Coding and non-coding polymorphisms in the lectin pathway activator L-ficolin gene in 188 Dutch blood bank donors

被引：38

作者：

Herpers, BL ^{[1
]}

Immink, MM ^{[1
]}

de Jong, BAW ^{[1
]}

van Velzen-Blad, H ^{[1
]}

de Jongh, BM ^{[1
]}

van Hannen, EJ ^{[1
]}

机构：

[1] St Antonius Hosp, Dept Med Microbiol & Immunol, NL-3430 EM Nieuwegein, Netherlands

来源：

MOLECULAR IMMUNOLOGY | 2006年 / 43卷 / 07期

关键词：

complement; L-ficolin; fibrinogen-like domain; SNP; DGGE;

D O I：

10.1016/j.molimm.2005.06.035

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Human L-ficolin (FCN) is a serum lectin characterized by a collagen-like and a fibrinogen-like domain that can activate the lectin pathway of complement. Structural and functional similarities to mannose-binding lectin (MBL) suggest a role for L-ficolin in innate immunity. Structural polymorphisms in the MBL2 gene lead to functional deficiency of MBL. Polymorphisms in the FCN2 gene have not been studied previously. We developed 10 denaturing gradient gel electrophoresis (DGGE) assays to screen a total of 188 Dutch Caucasians for polymorphisms in FCN2. Total gene screening in this large cohort revealed 10 single nucleotide polymorphisms (SNPs). Interestingly, two conserved coding SNPs were found in exon 8, leading to amino acid substitutions within the fibrinogen-like domain. Fibrinogen-like domains are highly conserved among several proteins in many species. As this domain is responsible for binding of L-ficolin, these newly found coding polymorphisms could alter the affinity of the protein for its substrates and possibly alter the ability of L-ficolin to recognize invading microorganisms. (C) 2005 Elsevier Ltd. All rights reserved.

引用

页码：851 / 855

页数：5

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