Search results for "Lectin pathway"

showing 8 items of 8 documents

Binding and activation of human and mouse complement by Cryptosporidium parvum (Apicomplexa) and susceptibility of C1q- and MBL-deficient mice to inf…

2008

Cryptosporidium parvum is a protozoan parasite (Apicomplexa) that causes gastrointestinal disease in animals and humans. Whereas immunocompetent hosts can limit the infection within 1 or 2 weeks, immunocompromised individuals develop a chronic, life-threatening disease. The importance of the adaptive cellular immune response, with CD4+ T-lymphocytes being the major players, has been clearly demonstrated. Several non-adaptive immune mechanisms have been suggested to contribute to the host defence, such as interferon-gamma (IFN-gamma) from NK cells, certain chemokines, beta-defensins and pro-inflammatory cytokines, but the influence of the complement systems has been less well studied. We ana…

ChemokineImmunologyProtozoan ProteinsCryptosporidiosisComplement factor ISodium ChlorideMannose-Binding LectinMicrobiologyMiceImmune systemmedicineAnimalsHumansRNA MessengerMolecular BiologyComplement ActivationImmunodeficiencyMannan-binding lectinCryptosporidium parvumbiologyReverse Transcriptase Polymerase Chain ReactionComplement C1qOocystsTemperaturemedicine.diseasebiology.organism_classificationVirologyComplement systemMice Inbred C57BLCryptosporidium parvumGene Expression RegulationLectin pathwayComplement C3bbiology.proteinCattleDisease SusceptibilityMolecular immunology
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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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Secreted proteophosphoglycan of Leishmania mexicana amastigotes activates complement by triggering the mannan binding lectin pathway.

1997

Cutaneous lesions induced by infection of mice with the protozoan parasite, Leishmania mexicana, contain abundant amounts of a high molecular mass proteophosphoglycan (PPG), which is secreted by the amastigote stage residing in phagolysosomes of macrophages and can then be released into the tissue upon rupture of the infected cells. Amastigote PPG forms sausage-shaped but soluble particles and belongs to a novel class of serine-rich proteins that are extensively O-glycosylated by phosphooligosaccharides capped by mannooligosaccharides. The purified molecule is shown here to efficiently activate complement (C) and deplete hemolytic activity of normal serum and may prevent the opsonization of…

ImmunologyLeishmania mexicanaProtozoan ProteinsCollectinLeishmaniasis CutaneousLeishmania mexicanaMiceImmunology and AllergyAnimalsAmastigoteComplement ActivationMannan-binding lectinSerine proteaseMice KnockoutbiologyMacrophagesComplement C4Complement C3biology.organism_classificationCollectinsComplement systemAntibody opsonizationBiochemistryLectin pathwaybiology.proteinMice Inbred CBACalciumProteoglycansCarrier ProteinsEuropean journal of immunology
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New functional ligands for ficolin-3 among lipopolysaccharides of Hafnia alvei.

2011

Ficolin-1 (M), ficolin-2 (L), ficolin-3 (H) and mannan-binding lectin (MBL) activate the complement system and have opsonic activity. The specificity of ficolin-3 is poorly characterized and currently limited to a few ligands only. We present new specific targets for human ficolin-3, identified among lipopolysaccharides (LPSs, endotoxin) of Hafnia alvei. The interaction was restricted to LPSs of four strains: 23, Polish Collection of Microorganisms (PCM) 1200, PCM 1203 and PCM 1205 and limited to their O-specific polysaccharides (O-specific PSs) composed of different numbers of oligosaccharide (OS) repeating units (RUs). Moreover, these LPS/ficolin-3 complexes activated the lectin pathway o…

LipopolysaccharidesDisaccharideLigandsBiochemistrychemistry.chemical_compoundLectinsAnimalsHumansBovine serum albuminOpsoninchemistry.chemical_classificationbiologyLectinO AntigensComplement Pathway Mannose-Binding LectinHafnia alveiSerum Albumin BovineOligosaccharideComplement systemEndotoxinschemistryBiochemistryLectin pathwaybiology.proteinCattleFicolinGlycobiology
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Differential expression of the murine mannose-binding lectins A and C in lymphoid and nonlymphoid organs and tissues.

2003

Abstract Mannose-binding lectin (MBL), a member of the collectin family, binds to carbohydrate structures on the surfaces of micro-organisms and may serve as a recognition molecule of the lectin pathway of complement activation. In rodents two forms, MBL-A and MBL-C, were described and shown to be products of two related, but uncoupled, genes. The liver is the main source of MBL biosynthesis. For rat MBL-A, expression has also been described in the kidney. Here we report that the two forms of murine MBL are differentially expressed in a number of nonhepatic tissues. Real-time RT-PCR revealed that the liver is the major site of expression for both MBL genes. Lower copy numbers were found in …

MaleLymphoid TissueImmunologyCollectinchemical and pharmacologic phenomenaIn situ hybridizationMannose-Binding LectinMiceIntestine SmallImmunology and AllergyAnimalsProtein IsoformsIn Situ HybridizationMannan-binding lectinMice Inbred BALB CInnate immune systembiologyLectinbacterial infections and mycosesAcquired immune systemMolecular biologyImmunohistochemistryComplement systemAnimals NewbornLiverOrgan SpecificityLectin pathwaybiology.proteinFemaleSpleenJournal of immunology (Baltimore, Md. : 1950)
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Activation of the lectin pathway in murine lupus nephritis.

2004

In systemic lupus erythematosus (SLE), hypocomplementaemia and complement deposition have been described both in man and in experimental models. A major involvement of the classical pathway of complement activation has been demonstrated in this disease, however relatively little is known about the involvement of the lectin pathway. Therefore in the present study we have analyzed the activity of all three pathways of complement activation in murine models of SLE. In the mouse, MBL is expressed in two forms, namely MBL-A and MBL-C. In the present study young and old MRL-lpr and control MRL+/+ mice were compared for the levels of complement activity with specific attention for the lectin pathw…

Mice Inbred MRL lprImmunologychemical and pharmacologic phenomenaurologic and male genital diseasesmedicine.disease_causeAutoimmunityClassical complement pathwayMiceImmune systemimmune system diseasesMurine lupusLectinsmedicineAnimalsskin and connective tissue diseasesMolecular BiologyAutoantibodiesChemistrybacterial infections and mycosesmedicine.diseaseLupus NephritisComplement systemLectin pathwayImmunologyAlternative complement pathwayNephritisMolecular immunology
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Evolution and Immune Function of Fish Lectins

2016

Abstract Lectins are sugar-binding proteins widely distributed among animals, plants, and microbial taxon, involved in diverse biological processes. In both invertebrates and vertebrates, they play key roles in nonself recognition and immune responses, such as nonself recognition, inflammatory processes, and immunomodulation. In fish, many lectin families have been identified, and their tissue-specific expression and localization of the various lectin repertoires and their ligands are consistent with their distinct biological roles in innate and adaptive immunity. Here, we discuss the involvement of F-type lectins, rhamnose-binding lectins, galectins, and C-type lectins in pathogen recognit…

biologyLectinchemical and pharmacologic phenomenaAcquired immune systemCell biologyKLRB1BiochemistryC-type lectinLectin pathwaybiology.proteinFicolinimmunity fish lectin inflammationMannan-binding lectinGalectin
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Neuronal immunoreactivity for mannose-binding lectin after venous occlusion-induced focal cerebral ischemia in rats

2012

Abstract A recent research reveals that complement activation exacerbates cerebral infarction. However, involvement of the lectin pathway, (the third complement activation pathway) in cerebral ischemia is not well studied. In this study, we investigated the appearance of mannose-binding lectin (MBL) in ischemic brain tissue. Male Wistar rats ( n  = 25) were divided into three groups: untreated control, sham, and vein occlusion (VO). Rats in the VO group had two adjacent photochemically occluded cortical veins. Regional cerebral blood flow (rCBF) was measured in the sham and VO groups. Rats were perfusion-fixed at 72 h in the sham group and at 3, 24, and 72 h after inducing ischemia in the V…

medicine.medical_specialtybusiness.industryCerebral infarctionGeneral NeuroscienceIschemiachemical and pharmacologic phenomenamedicine.diseaseVein occlusionComplement systemPsychiatry and Mental healthEndocrinologyCerebral blood flowInternal medicineLectin pathwayImmunologymedicineImmunohistochemistryNeurology (clinical)businessMannan-binding lectinNeurology, Psychiatry and Brain Research
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