Available online 9 June 2015
Invited Review
The beneficial role of curcumin on inflammation, diabetes and neurodegenerative disease: A recent update
Highlights
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- Antioxidant properties, metabolism and bioavailability of curcumin
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- Effect of curcumin on Alzheimer disease and diabetes
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- Anti-inflammatory effect of curcumin
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- Effect of curcumin on cellular signalling pathways
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- Some recent clinical trials with curcumin
Abstract
The
concept of using phytochemicals has ushered in a new revolution in
pharmaceuticals. Naturally occurring polyphenols (like curcumin, morin,
resveratrol, etc.) have gained importance because of their minimal side
effects, low cost and abundance. Curcumin (diferuloylmethane) is a
component of turmeric isolated from the rhizome of Curcuma longa.
Research for more than two decades has revealed the pleiotropic nature
of the biological effects of this molecule. More than 7000 published
articles have shed light on the various aspects of curcumin including
its antioxidant, hypoglycemic, anti-inflammatory and anti-cancer
activities. Apart from these well-known activities, this natural
polyphenolic compound also exerts its beneficial effects by modulating
different signalling molecules including transcription factors,
chemokines, cytokines, tumour suppressor genes, adhesion molecules,
microRNAs, etc. Oxidative stress and inflammation play a pivotal role in
various diseases like diabetes, cancer, arthritis, Alzheimer’s disease
and cardiovascular diseases. Curcumin, therefore, could be a therapeutic
option for the treatment of these diseases, provided limitations in its
oral bioavailability can be overcome. The current review provides an
updated overview of the metabolism and mechanism of action of curcumin
in various organ pathophysiologies. The review also discusses the
potential for multifunctional therapeutic application of curcumin and
its recent progress in clinical biology.
Keywords
- curcumin;
- antioxidant;
- inflammation;
- diabetes;
- neurodegenerative disease;
- cancer
Abbreviations
- ROS, Reactive Oxygen Species;
- DPPH, 2,2-diphenyl-1-picrylhydrazyl;
- ABTS, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid);
- Aβ, Amyloid beta;
- IL-1β, Interleukin 1beta;
- ICAM, intracellular cell adhesion molecule1;
- VCAM, vascular cell adhesion molecule;
- LPS, lipopoly saccharide;
- MCP1, Monocyte chemo attractant protein 1;
- PGE2,, Prostaglandin E2;
- iNOS, inducible nitric oxide synthase;
- TNFα, Tumour necrosis factor alpha;
- TLR, Toll like receptor;
- BACE1, Beta-site AAP cleaving enzyme 1;
- IL-12, 8, 5, 18, interleukin 12, 8, 5, 18;
- MIP1α, Monocyte inflammatory protein 1 alpha;
- COX-2, Cyclooxygenase 2;
- AMPK, 5' adenosine monophosphate-activated protein kinase;
- ELAM1, endothelial-leukocyte adhesion molecule1;
- LOX, lipooxygenase;
- HUVEC, Human umbilical vein endothelial cells;
- NO, nitric oxide;
- COX, cyclooxygenase1;
- VEGF, vascular endothelial growth factor;
- TGFβ1, Transforming growth factor β1;
- CRP, C-reactive protein;
- VSMC, Vascular smooth muscle cells;
- SOCS1, suppressor of cytokine signaling proteins;
- PARP, poly (ADP-ribose) polymerase 1;
- HIF, Hypoxia inducing factor1;
- AIF, Apoptosis inducing factor;
- ATF4, Activating transcription factor 1;
- XBP1, X-box binding protein1;
- PERK, PKR like ER kinase;
- GADD153, Growth arrest and DNA damage inducible
- Corresponding author. Bose Institute, P-1/12, CIT Scheme VII M, Calcutta-700054, West Bengal, INDIA, , Tel.:
+9133 25693243; fax: +9133 2355 3886.
- 1
- Both the authors contributed equally to the work.
Copyright © 2015 Published by Elsevier Ltd.
