Document Detail


Modification of substrate inhibition of synaptosomal acetylcholinesterase by cardiotoxins.
MedLine Citation:
PMID:  15469715     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Different types of cardiotoxin (I-V and n) were isolated and purified from the venom of the Taiwan cobra (Naja naja atra). The effects of these cardiotoxins were studied on membrane-bound acetylcholinesterase, which was isolated from a sheep's brain cortex. The results showed that cardiotoxins I-III, V, and n activated the enzyme by modification of substrate inhibition, but cardiotoxin IV's reaction was different. The inhibition and activation of acetylcholinesterase were linked to the functions of the hydrophobicity index, presence of a cationic cluster, and the accessible arginine residue. Our results indicate that Cardiotoxins have neither a cationic cluster nor an arginine residue in their surface area of loop I; therefore, in contrast to fasciculin, cardiotoxins are attached by loop II to the peripheral site of the enzyme. As a result, fasciculin seems to stabilize nonfunctional conformation, but cardiotoxins seem to stabilize the functional conformation of the enzyme. Based on our experimental and theoretical findings, similar secondary and tertiary structures of cardiotoxins and fasciculin seem to have an opposite function once they interact with acetylcholinesterase.
Authors:
Seyed-Omid Ranaei-Siadat; Gholam-Hosein Riazi; Mehdi Sadeghi; Long-Sen Chang; Shinne-Ren Lin; Peyman Eghtesadi-Araghi; Gholam Hossein Hakimelahi; Ali Akbar Moosavi-Movahedi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry and molecular biology     Volume:  37     ISSN:  1225-8687     ISO Abbreviation:  J. Biochem. Mol. Biol.     Publication Date:  2004 May 
Date Detail:
Created Date:  2004-10-07     Completed Date:  2004-11-15     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  9702084     Medline TA:  J Biochem Mol Biol     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  330-8     Citation Subset:  IM    
Affiliation:
Institute of Biotechnology and Biophysics, University of Tehran, Tehran, Iran.
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MeSH Terms
Descriptor/Qualifier:
Acetylcholinesterase / chemistry,  metabolism*
Amino Acid Sequence
Animals
Brain Chemistry
Cerebral Cortex / enzymology
Cobra
Cobra Cardiotoxin Proteins / chemistry,  genetics,  metabolism*
Elapid Venoms / chemistry,  genetics,  metabolism
Enzyme Activation
Molecular Sequence Data
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Alignment
Sheep
Synaptosomes / enzymology*
Chemical
Reg. No./Substance:
0/Cobra Cardiotoxin Proteins; 0/Elapid Venoms; 86697-68-9/fasciculin; EC 3.1.1.7/Acetylcholinesterase

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


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