Document Detail


Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations.
MedLine Citation:
PMID:  19307021     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
Anna St Swierzko; Maciej Cedzynski; Iwona Domzalska-Popadiuk; Shirley L MacDonald; Monika Borkowska-Klos; Anne P M Atkinson; Agnieszka Szala; Aleksandra Jopek; Jens C Jensenius; Masaya Kawakami; Jerzy Szczapa; Misao Matsushita; Janusz Szemraj; Marc L Turner; David C Kilpatrick
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Molecular immunology     Volume:  46     ISSN:  1872-9142     ISO Abbreviation:  Mol. Immunol.     Publication Date:  2009 May 
Date Detail:
Created Date:  2009-04-20     Completed Date:  2009-06-09     Revised Date:  2009-06-16    
Medline Journal Info:
Nlm Unique ID:  7905289     Medline TA:  Mol Immunol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1696-701     Citation Subset:  IM    
Affiliation:
Laboratory of Immunobiology of Infections, Institute of Medical Biology, Polish Academy of Sciences, Lodowa 106, 93-232 Lodz, Poland. aswierzko@cbm.pan.pl
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MeSH Terms
Descriptor/Qualifier:
Birth Weight / physiology
Cohort Studies
Female
Fetal Blood / chemistry,  metabolism*
Genetic Predisposition to Disease*
Genotype
Gestational Age
Humans
Infant, Low Birth Weight / blood,  metabolism
Infant, Newborn
Infant, Newborn, Diseases / blood,  genetics*,  metabolism
Infection / blood,  genetics,  metabolism
Male
Mannose-Binding Protein-Associated Serine Proteases / analysis,  genetics*,  metabolism*
Polymorphism, Single Nucleotide / physiology
Premature Birth / blood,  genetics,  metabolism
Chemical
Reg. No./Substance:
EC 3.4.21.-/MASP2 protein, human; EC 3.4.21.-/Mannose-Binding Protein-Associated Serine Proteases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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