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Cited by 41Complement system in diseasesNeonatal and Maternal InfectionsBiomarkers in Disease Mechanisms

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H-ficolin (ficolin-3) concentrations and FCN3 gene polymorphism in neonates

Michalski, Mateusz, Szala, Agnieszka, St. Swierzko, Anna, Lukasiewicz, Jolanta, Maciejewska, Anna, Kilpatrick, David C., Matsushita, Misao, Domzalska-Popadiuk, Iwona, Borkowska-Klos, Monika, Sokolowska, Anna, Szczapa, Jerzy, Lugowski, Czeslaw, Cedzynski, Maciej·2012·Immunobiology
DOI 10.1016/j.imbio.2011.12.004
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Abstract

Serum H-ficolin (ficolin-3) concentrations (n=613) and FCN3 genotypes (n=529) from a large group of neonates are presented. Both pre-term deliveries and low birthweight (independently of gestational age) were significantly associated with low H-ficolin concentrations but not with heterozygosity for the FCN3 1637delC frameshift mutation. The presence of the variant allele, however, apparently influenced the protein level. No association of FCN3 gene heterozygosity or relative functional H-ficolin insufficiency (determined as serum level ≤8.6 μg/ml) with perinatal infections was found. One premature newborn, with confirmed infection caused by Streptococcus agalactiae, was H-ficolin-deficient (FCN3 variant homozygote, no detectable protein). We present what is only the fourth case report of total H-ficolin deficiency in the world literature. This neonate was however previously found to be mannan-binding lectin (MBL) as well as MBL-associated serine protease-2 (MASP-2) deficient and also had low serum L-ficolin.

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  • The trans pQTL at FCN3 is a low-frequency frameshift variant (rs532781899, MAF = 1.4%) leading to FCN3 deficiency and reduced MASP1 levels (β = -1.16, P = 3.8 × 10 -312).

    “Notably, the trans pQTL at FCN3 is a low-frequency frameshift variant (rs532781899, MAF = 1.4%) leading to FCN3 deficiency [44][45][46] and, here, to reduced MASP1 levels (β = -1.16,P = 3.8 × 10 -312 )”

    From Plasma proteomic associations with genetics and health in the UK Biobank (2023) · cites this paper as [45]

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Research works printed but not linked: 30

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Metadata

Authors
Michalski, M., Szala, A., St. Swierzko, A., Lukasiewicz, J., Maciejewska, A., Kilpatrick, D. C., Matsushita, M., Domzalska-Popadiuk, I., Borkowska-Klos, M., Sokolowska, A., Szczapa, J., Lugowski, C., & Cedzynski, M.
Affiliations
  • University of Łódź (PL)
  • Institute for Medical Biology (PL)
  • Ludwik Hirszfeld Institute of Immunology and Experimental Therapy (PL)
  • Scottish National Blood Transfusion Service (GB)
  • Tokai University (JP)
  • Poznan University of Medical Sciences (PL)
ORCID
Venue
Immunobiology
Publisher
Elsevier BV
Published
2012-07
Volume
217
Issue
7
Pages
730-737
ISSN
0171-2985 (ISSN-L)
DOI
10.1016/j.imbio.2011.12.004
OpenAlex
W2005120005
Cited by
41
References
0
Citations by year
2023: 3 · 2022: 5 · 2021: 2 · 2020: 8 · 2019: 3 · 2017: 2 · 2016: 6 · 2015: 3 · 2014: 3 · 2013: 2 · 2012: 3
FWCI
1.13
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Immunobiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Royal Society of Edinburgh
  • Uniwersytet Medyczny im. Karola Marcinkowskiego w Poznaniu
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
  • Health Sciences › Medicine › Pediatrics, Perinatology and Child Health › Neonatal and Maternal Infections
  • Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
Keywords
ficolin-3, neonates, preterm birth, low birth weight, L-ficolin, perinatal infection, Streptococcus agalactiae, innate immunity
MeSH terms
Alleles, Female, Genotype, Gestational Age, Glycoproteins, Heterozygote, Homozygote, Humans, Infant, Low Birth Weight, Infant, Newborn, Male, Polymorphism, Genetic, Streptococcal Infections, Streptococcus agalactiae, Frameshift Mutation, Lectins, Mannose-Binding Lectin, Premature Birth, Mannose-Binding Protein-Associated Serine Proteases

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