Molecular basis of polymorphisms of human complement component C3.

Details

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State: Public
Version: Final published version
License: Not specified
Serval ID
serval:BIB_4821CE19A885
Type
Article: article from journal or magazin.
Collection
Publications
Title
Molecular basis of polymorphisms of human complement component C3.
Journal
The Journal of experimental medicine
Author(s)
Botto M., Fong K.Y., So A.K., Koch C., Walport M.J.
ISSN
0022-1007 (Print)
ISSN-L
0022-1007
Publication state
Published
Issued date
01/10/1990
Peer-reviewed
Oui
Volume
172
Number
4
Pages
1011-1017
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
C3 exhibits two common allotypic variants that may be separated by gel electrophoresis and are called C3 fast (C3 F) and C3 slow (C3 S). C3 F, the less common variant, occurs at appreciable frequencies only in Caucasoid populations (gene frequency = 0.20). An increased prevalence of the C3 F allele has been reported in patients with partial lipodystrophy, IgA nephropathy, and Indian childhood hepatic cirrhosis. Studies of the genomic organization of the human C3 gene led to the identification of a single change (C to G) between C3 S and C3 F at nucleotide 364 in exon 3. This leads, at the translation level, to the substitution of an arginine residue (positively charged) in C3 S for a glycine residue (neutral) in C3 F. This substitution results in a polymorphic restriction site for the enzyme HhaI. The resulting restriction fragment length polymorphism (RFLP) was investigated using genomic DNA, amplified using the polymerase chain reaction; there was absolute concordance between the genomic polymorphism and the distribution of C3 S and C3 F in 50 normal subjects. The molecular basis of a second structural polymorphism, defined by the monoclonal antibody HAV 4-1, was also characterized. The polymorphic determinant was identified at codon 314 in the exon 9 of the beta chain where a leucine residue (HAV 4-1+) is substituted for a proline residue (HAV 4-1-). Identification of the amino acid sequences of these polymorphic variants will facilitate characterization of possible functional differences between different allotypes of C3. Three RFLPs (BamHI, EcoRI, and SstI) were located to introns in the C3 gene. There was no allelic association between these three RFLPs, or between the RFLPs and the C3 F/S polymorphic site. Genetic equilibration of these polymorphisms has occurred within a gene of 41 kb.
Keywords
Antibodies, Monoclonal, Base Sequence, Complement C3/chemistry, Complement C3/genetics, DNA Probes, Humans, Molecular Sequence Data, Polymorphism, Genetic, Polymorphism, Restriction Fragment Length, Structure-Activity Relationship
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 8:38
Last modification date
09/08/2024 12:18
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