| Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum. | |
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MedLine Citation:
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PMID: 11772399 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sarcolipin (SLN) is a small peptide found in the sarcoplasmic reticulum of skeletal muscle. It is predicted to contain a single hydrophobic transmembrane alpha-helix. Fluorescence emission spectra for the single Trp residue of SLN suggest that SLN incorporates fully into bilayers of dioleoylphosphatidylcholine, but only partially into bilayers of phosphatidylcholines with long (C(22) or C(24)) fatty acyl chains. The fluorescence of SLN is quenched in bilayers of dibromostearoylphosphatidylcholine, also consistent with incorporation into the lipid bilayer. SLN was reconstituted with the Ca(2+)-ATPase of skeletal-muscle sarcoplasmic reticulum. Even at a 50:1 molar ratio of SLN/ATPase, SLN had no significant effect on the rate of ATP hydrolysis by the ATPase or on the Ca(2+)-dependence of ATP hydrolysis. However, at a molar ratio of SLN/ATPase of 2:1 or higher the presence of SLN resulted in a marked decrease in the level of accumulation of Ca(2+) by reconstituted vesicles. The effect of SLN was structurally specific and did not result from a breakdown in the vesicular structure or from the formation of non-specific ion channels. Vesicles were impermeable to Ca(2+) in the absence of ATP in the external medium. The effects of SLN on accumulation of Ca(2+) can be simulated assuming that SLN increases the rate of slippage on the ATPase and the rate of passive leak of Ca(2+) mediated by the ATPase. It is suggested that the presence of SLN could be important in non-shivering thermogenesis, a process in which heat is generated by hydrolysis of ATP by skeletal-muscle sarcoplasmic reticulum. |
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Authors:
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Wendy S Smith; Robert Broadbridge; J Malcolm East; Anthony G Lee |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: The Biochemical journal Volume: 361 ISSN: 0264-6021 ISO Abbreviation: Biochem. J. Publication Date: 2002 Jan |
Date Detail:
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Created Date: 2002-01-04 Completed Date: 2002-02-14 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2984726R Medline TA: Biochem J Country: England |
Other Details:
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Languages: eng Pagination: 277-86 Citation Subset: IM |
Affiliation:
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Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Southampton SO16 7PX, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphate
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metabolism* Amino Acid Sequence Animals Calcium / metabolism* Calcium-Transporting ATPases / metabolism* Hydrolysis Lipid Bilayers Molecular Sequence Data Muscle Proteins / metabolism* Muscle, Skeletal / enzymology* Proteolipids / metabolism* Rabbits Sarcoplasmic Reticulum / enzymology* Spectrometry, Fluorescence |
| Chemical | |
Reg. No./Substance:
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0/Lipid Bilayers; 0/Muscle Proteins; 0/Proteolipids; 145018-73-1/sarcolipin; 56-65-5/Adenosine Triphosphate; 7440-70-2/Calcium; EC 3.6.1.8/Calcium-Transporting ATPases |
| Comments/Corrections | |
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