ArticlePloS one2012
Non-synonymous polymorphisms in the FCN1 gene determine ligand-binding ability and serum levels of M-ficolin.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Collectins and ficolins in neonatal health and disease.Frontiers in immunology · 2023Review
- The clinical value of ficolin-3 gene polymorphism in rheumatic heart disease. An Egyptian adolescents study.BMC research notes · 2021Article
- Pattern Recognition Molecules of Lectin Complement Pathway in Ischemic Stroke.Pharmacogenomics and personalized medicine · 2021Article
- Review
- The Influence of the Lectin Pathway of Complement Activation on Infections of the Respiratory System.Frontiers in immunology · 2020Review
- Associations of Ficolins With Hematological Malignancies in Patients Receiving High-Dose Chemotherapy and Autologous Hematopoietic Stem Cell Transplantations.Frontiers in immunology · 2019Article
- Ficolins and the Recognition of Pathogenic Microorganisms: An Overview of the Innate Immune Response and Contribution of Single Nucleotide Polymorphisms.Journal of immunology research · 2019Review
- Sickening or Healing the Heart? The Association of Ficolin-1 and Rheumatic Fever.Frontiers in immunology · 2018Observational
- Ficolin-1 and Ficolin-3 Plasma Levels Are Altered in HIV and HIV/HCV Coinfected Patients From Southern Brazil.Frontiers in immunology · 2018Article
- Ficolin-1 Levels in Patients Developing Vasospasm and Cerebral Ischemia After Spontaneous Subarachnoid Hemorrhage.Molecular neurobiology · 2017Article
- Fibrinogen-Related Proteins in Tissue Repair: How a Unique Domain with a Common Structure Controls Diverse Aspects of Wound Healing.Advances in wound care · 2015Review
- Human lectins and their roles in viral infections.Molecules (Basel, Switzerland) · 2015Review
- CRP genotype and haplotype associations with serum C-reactive protein level and DAS28 in untreated early rheumatoid arthritis patients.Arthritis research & therapy · 2014Article
- The lectin pathway of complement and rheumatic heart disease.Frontiers in pediatrics · 2014Review
- Polymorphisms in the MASP1 gene are associated with serum levels of MASP-1, MASP-3, and MAp44.PloS one · 2013Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe innate immune system encompasses various recognition molecules able to sense both exogenous and endogenous danger signals arising from pathogens or damaged host cells. One such pattern-recognition molecule is M-ficolin, which is capable of activating the complement system through the lectin pathway. The lectin pathway is multifaceted with activities spanning from complement activation to coagulation, autoimmunity, ischemia-reperfusion injury and embryogenesis. Our aim was to explore associations between SNPs in FCN1, encoding M-ficolin and corresponding protein concentrations, and the impact of non-synonymous SNPs on protein function. PRINCIPAL
findingsWe genotyped 26 polymorphisms in the FCN1 gene and found 8 of these to be associated with M-ficolin levels in a cohort of 346 blood donors. Four of those polymorphisms were located in the promoter region and exon 1 and were in high linkage disequilibrium (r(2)≥0.91). The most significant of those were the AA genotype of -144C>A (rs10117466), which was associated with an increase in M-ficolin concentration of 26% compared to the CC genotype. We created recombinant proteins corresponding to the five non-synonymous mutations encountered and found that the Ser268Pro (rs150625869) mutation lead to loss of M-ficolin production. This was backed up by clinical observations, indicating that an individual homozygote of Ser268Pro would be completely M-ficolin deficient. Furthermore, the Ala218Thr (rs148649884) and Asn289Ser (rs138055828) were both associated with low M-ficolin levels, and the mutations crippled the ligand-binding capability of the recombinant M-ficolin, as indicated by the low binding to Group B Streptococcus. SIGNIFICANCE: Overall, our study interlinks the genotype and phenotype relationship concerning polymorphisms in FCN1 and corresponding concentrations and biological functions of M-ficolin. The elucidations of these associations provide information for future genetic studies in the lectin pathway and complement system.
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