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Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations
- Source :
- St Swierzko, A, Cedzynski, M, Domzalska-Popadiuk, I, MacDonald, S L, Borkowska-Klos, M, Atkinson, A P M, Szala, A, Jopek, A, Jensenius, J C, Kawakami, M, Szczapa, J, Matsushita, M, Szemraj, J, Turner, M L & Kilpatrick, D C 2009, ' Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations ', Molecular Immunology, vol. 46, no. 8-9, pp. 1696-701 . https://doi.org/10.1016/j.molimm.2009.02.022
- Publication Year :
- 2009
- Publisher :
- Elsevier BV, 2009.
-
Abstract
- Udgivelsesdato: 2009-May 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
- Subjects :
- Male
Proteases
medicine.medical_specialty
Genotype
Immunology
Gestational Age
Single-nucleotide polymorphism
Infections
Polymorphism, Single Nucleotide
Infant, Newborn, Diseases
Cohort Studies
Internal medicine
Mannan-binding lectin-associated serine protease-2
medicine
Birth Weight
Humans
Genetic Predisposition to Disease
Molecular Biology
biology
Infant, Newborn
Lectin
Gestational age
Infant, Low Birth Weight
Fetal Blood
Endocrinology
Mannose-Binding Protein-Associated Serine Proteases
Lectin pathway
Cord blood
biology.protein
Premature Birth
Female
Infection
MASP2
Subjects
Details
- ISSN :
- 01615890
- Volume :
- 46
- Database :
- OpenAIRE
- Journal :
- Molecular Immunology
- Accession number :
- edsair.doi.dedup.....57af8729c696822de6bb005bcea69882
- Full Text :
- https://doi.org/10.1016/j.molimm.2009.02.022