Aarhus University Seal / Aarhus Universitets segl

Jens Christian Jensenius

Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

  • Anna St Swierzko, Denmark
  • Maciej Cedzynski, Denmark
  • Iwona Domzalska-Popadiuk, Denmark
  • Shirley L MacDonald, Denmark
  • Monika Borkowska-Klos, Denmark
  • Anne P M Atkinson, Denmark
  • Agnieszka Szala, Denmark
  • Aleksandra Jopek, Denmark
  • Jens C Jensenius
  • Masaya Kawakami, Denmark
  • Jerzy Szczapa, Denmark
  • Misao Matsushita, Denmark
  • Janusz Szemraj, Denmark
  • Marc L Turner, Denmark
  • David C Kilpatrick, Denmark
  • Department of Medical Microbiology and Immunology
One collectin (mannan-binding lectin, MBL) and three ficolins (M-ficolin/ficolin-1, L-ficolin/ficolin-2 and H-ficolin/ficolin-3) share the capability to activate complement via the lectin pathway. This property depends on the ability of these lectins to form complexes with MBL-associated serine proteases (MASPs), particularly MASP-2. We report the results of an investigation of cord blood MASP-2 concentrations in a large, ethnically homogeneous cohort (n=1788) of neonates. The median value of MASP-2 in cord sera was determined to be 93 ng/ml (range <25-812). Serum MASP-2 concentrations correlated with gestational age and birthweight and were significantly lower in premature babies and other pre-term babies compared with term babies. Neonates with MASP-2 concentrations below 42 ng/ml were deemed to be MASP-2 deficient. That group had a shorter mean gestational age and a higher incidence of premature and low birthweight babies, but not of perinatal infections when compared with the others. Indeed, there was a trend towards higher MASP-2 concentrations amongst babies with infections. Among 362 samples tested for the D120G single nucleotide polymorphism (SNP) of the MASP2 gene, no homozygote for that mutation was found. Heterozygosity for this allele significantly influenced the protein concentration, but not the lectin pathway of complement activity (MBL-MASP-2 complex activity). Moreover, no association of this SNP was apparent with prematurity, low birthweight or perinatal infections.
Original languageEnglish
JournalMolecular Immunology
Volume46
Issue8-9
Pages (from-to)1696-701
Number of pages5
ISSN0161-5890
DOIs
Publication statusPublished - 2009

    Research areas

  • Birth Weight, Cohort Studies, Female, Fetal Blood, Genetic Predisposition to Disease, Genotype, Gestational Age, Humans, Infant, Low Birth Weight, Infant, Newborn, Infant, Newborn, Diseases, Infection, Male, Mannose-Binding Protein-Associated Serine Proteases, Polymorphism, Single Nucleotide, Premature Birth

See relations at Aarhus University Citationformats

ID: 18954465