Document Detail

Effect of spermine on association of protein kinase C with phospholipid vesicles.
MedLine Citation:
PMID:  2250564     Owner:  NLM     Status:  MEDLINE    
The in vitro mechanism by which polyamines affect protein kinase C (PK C) activation process was investigated in a reconstituted system consisting of purified enzyme and phospholipid vesicles of various phosphatidylserine content. It was found that the addition of spermine greatly interferes with the association of PK C to liposomes. This tetramine, at micromolar concentrations, was most potently effective while other polyamines such as spermidine and putrescine were almost ineffective; therefore the modulatory action appeared to be structure specific. The spermine effect is dramatically influenced by the density of the phosphatidylserine present on the liposome, suggesting the complex formation with the acidic component on phospholipid vesicles to be the mechanism by which this polyamine exerts its modulatory action.
M S Moruzzi; M G Monti; G Piccinini; G Marverti; B Tadolini
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Life sciences     Volume:  47     ISSN:  0024-3205     ISO Abbreviation:  Life Sci.     Publication Date:  1990  
Date Detail:
Created Date:  1991-01-16     Completed Date:  1991-01-16     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0375521     Medline TA:  Life Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1475-82     Citation Subset:  IM    
Istituto di Chimica Biologica, Università di Modena, Italy.
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MeSH Terms
Brain / enzymology
Liposomes / metabolism*
Phorbol 12,13-Dibutyrate / metabolism
Phosphatidylcholines / metabolism
Phosphatidylserines / metabolism
Protein Binding
Protein Kinase C / metabolism*
Rats, Inbred Strains
Spermine / pharmacology*
Reg. No./Substance:
0/Liposomes; 0/Phosphatidylcholines; 0/Phosphatidylserines; 37558-16-0/Phorbol 12,13-Dibutyrate; 71-44-3/Spermine; EC Kinase C

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