| Involvement of a Phosphorylation-Mediated Pathway to Regulate the Function of NSPL1 in Exercise. | |
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MedLine Citation:
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PMID: 21258182 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Skeletal-type neuroendocrine-specific protein like 1 (sk-NSPL1) has been demonstrated to be physiologically important in regulating the membrane translocation of glucose transporter 4 (GLUT4) in skeletal muscles. We investigated the levels of phosphorylation in proteins that are thought to be involved in exercise in wild-type and sk-NSPL1-deficient muscles with specific antibodies and phosphate-metal affinity chromatography resin (p-resin). In both normal skeletal muscle and sk-NSPL1-deficient muscle, adenosine monophosphate (AMP)-dependent kinase (AMPK) and acetyl-CoA carboxylase (ACC) were phosphorylated and adsorbed onto p-resin at high levels after exercise. On the other hand, the effect of 5-aminoimidazole-4-carboxyamide ribonucleoside (AICAR), which is an activator of AMPK, in blood glucose was greatly diminished in mutant mice. P-resin adsorbed sk-NSPL1 in the membrane fraction from wild-type muscle after exercise and AICAR administration. Isolated sk-NSPL1 from wild-type also had increased adsorption onto p-resin after treatment with Ca(2+) and adenosine triphosphate (ATP). After long-term incubation of sk-NSPL1-containing membrane without ATP, sk-NSPL1 adsorption onto anion-exchange resin was drastically reduced. These results suggest that the function of sk-NSPL1 is regulated by a [Ca(2+)](i)- and AMPK-mediated pathway under exercise, and support the hypothesis that sk-NSPL1 is an important factor in the downstream of the exercise-dependent pathway in GLUT4 translocation. |
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Authors:
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Takaaki Ikemoto; Masaaki Suzuki; Hirotaka Onoe |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-1-19 |
Journal Detail:
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Title: The Journal of veterinary medical science / the Japanese Society of Veterinary Science Volume: - ISSN: 0916-7250 ISO Abbreviation: - Publication Date: 2011 Jan |
Date Detail:
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Created Date: 2011-1-24 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9105360 Medline TA: J Vet Med Sci Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Affiliation:
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Functional Probe Research Laboratory, RIKEN Center for Molecular Imaging Science. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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