Document Detail


Effects of sphingosine on peripheral membrane interactions: comparison of adriamycin, cytochrome c, and phospholipase A2.
MedLine Citation:
PMID:  8388718     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
As revealed by resonance energy transfer utilizing pyrene-labeled phosphatidylcholine donor, the mainly electrostatically controlled binding of adriamycin (Adr) and cytochrome c (cyt c) to mixed egg yolk phosphatidic acid/phosphatidylcholine (eggPA/eggPC, 15:85 molar ratio) liposomes was reversed upon the inclusion of increasing contents of sphingosine. At a [sphingosine]/[eggPA] molar ratio of approximately 2:1, the degree of fluorescence quenching by cyt c and Adr was approximately the same as when using liposomes lacking eggPA. Similarly, the increase in the surface pressure of sphingosine/eggPA monolayers on an air/water interface due to the membrane penetration of either cyt c or Adr was progressively reduced by increasing the content of sphingosine in the monolayers. The above critical [sphingosine]/[acidic phospholipid] stoichiometry yielding dissociation of the positively charged ligands Adr or cyt c from membrane acidic phospholipids was shifted from 2:1 to 1:1 upon substituting egg phosphatidylglycerol (eggPG) for eggPA. Accordingly, charge neutralization of the acidic phospholipids by sphingosine could be involved. One eggPA (having maximally two negative charges) appears to require two molecules of sphingosine whereas the maximally singly charged eggPG is neutralized by one sphingosine. For comparison we also studied the effects of sphingosine on the phospholipase A2 catalyzed hydrolysis of the pyrene-labeled acidic alkylacyl phospholipid analog 1-octacosanyl-2-[6-(pyren-1-yl)]hexanoyl-sn-glycero-3- phosphatidylmethanol (C28-O-PHPM) and the corresponding phosphatidylcholine (C28-O-PHPC). In the presence of low Ca2+ concentrations (approximately 50 nM) limiting the rate of the enzymatic reaction, sphingosine gradually inhibited the hydrolysis of phosphatidylcholine, and at 1:6 sphingosine/C28-O-PHPC a nearly complete lack of hydrolysis was evident.(ABSTRACT TRUNCATED AT 250 WORDS)
Authors:
P Mustonen; J Lehtonen; A Kõiv; P K Kinnunen
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  32     ISSN:  0006-2960     ISO Abbreviation:  Biochemistry     Publication Date:  1993 May 
Date Detail:
Created Date:  1993-06-29     Completed Date:  1993-06-29     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  5373-80     Citation Subset:  IM    
Affiliation:
Department of Medical Chemistry, University of Helsinki, Finland.
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MeSH Terms
Descriptor/Qualifier:
Calcium / pharmacology
Cell Membrane / drug effects*,  metabolism
Cytochrome c Group / metabolism*
Doxorubicin / metabolism*
Electrochemistry
Energy Transfer
Hydrolysis
Liposomes / metabolism
Phosphatidic Acids / chemistry,  metabolism
Phosphatidylcholines / metabolism
Phosphatidylglycerols / metabolism
Phospholipases A / metabolism*
Phospholipases A2
Spectrometry, Fluorescence
Sphingosine / pharmacology*
Chemical
Reg. No./Substance:
0/Cytochrome c Group; 0/Liposomes; 0/Phosphatidic Acids; 0/Phosphatidylcholines; 0/Phosphatidylglycerols; 123-78-4/Sphingosine; 23214-92-8/Doxorubicin; 7440-70-2/Calcium; EC 3.1.1.-/Phospholipases A; EC 3.1.1.4/Phospholipases A2

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


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