The Effects of Curcumin on Serum Heat Shock Protein 27 Antibody Titers in Patients with Metabolic Syndrome.

08:00 EDT 29th June 2018 | BioPortfolio

Summary of "The Effects of Curcumin on Serum Heat Shock Protein 27 Antibody Titers in Patients with Metabolic Syndrome."

Metabolic syndrome (MetS) is associated with an increased risk of cardiovascular disease and diabetes mellitus. Inflammation and oxidant stress are features of MetS that can enhance the expression and release of heat shock proteins (Hsps), including the small heat shock protein, Hsp 27, and that may subsequently lead to the production of Hsp27 antibodies (anti-Hsp 27). Curcumin is an anti-inflammatory and antioxidant phytochemical that may ameliorate these features of MetS. We investigated the effects of unformulated curcumin and phospholipidated curcumin on antibody titers to heat shock protein 27 (anti-Hsp 27) in patients with MetS. A randomized double-blind, placebo-controlled clinical trial design was used in 120 patients with MetS (diagnosed according to the International Diabetes Federation [IDF] criteria). Participants were randomly allocated to 3 groups, with 40 individuals per group, that received either 1 g/d curcumin, phospholipidated curcumin, or a placebo for 6 weeks. The changes in serum concentrations of anti-Hsp 27 did not differ significantly between study groups (p = .283). There was no significant difference between baseline and end-of-trial concentrations of anti-Hsp 27 in groups supplemented with curcumin (p = .177), phospholipidated curcumin (p = .798), or placebo (p = .663). Curcumin supplementation (1 g/d) has no significant effects on anti-Hsp 27 titers in patients with MetS.


Journal Details

This article was published in the following journal.

Name: Journal of dietary supplements
ISSN: 1939-022X
Pages: 1-10


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Medical and Biotech [MESH] Definitions

A family of heat-shock proteins that contain a 70 amino-acid consensus sequence known as the J domain. The J domain of HSP40 heat shock proteins interacts with HSP70 HEAT-SHOCK PROTEINS. HSP40 heat-shock proteins play a role in regulating the ADENOSINE TRIPHOSPHATASES activity of HSP70 heat-shock proteins.

A subfamily of small heat-shock proteins that are closely related to ALPHA B-CRYSTALLIN. Hsp20 heat-shock proteins can undergo PHOSPHORYLATION by CYCLIC GMP-DEPENDENT PROTEIN KINASES.

Stress-inducible members of the heat-shock proteins 70 family. HSP72 heat shock proteins function with other MOLECULAR CHAPERONES to mediate PROTEIN FOLDING and to stabilize pre-existent proteins against aggregation.

A group of eukaryotic high-molecular mass heat-shock proteins that represent a subfamily of HSP70 HEAT-SHOCK PROTEINS. Hsp110 proteins prevent protein aggregation and can maintain denatured proteins in folding-competent states.

Heat and cold stress-inducible, transcription factors that bind to inverted 5'-NGAAN-3' pentamer DNA sequences and are regulated by poly(ADP) ribosylation. They play essential roles as transcriptional activators of the HEAT-SHOCK RESPONSE by inducing expression of large classes of MOLECULAR CHAPERONES and heat-shock proteins. They also function in DNA REPAIR; transcriptional reactivation of latent HIV-1; and pre-mRNA processing and nuclear export of HSP70 HEAT-SHOCK PROTEINS during heat stress.

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