPK inhibitors have become available. Natural products and biological components may also serve as potential p38 MAPK inhibitors. To this end, we will evaluate their potential for chronic pain management.
Keywords: Chronic pain, inhibitors, p38 MAPK, signaling pathway, structure.
Current Medicinal Chemistry
Title:p38 MAPK: A Potential Target of Chronic Pain
Volume: 21 Issue: 38
Author(s): X. Lin, M. Wang, J. Zhang and R. Xu
Affiliation:
Keywords: Chronic pain, inhibitors, p38 MAPK, signaling pathway, structure.
Abstract: p38 mitogen-activated protein kinases (p38 MAPK, p38) consist of 4 subunits: p38α, p38β, p38γ and p38δ. They play a well-recognized role in regulating intracellular signaling transduction in mammalian cells. p38 MAPK induces a variety of intracellular responses associated with neuropathic pain and other chronic pain. Thus, specific targeting p38 MAPK molecule and its signaling pathway represent potential therapeutic strategies for pain management. Based on the understanding of the crystal structure, biological functions and its signaling pathway of p38 MAPK, chemically synthesized p38 MAPK inhibitors have become available. Natural products and biological components may also serve as potential p38 MAPK inhibitors. To this end, we will evaluate their potential for chronic pain management.
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Cite this article as:
Lin X., Wang M., Zhang J. and Xu R., p38 MAPK: A Potential Target of Chronic Pain, Current Medicinal Chemistry 2014; 21 (38) . https://dx.doi.org/10.2174/0929867321666140915143040
DOI https://dx.doi.org/10.2174/0929867321666140915143040 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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