Document Detail


How do presynaptic PLA2 neurotoxins block nerve terminals?
MedLine Citation:
PMID:  10838563     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Snake presynaptic neurotoxins with phospholipase A2 activity block nerve terminals in an unknown way. Here, we propose that they enter the lumen of synaptic vesicles following endocytosis and hydrolyse phospholipids of the inner leaflet of the membrane. The transmembrane pH gradient drives the translocation of fatty acids to the cytosolic monolayer, leaving lysophospholipids on the lumenal layer. Such vesicles are highly fusogenic and release neurotransmitter upon fusion with the presynaptic membrane, but cannot be retrieved because of the high local concentration of fatty acids and lysophospholipids, which prevents vesicle neck closure.
Authors:
C Montecucco; O Rossetto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Trends in biochemical sciences     Volume:  25     ISSN:  0968-0004     ISO Abbreviation:  Trends Biochem. Sci.     Publication Date:  2000 Jun 
Date Detail:
Created Date:  2000-07-21     Completed Date:  2000-07-21     Revised Date:  2012-02-22    
Medline Journal Info:
Nlm Unique ID:  7610674     Medline TA:  Trends Biochem Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  266-70     Citation Subset:  IM    
Affiliation:
Centro CNR Biomembrane and Dipartimento di Scienze Biomediche, Università di Padova, Via G. Colombo 3, 35121 Padova, Italy. cesare@civ.bio.unipd.it
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MeSH Terms
Descriptor/Qualifier:
Elapid Venoms / toxicity
Models, Biological
Nerve Endings / drug effects
Neurons / drug effects*
Neurotoxins / toxicity*
Neurotransmitter Agents / metabolism
Phospholipases A / metabolism*
Phospholipases A2
Snake Venoms / metabolism*
Synapses / metabolism
Time Factors
Grant Support
ID/Acronym/Agency:
1068//Telethon
Chemical
Reg. No./Substance:
0/Elapid Venoms; 0/Neurotoxins; 0/Neurotransmitter Agents; 0/Snake Venoms; 52019-39-3/taipoxin; 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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