dc.contributor.author |
Watson, RN |
|
dc.contributor.author |
Loomes, KM |
|
dc.contributor.author |
Leonard, BL |
|
dc.contributor.author |
Whiting, L |
|
dc.contributor.author |
Hay, DL |
|
dc.contributor.author |
Xu, LY |
|
dc.contributor.author |
Kraegen, EW |
|
dc.contributor.author |
Phillips, ARJ |
|
dc.contributor.author |
Cooper, GJS |
|
dc.coverage.spatial |
United States |
|
dc.date.accessioned |
2022-06-21T23:38:09Z |
|
dc.date.available |
2022-06-21T23:38:09Z |
|
dc.date.issued |
2008 |
|
dc.identifier.citation |
(2008). Endocrinology, 149(1), 154-160. |
|
dc.identifier.issn |
0013-7227 |
|
dc.identifier.uri |
https://hdl.handle.net/2292/60061 |
|
dc.description.abstract |
Alpha-calcitonin gene-related peptide (alphaCGRP) is released mainly from sensory and motor nerves in response to physiological stimuli. Despite well-documented pharmacological effects, its primary physiological role has thus far remained obscure. Increased lipid content, particularly in skeletal muscle and liver, is strongly implicated in the pathogenesis of insulin resistance, but the physiological regulation of organ lipid is imperfectly understood. Here we report our systematic investigations of the effects of alphaCGRP on in vitro and in vivo indices of lipid metabolism. In rodents, levels of alphaCGRP similar to those in the blood markedly stimulated fatty acid beta-oxidation and evoked concomitant mobilization of muscle lipid via receptor-mediated activation of muscle lipolysis. alphaCGRP exerted potent in vivo effects on lipid metabolism in muscle, liver, and the blood via receptor-mediated pathways. Studies with receptor antagonists were consistent with tonic regulation of lipid metabolism by an endogenous CGRP agonist. These data reveal that alphaCGRP is a newly recognized regulator of lipid availability and utilization in key tissues and that it may elevate the availability of intramyocellular free fatty acids to meet muscle energy requirements generated by contraction by evoking their release from endogenous triglyceride. |
|
dc.format.medium |
Print-Electronic |
|
dc.language |
eng |
|
dc.publisher |
The Endocrine Society |
|
dc.relation.ispartofseries |
Endocrinology |
|
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
|
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
|
dc.subject |
Muscle, Skeletal |
|
dc.subject |
Animals |
|
dc.subject |
Rats |
|
dc.subject |
Rats, Wistar |
|
dc.subject |
Multienzyme Complexes |
|
dc.subject |
Fatty Acids |
|
dc.subject |
Calcitonin Gene-Related Peptide |
|
dc.subject |
Receptors, Calcitonin Gene-Related Peptide |
|
dc.subject |
Cyclic AMP |
|
dc.subject |
Neurotransmitter Agents |
|
dc.subject |
Oxidation-Reduction |
|
dc.subject |
Lipolysis |
|
dc.subject |
Phosphorylation |
|
dc.subject |
Male |
|
dc.subject |
Lipid Metabolism |
|
dc.subject |
AMP-Activated Protein Kinases |
|
dc.subject |
Protein Serine-Threonine Kinases |
|
dc.subject |
Nutrition |
|
dc.subject |
Liver Disease |
|
dc.subject |
Digestive Diseases |
|
dc.subject |
2.1 Biological and endogenous factors |
|
dc.subject |
Metabolic and endocrine |
|
dc.subject |
Science & Technology |
|
dc.subject |
Life Sciences & Biomedicine |
|
dc.subject |
Endocrinology & Metabolism |
|
dc.subject |
ACTIVATED PROTEIN-KINASE |
|
dc.subject |
FATTY-ACID OXIDATION |
|
dc.subject |
SKELETAL-MUSCLE |
|
dc.subject |
INSULIN-RESISTANCE |
|
dc.subject |
AMYLIN |
|
dc.subject |
CGRP |
|
dc.subject |
RAT |
|
dc.subject |
METABOLISM |
|
dc.subject |
RECEPTOR |
|
dc.subject |
Protein-Serine-Threonine Kinases |
|
dc.subject |
1116 Medical Physiology |
|
dc.subject |
1103 Clinical Sciences |
|
dc.subject |
Biomedical |
|
dc.subject |
Basic Science |
|
dc.subject |
06 Biological Sciences |
|
dc.subject |
07 Agricultural and Veterinary Sciences |
|
dc.subject |
11 Medical and Health Sciences |
|
dc.title |
Evidence that alpha calcitonin gene-related peptide is a neurohormone that regulates systemic lipid availability and utilization |
|
dc.type |
Journal Article |
|
dc.identifier.doi |
10.1210/en.2007-0583 |
|
pubs.issue |
1 |
|
pubs.begin-page |
154 |
|
pubs.volume |
149 |
|
dc.date.updated |
2022-05-03T04:50:33Z |
|
dc.rights.holder |
Copyright: The author |
en |
dc.identifier.pmid |
17932220 (pubmed) |
|
pubs.author-url |
https://www.ncbi.nlm.nih.gov/pubmed/17932220 |
|
pubs.end-page |
160 |
|
pubs.publication-status |
Published |
|
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
|
pubs.elements-id |
73605 |
|
pubs.org-id |
Science |
|
pubs.org-id |
Biological Sciences |
|
pubs.org-id |
Science Research |
|
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
|
dc.identifier.eissn |
1945-7170 |
|
dc.identifier.pii |
en.2007-0583 |
|
pubs.record-created-at-source-date |
2022-05-03 |
|
pubs.online-publication-date |
2007-10-11 |
|