Document Detail


Cyclen-hybrid compound captures copper to protect INS-1 cells from islet amyloid polypeptide cytotoxicity by inhibiting and lysing effects.
MedLine Citation:
PMID:  20856987     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Human islet amyloid polypeptide (hIAPP) deposit is the hallmark of type 2 diabetes pathology. Here, we report that apo-cyclen, attached to a specific hIAPP recognition motif (NYGAIL), captured copper ions and became proteolytically active. This cyclen-NYGAIL-copper complex was able to interfere with hIAPP aggregation and cleave hIAPP. These activities rescued INS-1 cells from hIAPP induced cytotoxicity.
Authors:
Jia Hu; Ye-Ping Yu; Wei Cui; Chuan-Lin Fang; Wei-Hui Wu; Yu-Fen Zhao; Yan-Mei Li
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-09-21
Journal Detail:
Title:  Chemical communications (Cambridge, England)     Volume:  46     ISSN:  1364-548X     ISO Abbreviation:  Chem. Commun. (Camb.)     Publication Date:  2010 Nov 
Date Detail:
Created Date:  2010-10-21     Completed Date:  2011-02-01     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9610838     Medline TA:  Chem Commun (Camb)     Country:  England    
Other Details:
Languages:  eng     Pagination:  8023-5     Citation Subset:  IM    
Affiliation:
Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084, China.
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MeSH Terms
Descriptor/Qualifier:
Cell Line
Copper / chemistry*
Heterocyclic Compounds / chemistry*
Humans
Islet Amyloid Polypeptide / toxicity*
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical
Reg. No./Substance:
0/Heterocyclic Compounds; 0/Islet Amyloid Polypeptide; 294-90-6/cyclen; 7440-50-8/Copper

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


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