Document Detail


Binding of spin-labeled fatty acids and lysophospholipids to hydrophobic region of calmodulin.
MedLine Citation:
PMID:  1663109     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In the presence of bovine brain calmodulin activated by calcium, the sharp triplet electron spin resonance (ESR) lines of free doxyl stearic acids decreased, and the broad resonance lines increased concomitantly, suggesting that the doxyl stearic acids bound to calmodulin calcium-dependently. The bound molecules were displaced by a calmodulin inhibitor, W-7, whereas their nitroxide radicals were hardly reduced by ascorbic acid, suggesting that the spin-labeled fatty acids bind to hydrophobic regions of calmodulin, and consequently inhibit calmodulin-dependent phosphodiesterase activity. These binding characteristics to calmodulin were different from those to bovine serum albumin. Moreover, the ESR spectra of two spin-labeled derivatives of lysophospholipid having a spin-labeled acyl group or a spin-labeled polar head group showed that it is the acyl chain of lysophospholipid that interacts with the hydrophobic region of calmodulin. The interactions of fatty acids and lysophospholipids with calmodulin seem to be quite different from those of acidic phospholipids, described previously [Suzuki, T., Katoh, H., & Uchida, M.K. (1986) Biochim. Biophys. Acta, 873, 379-386]. Thus, from the results of ESR study, we can obtain information on the function of fatty acids and lysophospholipids on calmodulin. Instead of enzyme assay, ESR spectroscopy is a useful means to examine lipid-protein interaction.
Authors:
T Suzuki-Nishimura; M K Uchida
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  110     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1991 Sep 
Date Detail:
Created Date:  1992-02-25     Completed Date:  1992-02-25     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  333-8     Citation Subset:  IM    
Affiliation:
Department of Molecular Pharmacology, Meiji College of Pharmacy, Tokyo.
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MeSH Terms
Descriptor/Qualifier:
Animals
Brain
Calmodulin / chemistry,  metabolism*
Cattle
Cyclic N-Oxides
Electron Spin Resonance Spectroscopy
Lysophospholipids / metabolism*
Protein Binding
Spin Labels* / chemical synthesis
Stearic Acids / metabolism*
Chemical
Reg. No./Substance:
0/Calmodulin; 0/Cyclic N-Oxides; 0/Lysophospholipids; 0/Spin Labels; 0/Stearic Acids; 2564-83-2/TEMPO

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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