| Anti-apoptotic activity of hemagglutinin-33 and botulinum neurotoxin and its implications to therapeutic and countermeasure issues. | |
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MedLine Citation:
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PMID: 22182409 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Botulinum neurotoxins (BoNTs), produced by Clostridium botulinum are the most toxic substances known to the mankind. BoNTs (seven serotypes, A-G) are produced along with a group of neurotoxin associated proteins (NAPs) in a physiologically coordinated manner, regulated by a common transcription factor for the gene cluster that encodes for the BoNT and NAPs. Hemagglutinin-33 (Hn-33) is a 33kDa subcomponent of NAPs, which is resistant to protease digestion, and accounts for about half of the NAPs molecules in the BoNT/A complex. Natural exposures to BoNT in food poisoning cases as well as in the medical applications of BoNT as a therapeutic agent, humans are exposed to the BoNT/A complex. The toxin itself is known to block neurotransmitter release from presynaptic nerves, but the effect of NAPs is unexplored. In this article, we report an important observation of the anti-apoptotic effect of Hn-33 in Hn-33-preincubated human neuroblastoma SH-SY5Y cells. Activity of caspases, which are the central executioners of apoptosis, was substantially (78%) reduced by Hn-33. Degradation of chromosomal DNA, another biochemical hallmark of apoptosis, was blocked in Hn-33 incubated SH-SY5Y cells. Interestingly, purified BoNT/A also showed substantial anti-apoptotic activity. These findings may have significant implications to the use of BoNT as a therapeutic agent, and to devise counter measures to botulinum poisoning. |
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Authors:
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Raj Kumar; Yu Zhou; Koyel Ghosal; Shuowei Cai; Bal Ram Singh |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-12-11 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: - ISSN: 1090-2104 ISO Abbreviation: - Publication Date: 2011 Dec |
Date Detail:
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Created Date: 2011-12-20 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Inc. |
Affiliation:
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Department of Chemistry and Biochemistry, The Botulinum Research Center, University of Massachusetts Dartmouth, North Dartmouth, MA 02747, United States. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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