title: Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations.
abstract: 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.
authors.affiliation: Laboratory of Immunobiology of Infections, Institute of Medical Biology, Polish Academy of Sciences, Lodowa 106, 93-232 Lodz, Poland. aswierzko@cbm.pan.pl
authors.forename: Anna
authors.initials: A
authors.lastname: St Swierzko
authors.forename: Maciej
authors.initials: M
authors.lastname: Cedzynski
authors.forename: Iwona
authors.initials: I
authors.lastname: Domzalska-Popadiuk
authors.forename: Shirley L
authors.initials: SL
authors.lastname: MacDonald
authors.forename: Monika
authors.initials: M
authors.lastname: Borkowska-Klos
authors.forename: Anne P M
authors.initials: AP
authors.lastname: Atkinson
authors.forename: Agnieszka
authors.initials: A
authors.lastname: Szala
authors.forename: Aleksandra
authors.initials: A
authors.lastname: Jopek
authors.forename: Jens C
authors.initials: JC
authors.lastname: Jensenius
authors.forename: Masaya
authors.initials: M
authors.lastname: Kawakami
authors.forename: Jerzy
authors.initials: J
authors.lastname: Szczapa
authors.forename: Misao
authors.initials: M
authors.lastname: Matsushita
authors.forename: Janusz
authors.initials: J
authors.lastname: Szemraj
authors.forename: Marc L
authors.initials: ML
authors.lastname: Turner
authors.forename: David C
authors.initials: DC
authors.lastname: Kilpatrick
mesh_terms: D001724:Birth Weight / Q000502:physiology; D015331:Cohort Studies; D005260:Female; D005312:Fetal Blood / Q000737:chemistry / Q000378:metabolism*; D020022:Genetic Predisposition to Disease; D005838:Genotype; D005865:Gestational Age; D006801:Humans; D007230:Infant, Low Birth Weight / Q000097:blood / Q000378:metabolism; D007231:Infant, Newborn; D007232:Infant, Newborn, Diseases / Q000097:blood / Q000235:genetics* / Q000378:metabolism; D007239:Infections / Q000097:blood / Q000235:genetics / Q000378:metabolism; D008297:Male; D050606:Mannose-Binding Protein-Associated Serine Proteases / Q000032:analysis / Q000235:genetics* / Q000378:metabolism*; D020641:Polymorphism, Single Nucleotide / Q000502:physiology; D047928:Premature Birth / Q000097:blood / Q000235:genetics / Q000378:metabolism
chemical_list: C105296:MASP2 protein, human; D050606:Mannose-Binding Protein-Associated Serine Proteases