Linked Life Data

16309849

Source:http://linkedlifedata.com/resource/pubmed/id/16309849

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-1-10
pubmed:abstractText
The molecular mechanism responsible for obesity-associated insulin resistance has been partially clarified: increased fatty acid levels in muscle fibers promote diacylglycerol synthesis, which activates certain isoforms of protein kinase C (PKC). This in turn triggers a kinase cascade which activates both IkappaB kinase-beta (IKK-beta) and c-Jun N-terminal kinase (JNK), each of which can phosphorylate a key serine residue in IRS-1, rendering it a poor substrate for the activated insulin receptor. Heat shock proteins Hsp27 and Hsp72 have the potential to prevent the activation of IKK-beta and JNK, respectively; this suggests that induction of heat shock proteins may blunt the adverse impact of fat overexposure on insulin function. Indeed, bimoclomol--a heat shock protein co-inducer being developed for treatment of diabetic neuropathy--and lipoic acid--suspected to be a heat shock protein inducer--have each demonstrated favorable effects on the insulin sensitivity of obese rodents, and parenteral lipoic acid is reported to improve the insulin sensitivity of type 2 diabetics. Moreover, there is reason to believe that heat shock protein induction may have a favorable impact on the microvascular complications of diabetes, and on the increased risk for macrovascular disease associated with diabetes and insulin resistance syndrome. Heat shock protein induction may also have potential for preventing or treating neurodegenerative disorders, controlling inflammation, and possibly even slowing the aging process. The possible complementarity of bimoclomol and lipoic acid for heat shock protein induction should be assessed, and further efforts to identify well-tolerated agents active in this regard are warranted.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/HSP27 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP72 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSPB1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Imides, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase 4, http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C, http://linkedlifedata.com/resource/pubmed/chemical/Pyridines, http://linkedlifedata.com/resource/pubmed/chemical/Thioctic Acid, http://linkedlifedata.com/resource/pubmed/chemical/bimoclomol
pubmed:status
MEDLINE
pubmed:issn
0306-9877
pubmed:author
pubmed:issnType
Print
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
527-34
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Induction of heat shock proteins may combat insulin resistance.
pubmed:affiliation
Natural Alternatives International, 1185 Linda Vista Dr., San Marcos, CA 92078, USA. mccarty@pantox.com
pubmed:publicationType
Journal Article