Search results for "Mannose-Binding Protein-Associated Serine Proteases"

showing 3 items of 3 documents

The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, …

2001

The proteases of the lectin pathway of complement activation, MASP-1 and MASP-2, are encoded by two separate genes. The MASP1 gene is located on chromosome 3q27, the MASP2 gene on chromosome 1p36.23-31. The genes for the classical complement activation pathway proteases, C1r and C1s, are linked on chromosome 12p13. We have shown that the MASP2 gene encodes two gene products, the 76 kDa MASP-2 serine protease and a plasma protein of 19 kDa, termed MAp19 or sMAP. Both gene products are components of the lectin pathway activation complex. We present the complete primary structure of the human MASP2 gene and the tight cluster that this locus forms with non-complement genes. A comparison of the …

Chromosomes Artificial BacterialTranscription GeneticGenetic LinkageRNA SplicingImmunologyMolecular Sequence DataBiologyGeneticsHumansPromoter Regions GeneticComplement ActivationGenetics (clinical)Mannan-binding lectinGeneticsComplement component 2Base SequenceCD69Serine EndopeptidasesC4AChromosome MappingCollectinsKLRB1Chromosomes Human Pair 1Lectin pathwayMannose-Binding Protein-Associated Serine ProteasesMultigene Familybiology.proteinCarrier ProteinsMASP2MASP1
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H-ficolin (ficolin-3) concentrations and FCN3 gene polymorphism in neonates

2011

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 …

MaleHeterozygotemedicine.medical_specialtyGenotypeImmunologyGestational AgeBiologymedicine.disease_causeMannose-Binding LectinStreptococcus agalactiaeFrameshift mutationLoss of heterozygosityPolymorphism (computer science)LectinsStreptococcal InfectionsInternal medicineGenotypemedicineHumansImmunology and AllergyFrameshift MutationAllelesGlycoproteinsMannan-binding lectinPolymorphism GeneticHomozygoteInfant NewbornHematologyInfant Low Birth WeightEndocrinologyStreptococcus agalactiaeMannose-Binding Protein-Associated Serine ProteasesImmunologyPremature BirthFemaleGene polymorphismFicolinImmunobiology
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Distinct Roles of Classical and Lectin Pathways of Complement in Preeclamptic Placentae

2022

Pre-eclampsia is a pregnancy complication characterized by defective vascular remodeling in maternal decidua responsible for reduced blood flow leading to functional and structural alterations in the placenta. We have investigated the contribution of the complement system to decidual vascular changes and showed that trophoblasts surrounding unremodeled vessels prevalent in preeclamptic decidua fail to express C1q that are clearly detected in cells around remodeled vessels predominant in control placenta. The critical role of C1q is supported by the finding that decidual trophoblasts of femaleC1qa-/-pregnant mice mated toC1qa+/+male mice surrounding remodeled vessels express C1q of paternal …

Malepre-eclampsiavascular remodelingComplement System ProteinPlacentaImmunologyMannose-Binding Protein-Associated Serine ProteaseSettore MED/08 - Anatomia PatologicaPre-Eclampsia.MicePregnancyLectinsficolin-3Immunology and AllergyAnimalsHumansSettore MED/05 - Patologia Clinicacomplement system; pre-eclampsia; vascular remodeling; C1q; ficolin-3C1qcomplement systemAnimalComplement C1qEndothelial CellsComplement System ProteinsMannose-Binding Protein-Associated Serine ProteasesFemale
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