Document Detail


Mutational analysis of type IV collagen alpha5 chain, with respect to heterotrimer formation.
MedLine Citation:
PMID:  18083113     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Alport syndrome (AS) is caused by mutations in type IV collagen alpha3, alpha4, and alpha5 chains. The three chains form a heterotrimer. In this study, we introduced 12 kinds of missense and three kinds of nonsense mutations, corresponding to AS mutations, into the NC1 domain of alpha5(IV) and characterized the mutant chains. Nine alpha5(IV) chains with amino acid substitutions and all three truncated alpha5(IV) chains did not form a heterotrimer and were not secreted from cells. Three alpha5(IV) chains with amino acid substitutions did, however, form heterotrimers in cells, but these were not secreted from cells. These findings indicate that a defect in heterotrimer formation is the main molecular mechanism underlying the pathogenesis of AS caused by mutation in the NC1 domain. We also showed that even a single amino acid deletion in the carboxyl-terminal region markedly affected the heterotrimerization, indicating that the carboxyl-terminal end is indispensable for heterotrimer formation.
Authors:
Takehiro Kobayashi; Toshio Kakihara; Makoto Uchiyama
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Publication Detail:
Type:  Journal Article     Date:  2007-12-18
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  366     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2008 Feb 
Date Detail:
Created Date:  2007-12-25     Completed Date:  2008-02-05     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  60-5     Citation Subset:  IM    
Affiliation:
Division of Pediatrics, Department of Homeostatic Regulation and Development, Niigata University Graduate School of Medical and Dental Sciences, 1-757 Asahimachi-dori, Niigata City 951-8510, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Binding Sites
Cell Line
Collagen Type IV / chemistry*,  metabolism*
Dimerization
Humans
Kidney / metabolism*
Mutagenesis, Site-Directed
Protein Binding
Chemical
Reg. No./Substance:
0/COL4A5 protein, human; 0/Collagen Type IV

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


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