Mannose-Binding Lectin: A specific mannose-binding member of the collectin family of lectins. It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY.Complement Activation: The sequential activation of serum COMPLEMENT PROTEINS to create the COMPLEMENT MEMBRANE ATTACK COMPLEX. Factors initiating complement activation include ANTIGEN-ANTIBODY COMPLEXES, microbial ANTIGENS, or cell surface POLYSACCHARIDES.Complement Pathway, Mannose-Binding Lectin: Complement activation triggered by the interaction of microbial POLYSACCHARIDES with serum MANNOSE-BINDING LECTIN resulting in the activation of MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASES. As in the classical pathway, MASPs cleave COMPLEMENT C4 and COMPLEMENT C2 to form C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.Mannose-Binding Protein-Associated Serine Proteases: Serum serine proteases which participate in COMPLEMENT ACTIVATION. They are activated when complexed with the MANNOSE-BINDING LECTIN, therefore also known as Mannose-binding protein-Associated Serine Proteases (MASPs). They cleave COMPLEMENT C4 and COMPLEMENT C2 to form C4b2a, the CLASSICAL PATHWAY C3 CONVERTASE.Complement C3: A glycoprotein that is central in both the classical and the alternative pathway of COMPLEMENT ACTIVATION. C3 can be cleaved into COMPLEMENT C3A and COMPLEMENT C3B, spontaneously at low level or by C3 CONVERTASE at high level. The smaller fragment C3a is an ANAPHYLATOXIN and mediator of local inflammatory process. The larger fragment C3b binds with C3 convertase to form C5 convertase.Complement System Proteins: Serum glycoproteins participating in the host defense mechanism of COMPLEMENT ACTIVATION that creates the COMPLEMENT MEMBRANE ATTACK COMPLEX. Included are glycoproteins in the various pathways of complement activation (CLASSICAL COMPLEMENT PATHWAY; ALTERNATIVE COMPLEMENT PATHWAY; and LECTIN COMPLEMENT PATHWAY).Complement C4: A glycoprotein that is important in the activation of CLASSICAL COMPLEMENT PATHWAY. C4 is cleaved by the activated COMPLEMENT C1S into COMPLEMENT C4A and COMPLEMENT C4B.Lectins: Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.Serine Endopeptidases: Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.Complement Factor D: A serum protein which is important in the ALTERNATIVE COMPLEMENT ACTIVATION PATHWAY. This enzyme cleaves the COMPLEMENT C3B-bound COMPLEMENT FACTOR B to form C3bBb which is ALTERNATIVE PATHWAY C3 CONVERTASE.Bibliometrics: The use of statistical methods in the analysis of a body of literature to reveal the historical development of subject fields and patterns of authorship, publication, and use. Formerly called statistical bibliography. (from The ALA Glossary of Library and Information Science, 1983)HungaryPublications: Copies of a work or document distributed to the public by sale, rental, lease, or lending. (From ALA Glossary of Library and Information Science, 1983, p181)Research: Critical and exhaustive investigation or experimentation, having for its aim the discovery of new facts and their correct interpretation, the revision of accepted conclusions, theories, or laws in the light of newly discovered facts, or the practical application of such new or revised conclusions, theories, or laws. (Webster, 3d ed)Biomedical Research: Research that involves the application of the natural sciences, especially biology and physiology, to medicine.Academies and Institutes: Organizations representing specialized fields which are accepted as authoritative; may be non-governmental, university or an independent research organization, e.g., National Academy of Sciences, Brookings Institution, etc.PubMed: A bibliographic database that includes MEDLINE as its primary subset. It is produced by the National Center for Biotechnology Information (NCBI), part of the NATIONAL LIBRARY OF MEDICINE. PubMed, which is searchable through NLM's Web site, also includes access to additional citations to selected life sciences journals not in MEDLINE, and links to other resources such as the full-text of articles at participating publishers' Web sites, NCBI's molecular biology databases, and PubMed Central.Umbilical Veins: Venous vessels in the umbilical cord. They carry oxygenated, nutrient-rich blood from the mother to the FETUS via the PLACENTA. In humans, there is normally one umbilical vein.Endothelial Cells: Highly specialized EPITHELIAL CELLS that line the HEART; BLOOD VESSELS; and lymph vessels, forming the ENDOTHELIUM. They are polygonal in shape and joined together by TIGHT JUNCTIONS. The tight junctions allow for variable permeability to specific macromolecules that are transported across the endothelial layer.Collectins: A class of C-type lectins that target the carbohydrate structures found on invading pathogens. Binding of collectins to microorganisms results in their agglutination and enhanced clearance. Collectins form trimers that may assemble into larger oligomers. Each collectin polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen-like region, an alpha-helical coiled-coil region, and carbohydrate-binding region.Zebrafish: An exotic species of the family CYPRINIDAE, originally from Asia, that has been introduced in North America. They are used in embryological studies and to study the effects of certain chemicals on development.Zebrafish Proteins: Proteins obtained from the ZEBRAFISH. Many of the proteins in this species have been the subject of studies involving basic embryological development (EMBRYOLOGY).MyoD Protein: A myogenic regulatory factor that controls myogenesis. Though it is not clear how its function differs from the other myogenic regulatory factors, MyoD appears to be related to fusion and terminal differentiation of the muscle cell.Embryo, Nonmammalian: The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.SOX9 Transcription Factor: A SOXE transcription factor that plays a critical role in regulating CHONDROGENESIS; OSTEOGENESIS; and male sex determination. Loss of function of the SOX9 transcription factor due to genetic mutations is a cause of CAMPOMELIC DYSPLASIA.Neural Crest: The two longitudinal ridges along the PRIMITIVE STREAK appearing near the end of GASTRULATION during development of nervous system (NEURULATION). The ridges are formed by folding of NEURAL PLATE. Between the ridges is a neural groove which deepens as the fold become elevated. When the folds meet at midline, the groove becomes a closed tube, the NEURAL TUBE.Rhombencephalon: The posterior of the three primitive cerebral vesicles of an embryonic brain. It consists of myelencephalon, metencephalon, and isthmus rhombencephali from which develop the major BRAIN STEM components, such as MEDULLA OBLONGATA from the myelencephalon, CEREBELLUM and PONS from the metencephalon, with the expanded cavity forming the FOURTH VENTRICLE.Complement Pathway, Classical: Complement activation initiated by the binding of COMPLEMENT C1 to ANTIGEN-ANTIBODY COMPLEXES at the COMPLEMENT C1Q subunit. This leads to the sequential activation of COMPLEMENT C1R and COMPLEMENT C1S subunits. Activated C1s cleaves COMPLEMENT C4 and COMPLEMENT C2 forming the membrane-bound classical C3 CONVERTASE (C4B2A) and the subsequent C5 CONVERTASE (C4B2A3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.Abortion, Habitual: Three or more consecutive spontaneous abortions.Mannose: A hexose or fermentable monosaccharide and isomer of glucose from manna, the ash Fraxinus ornus and related plants. (From Grant & Hackh's Chemical Dictionary, 5th ed & Random House Unabridged Dictionary, 2d ed)Mannose-Binding Lectins: A subclass of lectins that are specific for CARBOHYDRATES that contain MANNOSE.Lupus Erythematosus, Systemic: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys, and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.Protein Isoforms: Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.Myocardial Infarction: NECROSIS of the MYOCARDIUM caused by an obstruction of the blood supply to the heart (CORONARY CIRCULATION).Fibroblast Growth Factor 2: A single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FIBROBLAST GROWTH FACTOR 1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 1).Fibroblast Growth Factors: A family of small polypeptide growth factors that share several common features including a strong affinity for HEPARIN, and a central barrel-shaped core region of 140 amino acids that is highly homologous between family members. Although originally studied as proteins that stimulate the growth of fibroblasts this distinction is no longer a requirement for membership in the fibroblast growth factor family.Receptors, Fibroblast Growth Factor: Specific molecular sites or structures on cell membranes that react with FIBROBLAST GROWTH FACTORS (both the basic and acidic forms), their analogs, or their antagonists to elicit or to inhibit the specific response of the cell to these factors. These receptors frequently possess tyrosine kinase activity.Cholinesterase Reactivators: Drugs used to reverse the inactivation of cholinesterase caused by organophosphates or sulfonates. They are an important component of therapy in agricultural, industrial, and military poisonings by organophosphates and sulfonates.Fibroblast Growth Factor 1: A 17-kDa single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. It binds to HEPARIN, which potentiates its biological activity and protects it from proteolysis. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages, and also has chemotactic and mitogenic activities. It was originally named acidic fibroblast growth factor based upon its chemical properties and to distinguish it from basic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 2).Complement Pathway, Alternative: Complement activation initiated by the interaction of microbial ANTIGENS with COMPLEMENT C3B. When COMPLEMENT FACTOR B binds to the membrane-bound C3b, COMPLEMENT FACTOR D cleaves it to form alternative C3 CONVERTASE (C3BBB) which, stabilized by COMPLEMENT FACTOR P, is able to cleave multiple COMPLEMENT C3 to form alternative C5 CONVERTASE (C3BBB3B) leading to cleavage of COMPLEMENT C5 and the assembly of COMPLEMENT MEMBRANE ATTACK COMPLEX.Complement Factor B: A glycine-rich, heat-labile serum glycoprotein that contains a component of the C3 CONVERTASE ALTERNATE PATHWAY (C3bBb). Bb, a serine protease, is generated when factor B is cleaved by COMPLEMENT FACTOR D into Ba and Bb.Postoperative Complications: Pathologic processes that affect patients after a surgical procedure. They may or may not be related to the disease for which the surgery was done, and they may or may not be direct results of the surgery.Coronary Artery Bypass: Surgical therapy of ischemic coronary artery disease achieved by grafting a section of saphenous vein, internal mammary artery, or other substitute between the aorta and the obstructed coronary artery distal to the obstructive lesion.Lewis Blood-Group System: A group of dominantly and independently inherited antigens associated with the ABO blood factors. They are glycolipids present in plasma and secretions that may adhere to the erythrocytes. The phenotype Le(b) is the result of the interaction of the Le gene Le(a) with the genes for the ABO blood groups.Haplotypes: The genetic constitution of individuals with respect to one member of a pair of allelic genes, or sets of genes that are closely linked and tend to be inherited together such as those of the MAJOR HISTOCOMPATIBILITY COMPLEX.Allergy and Immunology: A medical specialty concerned with the hypersensitivity of the individual to foreign substances and protection from the resultant infection or disorder.Access to Information: Individual's rights to obtain and use information collected or generated by others.Periodicals as Topic: A publication issued at stated, more or less regular, intervals.Journal Impact Factor: A quantitative measure of the frequency on average with which articles in a journal have been cited in a given period of time.Immune System Diseases: Disorders caused by abnormal or absent immunologic mechanisms, whether humoral, cell-mediated, or both.Shock, Septic: Sepsis associated with HYPOTENSION or hypoperfusion despite adequate fluid resuscitation. Perfusion abnormalities may include, but are not limited to LACTIC ACIDOSIS; OLIGURIA; or acute alteration in mental status.Publishing: "The business or profession of the commercial production and issuance of literature" (Webster's 3d). It includes the publisher, publication processes, editing and editors. Production may be by conventional printing methods or by electronic publishing.

Mannan binding lectin in febrile adults: no correlation with microbial infection and complement activation. (1/88)

AIMS: To study the role of the mannan binding lectin (MBL) pathway of complement activation in the host defence to microbial infection in vivo, and the role of MBL in infectious mortality in non-selected patients. METHODS: A prospective observational study on 177 hospitalised medical patients with new onset fever. The presence, origin, and microbial cause of infection, the circulating MBL and complement activation product 3a (C3a), and the 28 day hospital course were determined. RESULTS: The patients had median MBL values similar to healthy blood donors: 18% of the patients and 14% of the blood donors had MBL deficiency, with values below 0.1 microg/ml. Median C3a was higher in patients with microbiologically confirmed infection than in those without, whereas there was no difference in MBL values or frequency of deficiency among patient groups with or without positive local cultures or bacteraemia. The mortality rate was 8% and the outcome groups did not differ in MBL. In febrile adults hospitalised in internal medicine wards, microbial infection induces complement activation, independently of MBL. CONCLUSIONS: The results argue against a predominant role for the MBL pathway of complement activation and a deficiency of MBL predisposing to serious and invasive microbial infection in non-selected adults.  (+info)

Human mannose-binding lectin and L-ficolin function as specific pattern recognition proteins in the lectin activation pathway of complement. (2/88)

The innate immune response in vertebrates and invertebrates requires the presence of pattern recognition receptors or proteins that recognize microbial cell components including lipopolysaccharide, bacterial peptidoglycan (PGN), and fungal 1,3-beta-D-glucan. We reported previously that PGN and 1,3-beta-D-glucan recognition proteins from insect hemolymph were able to induce the activation of the prophenoloxidase-activating system, one of the major invertebrate innate immune reactions. The goal of this study was to characterize the biochemical properties and effects of the human counterparts of these molecules. Soluble pattern recognition proteins were purified from human serum and identified as human mannose-binding lectin (MBL) and L-ficolin. The use of specific microbial cell component-coupled columns demonstrated that MBL and L-ficolin bind to PGN and 1,3-beta-D-glucan, respectively. Purified MBL and L-ficolin were associated with MBL-associated serine proteases-1 and -2 (MASPs) and small MBL-associated protein as determined by Western blot analysis. Finally, the binding of purified MBL/MASP and L-ficolin/MASP complexes to PGN and 1,3-beta-D-glucan, respectively, resulted in the activation of the lectin-complement pathway. These results indicate that human PGN and 1,3-beta-D-glucan recognition proteins function as complement-activating lectins.  (+info)

Role of mannose-binding lectin in the innate defense against Candida albicans: enhancement of complement activation, but lack of opsonic function, in phagocytosis by human dendritic cells. (3/88)

Mannose-binding lectin (MBL) is a serum collectin believed to be of importance in innate immunity. We have investigated the role of MBL in the first-line defense against Candida albicans, an opportunistic fungal pathogen. MBL bound C. albicans via its lectin domain, resulting in agglutination of the organisms upon their outgrowth of hyphae. In a human in vitro MBL system, deposition of C4 fragments on C. albicans was increased when exogenous MBL was added to serum samples from MBL-deficient individuals. Similar enhancement of deposition of iC3b also was observed. MBL and enhanced opsonic C3 fragments mediated by MBL did not facilitate opsonophagocytosis of the organisms by monocyte-derived dendritic cells (DCs). However, MBL was found to inhibit the growth of C. albicans independently of complement activation, although, with complement activation, further inhibition was observed. We concluded that MBL plays an important role in the first-line defense against C. albicans without the need for opsonophagocytosis by DCs, in which a direct interaction of MBL with C. albicans results in agglutination and accelerated complement activation via the lectin pathway, leading to inhibition of growth.  (+info)

Role of L-ficolin/mannose-binding lectin-associated serine protease complexes in the opsonophagocytosis of type III group B streptococci. (4/88)

Serotype III group B streptococci (GBS) are a common cause of neonatal sepsis and meningitis. Although deficiency in maternal capsular polysaccharide (CPS)-specific IgG correlates with susceptibility of neonates to the GBS infection, serum deficient in CPS-specific IgG mediates significant opsonophagocytosis. This IgG-independent opsonophagocytosis requires activation of the complement pathway, a process requiring the presence of both Ca(2+) and Mg(2+), and is significantly reduced by chelating Ca(2+) with EGTA. In these studies, we defined a role of L-ficolin/mannose-binding lectin-associated serine protease (MASP) complexes in Ca(2+)-dependent, Ab-independent opsonophagocytosis of serotype III GBS. Incubation of GBS with affinity-purified L-ficolin/MASP complexes and C1q-depleted serum deficient in CPS-specific Ab supported opsonophagocytic killing, and this killing was inhibited by fluid-phase N-acetylglucosamine, the ligand for L-ficolin. Binding of L-ficolin was proportional to the CPS content of individual strains, and opsonophagocytic killing and C4 activation were inhibited by fluid-phase CPS, suggesting that L-ficolin binds to CPS. Sialic acid is known to inhibit alternative complement pathway activation, and, as expected, the bactericidal index (percentage of bacteria killed) for individual strains was inversely proportional to the sialic acid content of the CPS, and L-ficolin-initiated opsonophagocytic killing was significantly increased by addition of CPS-specific IgG2, which increased activation of the alternative pathway. We conclude that binding of L-ficolin/MASP complexes to the CPS generates C3 convertase C4b2a, which deposits C3b on GBS. C3b deposited by this lectin pathway forms alternative pathway C3 convertase C3bBb whose activity is enhanced by CPS-specific IgG2, leading to increased opsonophagocytic killing by further deposition of C3b on the GBS.  (+info)

Deficiency of the mannan-binding lectin pathway of complement and poor outcome in cystic fibrosis: bacterial colonization may be decisive for a relationship. (5/88)

In cystic fibrosis (CF) prognosis concerning lung damage development is highly variable and difficult to predict. Mannan-binding lectin (MBL) deficiency has been reported to be associated with poor outcome in CF lung disease. MBL is a recognition molecule of the MBL pathway of the complement system and is encoded by a gene characterized by a high degree of polymorphism. Some genotypes result in low serum concentrations of MBL. MBL-associated serine protease 2 (MASP-2) is another protein belonging to the MBL pathway. A mutation resulting in low levels of MASP-2 in serum has been described recently. In the present study, 112 CF patients aged 4-54 years were investigated for MBL and MASP-2 genotypes, serum levels of MBL and MASP-2 and the MBL pathway function in serum. No correlation to reduced lung function or need for lung transplantation was seen, either for MBL deficiency, MASP-2 gene mutation or reduced MBL pathway function. However, in the 27 patients colonized with Staphylococcus aureus, MBL-deficient genotypes were associated with decreased lung function. As expected, MBL pathway function in serum was reduced both in MBL-deficient patients and in patients carrying a mutant MASP-2 allele. An unexpected finding was that CF patients had higher serum levels of MBL than healthy controls when corrected for MBL genotype. In conclusion, MBL pathway function was affected both by MBL and by MASP-2 genotypes. However, MBL or MASP-2 levels in serum did not affect the clinical outcome in the cohort of CF patients studied.  (+info)

Composition of the lectin pathway of complement in Gallus gallus: absence of mannan-binding lectin-associated serine protease-1 in birds. (6/88)

The lectin pathway of complement is activated by multimolecular complexes that recognize and bind to microbial polysaccharides. These complexes comprise a multimeric carbohydrate recognition subunit (either mannan-binding lectin (MBL) or a ficolin), three MBL-associated serine proteases (MASP-1, -2, and -3), and MAp19 (a truncated product of the MASP-2 gene). In this study we report the cloning of chicken MASP-2, MASP-3, and MAp19 and the organization of their genes and those for chicken MBL and a novel ficolin. Mammals usually possess two MBL genes and two or three ficolin genes, but chickens have only one of each, both of which represent the undiversified ancestors of the mammalian genes. The primary structure of chicken MASP-2 is 54% identical with those of the human and mouse MASP-2, and the organization of its gene is the same as in mammals. MASP-3 is even more conserved; chicken MASP-3 shares approximately 75% of its residues with human and Xenopus MASP-3. It is more widely expressed than other lectin pathway components, suggesting a possible function of MASP-3 different from those of the other components. In mammals, MASP-1 and MASP-3 are alternatively spliced products of a single structural gene. We demonstrate the absence of MASP-1 in birds, possibly caused by the loss of MASP-1-specific exons during phylogeny. Despite the lack of MASP-1-like enzymatic activity in sera of chicken and other birds, avian lectin pathway complexes efficiently activate C4.  (+info)

Gastrointestinal ischemia-reperfusion injury is lectin complement pathway dependent without involving C1q. (7/88)

Complement activation plays an important role in local and remote tissue injury associated with gastrointestinal ischemia-reperfusion (GI/R). The role of the classical and lectin complement pathways in GI/R injury was evaluated using C1q-deficient (C1q KO), MBL-A/C-deficient (MBL-null), complement factor 2- and factor B-deficient (C2/fB KO), and wild-type (WT) mice. Gastrointestinal ischemia (20 min), followed by 3-h reperfusion, induced intestinal and lung injury in C1q KO and WT mice, but not in C2/fB KO mice. Addition of human C2 to C2/fB KO mice significantly restored GI/R injury, demonstrating that GI/R injury is mediated via the lectin and/or classical pathway. Tissue C3 deposition in C1q KO and WT, but not C2/fB KO, mice after GI/R demonstrated that complement was activated in C1q KO mice. GI/R significantly increased serum alanine aminotransferase, gastrointestinal barrier dysfunction, and neutrophil infiltration into the lung and gut in C1q KO and WT, but not C2/fB KO, mice. MBL-null mice displayed little gut injury after GI/R, but lung injury was present. Addition of recombinant human MBL (rhuMBL) to MBL-null mice significantly increased injury compared with MBL-null mice after GI/R and was reversed by anti-MBL mAb treatment. However, MBL-null mice were not protected from secondary lung injury after GI/R. These data demonstrate that C2 and MBL, but not C1q, are necessary for gut injury after GI/R. Lung injury in mice after GI/R is MBL and C1q independent, but C2 dependent, suggesting a potential role for ficolins in this model.  (+info)

Mannose-binding lectin is a regulator of inflammation that accompanies myocardial ischemia and reperfusion injury. (8/88)

The mannose-binding lectin (MBL), a circulating pattern recognition molecule, recognizes a wide range of infectious agents with resultant initiation of the complement cascade in an Ab-independent manner. MBL recognizes infectious non-self and altered self in the guise of apoptotic and necrotic cells. In this study, we demonstrate that mice lacking MBL, and hence are devoid of MBL-dependent lectin pathway activation but have fully active alternative and classical complement pathways, are protected from cardiac reperfusion injury with resultant preservation of cardiac function. Significantly, mice that lack a major component of the classical complement pathway initiation complex (C1q) but have an intact MBL complement pathway, are not protected from injury. These results suggest that the MBL-dependent pathway of complement activation is a key regulator of myocardial reperfusion ischemic injury. MBL is an example of a pattern recognition molecule that plays a dual role in modifying inflammatory responses to sterile and infectious injury.  (+info)

*MASP1 (protein)

"Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin- ... Petersen SV, Thiel S, Jensenius JC (Aug 2001). "The mannan-binding lectin pathway of complement activation: biology and disease ... MASP-1 is a serine protease that functions as a component of the lectin pathway of complement activation. The complement ... the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role ...

*ACAMPs

Collectins (e.g. mannose-binding lectin and surfactant protein A) bind the altered surface sugars on apoptotic cell and enable ... components of complement pathways (e.g. C1q, C3b) and other molecules found in extracellular space. ... lectins (binding the altered sugars), the receptor tyrosine kinase MER (recognizing GAS-6), LRP1 (interacts with calreticulin ... Besides complement particles C1q and C3b which help to opsonize the apoptotic cells, also thrombospondin, pentraxins (C- ...

*List of MeSH codes (G04)

... complement pathway, classical MeSH G04.610.255.849 --- complement pathway, mannose-binding lectin MeSH G04.610.270.070 --- ... binding sites, antibody MeSH G04.610.143.281 --- cross reactions MeSH G04.610.143.545 --- hemolysis MeSH G04.610.143.612 --- ...

*Lectin pathway

The lectin pathway starts with mannose-binding lectin (MBL) or ficolin binding to certain sugars. In this pathway, mannose- ... Classical complement pathway Alternative complement pathway Mannan-binding lectin Wallis R, Mitchell DA, Schmid R, Schwaeble WJ ... In contrast to the classical complement pathway, the lectin pathway does not recognize an antibody bound to its target. ... are bound by MBL. Mannan-binding lectin, also called mannose-binding protein, is a protein belonging to the collectin family ...

*C3a (complement)

The lectin pathway is activated when pattern-recognition receptors, like mannan-binding lectin or ficolins, recognize and bind ... These bound receptors then complex with Mannose-Binding Lectin-Associated Serine Proteases (MASPs), which have proteolytic ... Degn, Søren E.; Thiel, Steffen; Jensenius, Jens C. (2007-01-01). "New perspectives on mannan-binding lectin-mediated complement ... The classical pathway of complement activation is initiated when the C1 complex, made up of C1r and C1s serine proteases, ...

*Complement system

... mannose-binding lectin (MBL), and ficolins, instead of C1q. This pathway is activated by binding of MBL to mannose residues on ... the classical complement pathway, the alternative complement pathway, and the lectin pathway. In 1888, George Nuttall found ... The mannose-binding lectin pathway can be activated by C3 hydrolysis or antigens without the presence of antibodies (non- ... Polymorphisms of complement component 3, complement factor B, and complement factor I, as well as deletion of complement factor ...

*MASP2 (protein)

"Selective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin- ... Mannan-binding lectin Mannan-binding lectin pathway (lectin pathway) GRCh38: Ensembl release 89: ENSG00000009724 - Ensembl, May ... Petersen SV, Thiel S, Jensenius JC (2001). "The mannan-binding lectin pathway of complement activation: biology and disease ... Mannan-binding lectin serine protease 2 also known as mannose-binding protein-associated serine protease 2 (MASP-2) is an ...

*Mannan-binding lectin

... and the lectin pathway. One way that the most-recently discovered lectin pathway is activated is through mannose-binding lectin ... Binding of MBL to a micro-organism results in activation of the lectin pathway of the complement system. Another important ... Mannose-binding lectin (MBL), also called mannose-binding protein or mannan-binding protein (MBP), is a lectin that is ... The complement system can be activated through three pathways: the classical pathway, the alternative pathway, ...

*Humoral immunity

... the classical complement pathway, the alternate complement pathway, and the mannose-binding lectin pathway. The classical ... 12 of which are directly involved in the complement pathways. The complement system is involved in the activities of both ... The complement system consists of more than 35 soluble and cell-bound proteins, ... The B cell waits for the TH cell to bind to the complex and this binding will activate TH cell and it releases cytokines that ...

*Map44

... mannan-binding lectin lectin pathway Degn, Søren; Annette G. Hansen; Rudi Steffensen; Christian Jacobsen; Jens C. Jensenius; ... Mannose-binding lectin-associated protein of 44 kDa (MAp44) is a protein arising from the human MASP1 gene. MASP-1, MASP-3 and ... Protein Associated with Pattern Recognition Molecules of the Complement System and Regulating the Lectin Pathway of Complement ... MAp44 has been suggested to act as a competitive inhibitor of lectin pathway activation, by displacing MASP-2 from MBL, hence ...

*Complement system

Lectin pathway. The lectin pathway is homologous to the classical pathway, but with the opsonin, mannose-binding lectin (MBL), ... Three biochemical pathways activate the complement system: the classical complement pathway, the alternative complement pathway ... The mannose-binding lectin pathway can be activated by C3 hydrolysis or antigens without the presence of antibodies (non- ... Alternative pathwayEdit. Main article: Alternative complement pathway. The alternative pathway is continuously activated at a ...

*C3-convertase

... in response to binding to CRP or immunoglobulin, and in the lectin pathway it is driven by mannose binding lectin and its ... lectin, and alternative pathways. Cleavage of complement C3 by a free floating convertase, thrombin, plasmin or even a ... Binding β1H to C3b increases C3bINA binding, while factor B binding prevents C3bINA binding and is competitive with β1H binding ... C4 binding protein (C4BP) interferes with the assembly of the membrane-bound C3 convertase of the classical pathway. C4BP is a ...

*Opsonin

IgM antibodies also bind to PC. Collectin molecules such as mannose-binding lectin (MBL), surfactant protein A (SP-A), and SP-D ... C3b can spontaneously bind to pathogen surfaces through the alternative complement pathway. Furthermore, pentraxins can ... C3b, C4b, and C1q are important complement molecules that serve as opsonins. As a part of the alternative complement pathway, ... The antigen-antibody complex can also activate complement through the classical complement pathway. Phagocytic cells do not ...

*Malpuech facial clefting syndrome

Both genes encode proteins of the lectin complement pathway, which plays a role in the complement system of innate, or non- ... "Mannose binding lectin (MBL) and HIV". Molecular Immunology. 42 (2): 145-52. doi:10.1016/j.molimm.2004.06.015. PMID 15488604. ... The protein is a type of connectin called a mannan-binding lectin, which plays a role in innate immunity by binding to ... "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome". Nature Genetics. 43 (3): 197-203. doi: ...

*Humoral immunity

... the classical complement pathway, the alternate complement pathway, and the mannose-binding lectin pathway. The classical ... Complement system[edit]. Main article: Complement system. The complement system is a biochemical cascade of the innate immune ... 12 of which are directly involved in the complement pathways.[1] The complement system is involved in the activities of both ... The B cell waits for the TH cell to bind to the complex. This binding will activate TH cell and it releases cytokines that ...

*LMAN1

2003). "High mannose glycans and sialic acid on gp120 regulate binding of mannose-binding lectin (MBL) to HIV type 1". AIDS Res ... The protein is a mannose-specific lectin and is a member of a novel family of plant lectin homologs in the secretory pathway of ... 1994). "Complement activation upon binding of mannan-binding protein to HIV envelope glycoproteins". AIDS. 7 (10): 1307-13. doi ... "Entrez Gene: LMAN1 lectin, mannose-binding, 1". Khoriaty R, Vasievich MP, Ginsburg D., Blood. 2012 Jul 5;120(1):31-8. doi: ...

*Collectin

... s are linked with activation of lectin pathway of complement activation. At the beginning, there is a binding of ... Nine types of collectins have been defined: MBL = mannan-binding lectin (mannose-binding lectin) SP-A = surfactant protein A SP ... "The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation ... "The mannan-binding lectin-associated serine proteases (MASPs) and MAp19: four components of the lectin pathway activation ...

*Humoral immunity

... the classical complement pathway, the alternate complement pathway, and the mannose-binding lectin pathway. The classical ... Complement systemEdit. Main article: Complement system. The complement system is a biochemical cascade of the innate immune ... 12 of which are directly involved in the complement pathways.[1] The complement system is involved in the activities of both ... The B cell waits for the TH cell to bind to the complex. This binding will activate TH cell and it releases cytokines that ...

*Chromosome 5 (human)

Lectin mannose binding 2 LNCR3 encoding protein Lung cancer susceptibility 3 LPCAT1: Lysophosphatidylcholine acyltransferase 1 ... Complement C1q tumor necrosis factor-related protein 3 C5orf3: encoding protein FAM114A2 C5orf13: Neuronal regeneration related ... encodes G protein-coupled receptor protein signaling pathway YIPF5: Yip1 domain family member 5 YTHDC2: encoding protein YTH ... Purine-rich element-binding protein A PWWP2A: encoding protein PWWP domain containing 2A RANBP3L: encoding protein RAN binding ...

*Mannan-binding lectin-associated serine protease-2

Matsushita, M.; Fujita, T. (1992). "Activation of the classical complement pathway by mannose-binding protein in association ... mannose-binding lectin-associated serine protease-2, p100, mannan-binding lectin-associated serine peptidase 2) is an enzyme. ... and after Arg76 in complement component C4 (-Gly-Leu-Gln-Arg-Ala-Leu-Glu-Ile) This mannan-binding lectin (MBL) recognizes ... "A second serine protease associated with mannan-binding lectin that activates complement". Nature. 386 (6624): 506-510. doi: ...

*Outline of immunology

... system Complement system Classical complement pathway Mannan-binding lectin pathway Alternate complement pathway Complement ... C-type lectin receptors (CLRs) Group 1 CLRs - Mannose receptors MRC1 MRC2 DEC205 (CD205) Group 2 CLRs - Asialoglycoprotein ... C4a C2 Mannan-binding lectin pathway MASP1 / MASP2 Mannan-binding lectin Alternative complement pathway Factor B Factor D ... Secreted PRRs Complement system (see complement proteins section) Collectins Mannan-binding lectin (MBL) Surfactant protein A ( ...

*Dengue fever

Examples include the genes coding for the proteins known as TNFα, mannan-binding lectin, CTLA4, TGFβ, DC-SIGN, PLCE1, and ... specifically the C-type lectins called DC-SIGN, mannose receptor and CLEC5A. DC-SIGN, a non-specific receptor for foreign ... and various lines of research have implied a role for T cells and soluble factors such as cytokines and the complement system. ... through the innate immune system by augmenting the production of a large group of proteins mediated by the JAK-STAT pathway. ...

*Kolektin - Wikipedie

Selander B, Mårtensson U, Weintraub A (2006). "Mannan-binding lectin activates C3 and the alternative complement pathway ... Jack DL, Read RC, Tenner AJ (2001). "Mannose-Binding Lectin Regulates the Inflammatory Response of Human Professional ... Hartshorn KL, Sastry K, White MR, (1993). "Human Mannose-binding Protein Functions as an Opsonin for Influenza A Viruses". J. ... Watford WT, Ghio AJ, Wright JR (2000). "Complement-mediated host defense in the lung". Am J Physiol Lung Cell Mol Physiol 279: ...

*Complement component 1s

"Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates". Journal of Immunology. 161 (9): 4924- ... complement activation, lectin pathway. • complement activation. • regulation of complement activation. Sources:Amigo / QuickGO ... Complement component 1s (EC 3.4.21.42, C1 esterase, activated complement C1s, complement C overbar 1r, C1s) is a protein ... protein binding. • hydrolase activity. • metal ion binding. • identical protein binding. • serine-type endopeptidase activity. ...

*Pattern recognition receptor

Once bound to the ligands MBL and Ficolin oligomers recruit MASP1 and MASP2 and initiate the lectin pathway of complement ... Dommett RM, Klein N, Turner MW (September 2006). "Mannose-binding lectin in innate immunity: past, present and future". Tissue ... One very important collectin is mannan-binding lectin (MBL), a major PRR of the innate immune system that binds to a wide range ... Membrane-bound PRRs include Toll like receptors (TLRs) and C-type lectin receptors (CLRs). Cytoplasmic PRRs include NOD-like ...

*Sialic acid

... can "hide" mannose antigens on the surface of host cells or bacteria from mannose-binding lectin.[citation needed] ... Fulcher CA, "MetaCyc Chimeric Pathway: superpathway of sialic acid and CMP-sialic acid biosynthesis", "MetaCyc, March 2009" ... This prevents activation of complement. Sialic acid in the form of polysialic acid is an unusual posttranslational modification ... The alpha-anomer is the form that is found when sialic acid is bound to glycans. However, in solution, it is mainly (over 90%) ...

*Glycosylation

... via sugar-binding proteins called lectins, which recognize specific carbohydrate moieties.[1] Glycosylation is an important ... A mannose sugar is added to the first tryptophan residue in the sequence W-X-X-W (W indicates tryptophan; X is any amino acid ... disorders of lipid glycosylation and disorders of other glycosylation pathways and of multiple glycosylation pathways. No ... the first crystal structure of a protein containing this type of glycosylation has been determined-that of human complement ...

*Natasha Anwar

... the ability of mannose binding lectin, a component of the immune system involved in the lectin pathway of opsonization, to bind ... "Activation of complement by mannose-binding lectin on isogenic mutants of Neisseria meningitidis serogroup B". Journal of ... In addition, activation of the lectin pathway of opsonization had also been detected by the presence of a cleaved product. Both ... It was found that when the outer core was removed, strong binding of MBL to N. meningitidis was detected, even when ...
Rooryck C, Diaz-Font A, Osborn DP, Chabchoub E, Hernandez-Hernandez V, Shamseldin H, Kenny J, Waters A, Jenkins D, Kaissi AA, Leal GF, Dallapiccola B, Carnevale F, Bitner-Glindzicz M, Lees M, Hennekam R, Stanier P, Burns AJ, Peeters H, Alkuraya FS, Beales PL. Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome. Nat Genet. 2011 Mar;43(3):197-203.. ...
(lek tin) The lectin pathway for complement activation is triggered by the binding of a serum lectin (mannan binding lectin; MBL) to mannose containing proteins or to carbohydrates on viruses or bacteria
The complement system plays a key role in host defense against pneumococcal infection. Three different pathways, the classical, alternative and lectin pathways, mediate complement activation. While there is limited information available on the roles of the classical and the alternative activation pathways of complement in fighting streptococcal infection, little is known about the role of the lectin pathway, mainly due to the lack of appropriate experimental models of lectin pathway deficiency. We have recently established a mouse strain deficient of the lectin pathway effector enzyme mannan-binding lectin associated serine protease-2 (MASP-2) and shown that this mouse strain is unable to form the lectin pathway specific C3 and C5 convertases. Here we report that MASP-2 deficient mice (which can still activate complement via the classical pathway and the alternative pathway) are highly susceptible to pneumococcal infection and fail to opsonize Streptococcus pneumoniae in the none-immune host. ...
Principal Investigator:MATSUSHITA Misao, Project Period (FY):1996 - 1997, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Immunology
Microbial infection urges prompt intervention by the immune system. The complement cascade and neutrophil granulocytes are the predominant contributors to this immediate anti-microbial action. We have previously shown that mannan-binding lectin-associated serine protease-1 (MASP-1), the most abundant enzyme of the complement lectin pathway, can induce p38-MAPK activation, NFkappaB signaling, and Ca2+-mobilization in endothelial cells. Since neutrophil chemotaxis and transmigration depends on endothelial cell activation, we aimed to explore whether recombinant MASP-1 (rMASP-1) is able to induce cytokine production and subsequent neutrophil chemotaxis in human umbilical vein endothelial cells (HUVEC). We found that HUVECs activated by rMASP-1 secreted IL-6 and IL-8, but not IL-1alpha, IL-1ra, TNFalpha and MCP-1. rMASP-1 induced dose-dependent IL-6 and IL-8 production with different kinetics. rMASP-1 triggered IL-6 and IL-8 production was regulated predominantly by the p38-MAPK pathway. Moreover, the
BioMed Research International is a peer-reviewed, Open Access journal that publishes original research articles, review articles, and clinical studies covering a wide range of subjects in life sciences and medicine. The journal is divided into 55 subject areas.
Omeros Corporation is a biopharmaceutical company engaged in discovering, developing and commercializing small-molecule and protein therapeutics for market, as well as orphan indications targeting inflammation, coagulopathies and disorders of the central nervous system. The Companys marketed drug product, Omidria (phenylephrine and ketorolac injection), is used during cataract surgery or intraocular lens replacement. Its clinical programs include Mannan-binding lectin-associated serine protease-2 (MASP-2) (OMS721)-Lectin Pathway Disorders; PDE10 (OMS824)-CNS Disorders; peroxisome proliferator-activated receptor gamma (PPARy) (OMS405)-Addiction, and OMS201-Urology. Its preclinical programs include phosphodiesterase 7 (PDE7) (OMS527), Plasmin (OMS616), MASP-3 (OMS906)-Alternative Pathway Disorders, GPR17-CNS Disorders, GPR101-Metabolic Disorders, GPR151-CNS Disorders, GPR161-Cancer, GPR174-Immune Disorders, GPR183-Skeletal and Infectious Diseases, GPCR Platform and Antibody Platform.. ...
The complement system constitutes a critical component of the innate immune response. The lectin pathway is one of the three activation pathways of the complement activation cascade that can recognise and respond to structures on oxygen deprived cells and contribute to ischaemia and reperfusion injury (IRI). Cerebral IRI mediated inflammation is known to be responsible for secondary damage in the penumbra region surrounding the initial area of infarct and the prevention of IRI-mediated secondary damage provides an attractive target for therapeutic intervention. Mannose binding lectin associated serine protease 2 (MASP-2) is the key effector enzyme of the lectin pathway, since depletion of this enzyme completely ablates lectin pathway function or activity. This study assessed the impact of MASP-2 deficiency on cerebral IRI and to what extent MASP-2 targeting can reduce the secondary inflammatory damage following an ischaemic insult. The 3 vessel occlusion (3-VO) model of stroke was found to be ...
Background and Aim: Mannose binding-lectin (MBL) is an important component of innate immunity, and activator of the lectin complement pathway. Within the MBL2 gene are seven "secretor" haplotypes that code for altered serum MBL levels and complement activation. As complement is important in the pathophysiology of myocardial injury, we determined if MBL2 secretor haplotypes are independently associated with an increased risk of in-hospital, postoperative MI in patients undergoing CABG surgery.. Methods: Prospective, longitudinal multi-institutional study of 978 patients undergoing primary, elective CABG-only surgery with cardiopulmonary bypass between 8/2001 and 5/2005. Genotyping of 18 polymorphic sites within the MBL2 gene was performed at the National Cancer Institute using Sequenom MALDI-TOF. Multivariate, stepwise logistic regression was performed controlling for patient demographics, preoperative risk factors, medications and intraoperative variables to determine if MBL2 secretor haplotypes ...
1Q3X: The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
My daughter was just diagnosed with a MBL (mannose-binding lectin) deficiency. She is 6 years old now and has been plagued by multiple pneumonias and sinus infections. What is the prognosis of this def...
MBL : Evaluation of children and adults with a clinical history of recurrent infections Results may be useful for genetic counseling and support aggressive management of recurrent infections in patients with reduced levels of mannose-binding lectin
Sigma-Aldrich offers abstracts and full-text articles by [Michael Osthoff, Melinda M Dean, Paul N Baird, Andrea J Richardson, Mark Daniell, Robyn H Guymer, Damon P Eisen].
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
摘要 利用Bac-to-Bac昆虫杆状病毒表达系统表达具有天然构象的猪Ficolin α。首先构建重组穿梭质粒rBacmid-Ficolin α,转染sf9细胞获得重组杆状病毒rBV-Ficolin α;通过Image J软件对优化表达的Western blot图片进行灰度分析确定较佳表达条件;纯化目的蛋白质后,进一步评价其体外抗病毒活性。Western blot结果显示以7.5 MOI接种量感染的sf9细胞在96 h时获得了较高的表达,同时获得的重组猪Ficolin α具有抗猪繁殖与呼吸综合征病毒(PRRSV)活性。猪Ficolin α在sf9昆虫细胞中获得成功表达,且具有良好的抗PRRSV活性。本研究可以为猪Ficolin α的抗病毒活性及作用机制研究提供物质基础。. ...
Hi, a little bit of background - 27 yr. old female. Drink once a week and ex-smoker. Medications currently taking Multi-vitamin w/ numerous supplements, Nasonex, Xananx on occassion, Allegra-D on occa...
MBL forms oligomers of subunits, which are trimers (6- to 18-heades correspond to a dimer and a hexamer, respectively). Multimers of MBL form a complex with MASP1 (Mannose-binding lectin-Associated Serine Protease), MASP2 and MASP3, that are protease zymogens. The MASPs are very similar to C1r and C1s molecules of the classical complement pathway, respectively, and are thought to have a common evolutionary ancestor. When the carbohydrate-recognising heads of MBL bind to specifically arranged mannose residues on the surface of a pathogen, MASP-1 and MASP-2 are activated to cleave complement components C4 and C2 into C4a, C4b, C2a, and C2b. In addition, two smaller MBL-associated proteins (MAps) are found in complex with MBL. MBL-associated protein of 19 kDa (MAp19) and MBL-associated protein of 44 kDa (Map44). MASP-1, MASP-3 and MAp44 are alternative splice products of the MASP1 gene, while MASP-2 and MAp19 are alternative splice products of the MASP-2 gene. MAp44 has been suggested to act as a ...
Jenny, Lorenz and Dobó, József and Gál, Péter and Pál, Gábor and Lam, Wilbur A. and Schroeder, Verena (2018) MASP-1 of the complement system enhances clot formation in a microvascular whole blood flow model. PLOS ONE, 13 (1). pp. 1-14. ISSN 1932-6203 Oroszlán, Gábor and Dani, Ráhel and Szilágyi, András and Závodszky, Péter and Thiel, Steffen and Gál, Péter and Dobó, József (2017) Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic Modeling of Lectin Pathway Activation Provides Possible Mechanism. FRONTIERS IN IMMUNOLOGY, 8. pp. 1-14. ISSN 1664-3224 Tóbiás, Zoltán and Pálinkó, Dóra and Sztanó, Balázs and Csanády, Miklós and Gál, Péter and Rovó, László (2017) A laryngomalacia endoszkópos ultrapulzációs-lézeres (ultra dream pulse) sebészete. A módszer hazai bevezetése során szerzett tapasztalataink , Endoscopic ultra dream pulse laser surgery of laryngomalacia. Our experiences gained during the ...
Several common mutations of the MBL2 gene can lead to a condition called mannose-binding lectin deficiency. People with this condition have low levels of mannose-binding lectin and may be susceptible to recurrent infections. Several of the disease-associated mutations occur in a region of the MBL2 gene known as exon 1 and result in a change to single protein building blocks (amino acids) in the mannose-binding lectin subunit. Other mutations occur in an area of DNA near the MBL2 gene called the promoter region, which helps control the production of the mannose-binding lectin subunit.. The change of a single amino acid in the mannose-binding lectin subunit eliminates its ability to assemble into the functional mannose-binding lectin. Similarly, certain mutations in the promoter region of the MBL2 gene reduce production of the mannose-binding lectin subunit, leading to a decreased number of subunits available for protein assembly and a reduction in the amount of functional protein. With decreased ...
The high degree of parallelism in complement activation hinders a better understanding of the individual roles and relative importance of the three activation pathways both in physiological as well as in pathological processes. Specific inhibitors are extremely useful tools for basic research and therapeutic purposes. Previously, there were attempts to develop pathway-selective inhibitors by preventing the binding of the recognition molecules (C1q and MBL) to their targets (50, 51). Each activation pathway is associated with unique proteases, which could be appropriate targets for such inhibitors. Although SPs are among the most druggable targets of the complement system, early drug development efforts failed to yield specific complement inhibitors (21).. There are several X-ray structures of complement initiator proteases, but none of these present the protease in complex with an interacting peptide substrate or inhibitor (38-40, 52, 53). Without such a binding partner, the functional binding ...
Functional mannose-binding lectin (f-MBL) plays an important role in the innate neonatal immune system. We studied the origin of f-MBL in umbilical cord blood (UCB) by measuring maternal MBL (n=47), collected before elective cesarean section, and neo
Blotting, Western; Calcium; Cells, Cultured; Complement Activation; Complement Pathway, Mannose-Binding Lectin; Human Umbilical Vein Endothelial Cells; Humans; Immunity, Innate; Mannose-Binding Lectin; Mannose-Binding Protein-Associated Serine Proteases; Microscopy, Fluorescence; Mutation; Peptide Fragments; Protein Binding; Proteolysis; Recombinant Proteins ...
Innate immunity relies upon the ability of a variety of recognition molecules to sense pathogens through conserved molecular signatures that are often carbohydrates. Ficolins are oligomeric proteins assembled from collagen-like stalks and fibrinogen-
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Hi Everyone, Three weeks ago, I found out from Gareths Immunologist that he has MBL deficiency --- Mannose-binding Lectin deficiency. From what I have b...
Low lectin foods - what can a very low level of mannose-binding lectin mean and how can it be treated? a rare. deficiency to affect someone clinically,
MBL-C antibody [14D12] (mannose-binding lectin (protein C) 2) for IA, ICC/IF, IHC-Fr, WB. Anti-MBL-C mAb (GTX54388) is tested in Mouse samples. 100% Ab-Assurance.
MBL-C antibody, C-term (mannose-binding lectin (protein C) 2, soluble) for WB. Anti-MBL-C pAb (GTX89586) is tested in Human samples. 100% Ab-Assurance.
Ficolin-3 Isoform 2 products available through Novus Biologicals. Browse our Ficolin-3 Isoform 2 product catalog backed by our Guarantee+.
多种适用的MBL2ELISA试剂盒,如小鸡, Cow, 人等。在antibodies-online.cn对比MBL2ELISA试剂盒,以便找到您需要的产品。
Mannose binding lectin (MBL) is an important host defence protein against opportunistic fungal pathogens. This carbohydrate-binding protein, an opsonin and lectin pathway activator, binds through multiple lectin domains to the repeating sugar arrays displayed on the surface of a wide range of clinically relevant microbial species. We investigated the contribution of MBL to antifungal innate immunity towards C. parapsilosis in vitro. High avidity binding was observed between MBL and C. albicans and C. parapsilosis. Addition of MBL to MBL deficient serum increased the deposition of C4 and C3b and enhanced the uptake of C. albicans, C. parapsilosis and acapsular C. neoformans by polymorphonuclear cells (PMNs). Compared to other microorganisms, such as Escherichia coli, Staphylococcus aureus and Cryptococcus neoformans, C. parapsilosis and Candida albicans were potent activators of the lectin pathway. Our results suggest that MBL plays a crucial role in the innate immunity against infections caused by yeast
This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants.[provided by RefSeq, Apr 2010 ...
Mannan Binding Lectin (MBL) is a member of the lectin pathway of the complement system and plays an important role in the innate immune system. MBL replacement in MBL-deficient children with chemotherapy-induced neutropenia represents a new approach to lower the risk of febrile episodes, of hospital admission, of prolonged use of intravenous antibiotics and of severe infections.. The aim of the Phase II study is to find evidence for the correct prediction of plasma levels of MBL necessary for clinical effects and biological efficacy, to confirm the dosage regimen needed to reach the required MBL plasma levels, and reconfirm the safety and lack of side-effects. ...
Mannan-Binding lectin (MBL) is a serum lectin and an important constituent of the innate immune system. Processes linked to the innate immune response have previously been implicated in Alzheimers disease (AD). MBL is associated with blood vessels in the brain and AD patients demonstrate lower MBL levels in the cerebrospinal fluid compared to controls. We investigated six single nucleotide polymorphisms, linked to MBL deficiency, in the corresponding MBL2 gene in AD patients and controls. Two MBL2 haplotypes, LXP and LYQ, were significantly associated with AD risk (OR = 1.6, p = 0.01 and OR = 1.5, p = 0.02, respectively). The present study is the first investigating MBL2 genotypes and haplotypes in relation to AD. Our findings support that the MBL2 gene impact the disease risk.
This unit contains protocols that can be used to measure mannan‐binding lectin (MBL) levels and MBL pathway activity in human plasma or serum
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Background: Mannose-binding lectin is a collectin involved in host defense against infection. Whether mannose-binding lectin deficiency is associated with acute exacerbations of chronic obstructive pulmonary disease is debated. Methods: Participants in a ...
A komplement rendszer aktiválódásának lektin útja az egyik első védelmi vonalnak tekinthető a szervezet fertőzések elleni védekezésében. A mannóz kötő lektin (MBL) baktérium felszínhez való kötődése után szerin proteáz zimogének (MASP= MBL-kötött szerin proteáz) aktiválódnak, melyek többféle mechanizmus révén járulnak hozzá az idegen mikroorganizmus megsemmisítéséhez ill. eltávolításához. Munkánk során felderítettük, a proteolitikus kaszkádrendszer beindításáért felelős MASP-2 enzim autoaktiválódásásnak mechanizmusát atomi szinten. Felfedeztük a MASP-2 egy eddig ismeretlen biológiai funkcióját, amely kapcsolatot teremt a véralvadási és a komplement kaszkád között. A MASP-2 hasítja és aktiválja a protrombint. Ugyancsak részletesen tanulmányoztuk a MASP-1 trombin-szerű aktivitását is. Ezek az eredmények arra utalnak, hogy a vérben lévő két proteolitikus kaszkádrendszer szoros evolúciós és funkcionális ...
pep:known chromosome:VEGA66:18:65980754:66002637:-1 gene:OTTMUSG00000030654 transcript:OTTMUST00000075892 gene_biotype:protein_coding transcript_biotype:protein_coding gene_symbol:Lman1 description:lectin, mannose-binding, 1 ...
RATIONALE: Recombinant human mannose-binding lectin (MBL) may be effective in preventing infection in young patients with fever and neutropenia receivin
Atherosclerosis is a chronic inflammatory disorder that is characterized by the accumulation of modified lipoproteins in the arterial intima. C1q and mannan-binding lectin (MBL) are not only recognition components involved in activation of inflammation via the complement cascade, but they are also able to directly modulate phagocyte activation. Studies in C1q−/− and MBL−/− mice suggest that these molecules play a protective role in the early atherosclerotic lesion in the absence of, or prior to, expression of other complement components. However, in later stages, complement activation becomes an inappropriate inflammatory response, contributing to disease pathology. Therefore, to investigate possible molecular interactions of C1q and MBL in atherosclerotic lesions, we examined the influence of C1q and MBL in the clearance of native and modified lipoproteins by human monocytes and monocyte-derived macrophages. Both C1q and MBL are shown to bind and enhance the monocyte/monocyte-derived ...
Download Free Full-Text of an article Serum mannan-binding lectin in patients with pulmonary tuberculosis: Its lack of a relationship to the disease and response to treatment
Ficolin-3 is a protein that in humans is encoded by the FCN3 gene. Ficolin-3 was initially identified as H-ficolin, in which H is after the Hakata antigen that was previously found as an autoantigen in patients who lived in the city of Hakata. Ficolins are a group of proteins which consist of a collagen-like domain and a fibrinogen-like domain. In human serum, there are two types of ficolins, both of which have lectin activity. The protein encoded by this gene is a thermolabile beta-2-macroglycoprotein found in all human serum and is a member of the ficolin/opsonin p35 lectin family. The protein, which was initially identified based on its reactivity with sera from patients with systemic lupus erythematosus, has been shown to have a calcium-independent lectin activity. The protein can activate the complement pathway in association with MASPs and sMAP, thereby aiding in host defense through the activation of the lectin pathway. Alternative splicing occurs at this locus and two variants, each ...
(= MBL; formerly mannan binding protein, MBP) Plasma protein (32 kD) structurally related to complement C1, that binds specific carbohydrates (mannans) on the surface of various microorganisms including bacteria, yeasts, parasitic protozoa, and…
Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity (By similarity). Inhibits the biological activity of mature myostatin, but not activin.
Protease-inhibitor that contains multiple distinct protease inhibitor domains. Probably has serine protease- and metalloprotease-inhibitor activity. Inhibits the biological activity of mature myostatin, but not activin (By similarity).
SEATTLE--(BUSINESS WIRE)--Omeros Corporation (NASDAQ: OMER) today announced that the US Food and Drug Administration (FDA) has granted breakthrough therapy designation to OMS721 for the treatment of Immunoglobulin A (IgA) nephropathy. OMS721 is Omeros lead human monoclonal antibody targeting mannan-binding lectin
Corals form the framework of the worlds coral reefs and are under threat from increases in disease and bleaching (symbiotic dysfunction), yet the mechanisms of pathogen and symbiont recognition remain largely unknown. Here we describe the isolation and characterisation of an ancient mannose-binding lectin in the coral Acropora millepora, which is likely to be involved in both processes. The lectin (Millectin) was isolated by affinity chromatography and was shown to bind to bacterial pathogens as well as coral symbionts, dinoflagellates of the genus Symbiodinium. cDNA analysis of Millectin indicate extensive sequence variation in the binding region, reflecting its ability to recognise various mannose-like carbohydrate structures on non-self cells, including symbionts and pathogens. This is the first mannose-binding lectin to show extensive sequence variability as observed for pattern recognition proteins in other invertebrate immune systems and, given that invertebrates rely on non-adaptive ...
We previously reported an association between relative L-ficolin deficiency and recurrent respiratory infections co-existing with allergic disorders in children. To confirm and extend this preliminary finding, we performed a prospective study on children of a similar age (mean 8.9 years) designed to establish whether the principal relationship was with infection or allergy. Serum L-ficolin values in healthy children were normally distributed with a mean value of 3838 ng/ml. L-ficolin concentrations were generally lower in patients with asthma and/or allergic rhinitis with (mean 3413 ng/ml; p=0.02) or without (3512 ng/ml; p|0.07) respiratory infections, but not in patients with respiratory infections without allergic disease (3623 ng/ml; p=0.2). The lower average values in the group comprised of children with respiratory allergy and infections were largely due to a high proportion of very low values: 18.3% had values below 2150 ng/ml compared to only 5.5% of healthy controls (OR=3.9; p=0.01). This
Ser Leu Ser Lys1 5 10 15Ala Ser Ala His Thr Val Glu Leu Asn Asn Met Phe Gly Gln Ile Gln 20 25 30Ser Pro Gly Tyr Pro Asp Ser Tyr Pro Ser Asp Ser Glu Val Thr Trp 35 40 45Asn Ile Thr Val Pro Asp Gly Phe Arg Ile Lys Leu Tyr Phe Met His 50 55 60Phe Asn Leu Glu Ser Ser Tyr Leu Cys Glu Tyr Asp Tyr Val Lys Val65 70 75 80Glu Thr Glu Asp Gln Val Leu Ala Thr Phe Cys Gly Arg Glu Thr Thr 85 90 95Asp Thr Glu Gln Thr Pro Gly Gln Glu Val Val Leu Ser Pro Gly Ser 100 105 110Phe Met Ser Ile Thr Phe Arg Ser Asp Phe Ser Asn Glu Glu Arg Phe 115 120 125Thr Gly Phe Asp Ala His Tyr Met Ala Val Asp Val Asp Glu Cys Lys 130 135 140Glu Arg Glu Asp Glu Glu Leu Ser Cys Asp His Tyr Cys His Asn Tyr145 150 155 160Ile Gly Gly Tyr Tyr Cys Ser Cys Arg Phe Gly Tyr Ile Leu His Thr 165 170 175Asp Asn Arg Thr Cys Arg Val Glu Cys Ser Asp Asn Leu Phe Thr Gln 180 185 190Arg Thr Gly Val Ile Thr Ser Pro Asp Phe Pro Asn Pro Tyr Pro Lys 195 200 205Ser Ser Glu Cys Leu Tyr Thr Ile Glu Leu Glu Glu Gly Phe Met Val 210 215 220Asn Leu Gln Phe Glu ...
Your trusted lab partner for Mannan Binding Lectin (MBL) testing, Viracor Eurofins delivers your results faster, when it matters most.
With enhanced promotor, Mannan Binding Lectin / MBL2 cDNA ORF Clone, Mouse in pCMV3-C-OFPSpark is expression-ready, and confirmed by full-length sequence & expression validation
Eisen, Damon P., Dean, Melinda M., Boermeester, Marja A., Fidler, Katy J., Gordon, Anthony C., Kronborg, Gitte, Kun, Jürgen F.J., Lau, Yu Lung, Payeras, Antonis, Valdimarsson, Helgi, Brett, Stephen J., Mila, Joan, Ip, W.K. Eddie, Peters, Mark J., Saevarsdottir, Saedis, van Till, J.W. Oliver, Hinds, Charles J., and McBryde, Emma S. (2008) Low serum mannose‐binding lectin level increases the risk of death due to pneumococcal infection. Clinical Infectious Diseases, ...
Since an initial publication in 1998, population-based studies identified mannose-binding lectin (MBL) as a modifier of atherosclerosis development; both proatherogenic and antiatherogenic roles of MBL were demonstrated. However, as stated by G.K. Hansson in his 2006 Arteriosclerosis, Thrombosis, and Vascular Biology editorial, "confusion prevails." The mechanisms by which MBL influences atherosclerosis development are unknown, and epidemiological data are conflicting, emphasizing the need for additional experimental studies. MBL is considered to be an important initiating complement component with immune regulatory properties and considerable variation in plasma levels between individuals. Its function ranges from complement activation to the MBL-mediated uptake of late apoptotic cells, cellular debris, and foreign organisms by macrophages. In the present study, local MBL-A and MBL-C gene expressions were demonstrated in murine atherosclerotic lesions. Interestingly, mice carrying MBL-A and -C ...
Mannose-binding lectin deficiency linked to cytomegalovirus (CMV) reactivation and survival in lung transplantation (pages 410-416). J. M. Kwakkel-van Erp, A. W. M. Paantjens, D. A. van Kessel, J. C. Grutters, J. M. M. van den Bosch, E. A. van de Graaf and H. G. Otten. Version of Record online: 27 JUN 2011 , DOI: 10.1111/j.1365-2249.2011.04436.x. ...
Draw blood in a plain red-top tube(s), serum gel tube(s) is acceptable. Spin down and send 1 mL of serum frozen in a plastic vial.
Mannose-binding lectin status is associated with risk of major infection following myeloablative sibling allogeneic hematopoietic stem cell transplantation
Mannose-binding protein is a component of the innate or natural immune system which binds to mannose residues on a variety of different microorganisms. When bound, this lectin will trigger the complement pathway resulting in opsonization. Mannose-binding protein is also an acute phase reactant produced by the liver. Patients who have abnormal levels of mannose-binding protein may have recurrent significant infections in the absence of abnormalities in the four major arms of the immune system. Abnormal mannose-binding protein concentrations have been found in patients with infectious disorders such as tuberculosis, hepatitis B, and in autoimmune disorders including recurrent spontaneous abortion and systemic lupus erythematosis ...
Read "Obtaining and refolding a recombinant mannan-binding lectin from the holothurian Apostichopus japonicus, Russian Journal of Marine Biology" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Alleles; Carrier Proteins; Collectins; Complement Activation; Gene Frequency; Genetic Predisposition to Disease; Humans; Mannans; Meningococcal Infections ...
To model gene profiles in the early phases of a systemic infection, we administered endotoxin to normal volunteers and measured serial changes in gene expression in PBMC and whole blood. The greatest changes occurred by 6 h and resolved by 24 h. Exposure to a single microbial component resulted in a rich variety of changes in gene expression including the induction of genes associated with pattern recognition molecules, signal transduction, transcription factors, cell mobility, cell proliferation, and microbial killing, the downregulation of lymphocyte-associated genes, and expression of genes not previously associated with endotoxemia or acute inflammation. The endotoxin phenotype did not persist in the blood transcriptome at 24 h. This broad and rapid on-off response of gene expression is in stark contrast to the sustained inflammatory phenotype that occurs during clinical sepsis, due in part to continued exposure to microbial components with recruitment of pathways that promote a sustained ...
MBL2 - MBL2 - Human, 4 unique 29mer shRNA constructs in retroviral RFP vector shRNA available for purchase from OriGene - Your Gene Company.
From different parts of the world, South Asian ethnicity has been reported to be an independent risk factor for cardiovascular events [1, 18], although survival thereafter does not seem to be worse compared to Caucasians [19, 20]. We studied the effect of MBL genotype and level in a group of type 2 diabetic subjects of South Asians descent.. The main finding of the present study is that in type 2 diabetic South Asians, the O/O MBL genotype was significantly associated with the occurrence of cardiovascular events compared to wild-type.. The association between low MBL genotype and cardiovascular events has previously been reported in different populations [12, 21, 22]. For instance, the Strong Heart Study included American Indians [12], which - like South Asians-have a high burden of diabetes and subsequent vascular complications. A low MBL genotype was associated with a threefold increased risk for coronary heart disease.. With respect to serum MBL levels and cardiovascular events, data are more ...
4AKD: Structures and Binding Specificity of Galactose- and Mannose-Binding Lectins from Champedak: Differences from Jackfruit Lectins
Bottazzi B, Fornasari L, Frangolho A, Giudicatti S, Mantovani A, Marabelli F, et al. Multiplexed label-free optical biosensor for medical diagnostics. Journal of biomedical optics. 2014;19(1):17006.. Beghe B, Verduri A, Bottazzi B, Stendardo M, Fucili A, Balduzzi S, et al. Echocardiography, spirometry, and systemic acute-phase inflammatory proteins in smokers with COPD or CHF: an observational study. PloS one. 2013;8(11):e80166.. Job ER, Bottazzi B, Short KR, Deng YM, Mantovani A, Brooks AG, et al. A single amino acid substitution in the hemagglutinin of H3N2 subtype influenza A viruses is associated with resistance to the long pentraxin PTX3 and enhanced virulence in mice. J Immunol. 2014;192(1):271-81.. Mantovani A, Valentino S, Gentile S, Inforzato A, Bottazzi B, Garlanda C. The long pentraxin PTX3: a paradigm for humoral pattern recognition molecules. Ann N Y Acad Sci. 2013;1285(1):1-14.. Latini R, Gullestad L, Masson S, Nymo SH, Ueland T, Cuccovillo I, et al. Pentraxin-3 in chronic heart ...
The ficolins share a common organization and function with the collectins: serum mannose-binding and the pulmonary surfactant proteins A and D. All of these proteins are soluble mediators of innate immunity and consist of globular sugar-binding domains attached to collagenous stalks, which can invoke innate immune responses either through complement fixation or interaction with receptors on the surfaces of macrophages. Amongst these proteins, the ficolins have been most extensively investigated with CFG resources, while mannose-binding protein is the best characterized. The ficolins have fibrinogen-like sugar-binding domains, rather than C-type carbohydrate-recognition domains, but conceptually fall within the same group. See also: paradigm page for Ficolin M (Ficolin 1) ...
The ficolins share a common organization and function with the collectins: serum mannose-binding and the pulmonary surfactant proteins A and D. All of these proteins are soluble mediators of innate immunity and consist of globular sugar-binding domains attached to collagenous stalks, which can invoke innate immune responses either through complement fixation or interaction with receptors on the surfaces of macrophages. Amongst these proteins, the ficolins have been most extensively investigated with CFG resources, while mannose-binding protein is the best characterized. The ficolins have fibrinogen-like sugar-binding domains, rather than C-type carbohydrate-recognition domains, but conceptually fall within the same group. See also: paradigm page for Ficolin M (Ficolin 1) ...
The complement system is an enzyme cascade that is a collection of blood and cell surface proteins to help the abilities of antibodies to clear pathogens from an organism. The complement system that comprises 30 different proteins, including serum proteins, serosal proteins, and cell membrane receptors is an important part of the innate immune system. There are three different complement pathways, the classical complement pathway, the alternative complement pathway, and the mannose-binding lectin pathway.
Objectives: Mannose-binding lectin (MBL) is active in the innate immune defense against microorganisms. In this study, we determined whether vulvar vestibulitis syndrome, a disorder of unknown etiology, was associated with an altered distribution of MBL alleles.. Study design: Buccal swabs were obtained from women with vulvar vestibulitis syndrome in New York (62) and from 2 cities in Sweden (60), as well as control women in New York (48) and Sweden (51). DNA was tested for a single nucleotide polymorphism at codon 54 in exon I by polymerase chain reaction, endonuclease digestion, and gel electrophoresis. Blood samples were also obtained from the New York women and tested by ELISA for plasma MBL concentrations. The relationships between genotype, allele frequencies, blood MBL levels, and diagnosis were analyzed by Fisher exact test and one-way analysis of variance.. Results: The variant MBL allele, MBL*B, was detected in 35.5% and 26.7% of vulvar vestibulitis patients from New York and Sweden, ...
The complement system provides a fundamental component of the body's immune response to invading microorganisms. This chapter highlights the various roles of the complement system in the orchestration of the immune response towards microbial infections, gives examples of microbial strategies to evade complement-mediated clearance, and discusses how acquired and inherited complement deficiencies may predispose an organism to infectious disease. Complement is activated by three pathways: the classical pathway, the alternative pathway, and the lectin pathway. The lectin pathway is activated by carbohydrate recognition molecules that bind to polysaccharide on the surface of a pathogen. Factor B, factor D, and properdin (factor P) are specific components of the alternative pathway of complement activation. The complement activation is tightly regulated by membrane-bound and fluid-phase regulatory components to avoid runaway activation of the enzymatic cascade that could lead to excess host tissue damage

Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases  and Activate...Mouse Ficolin B Has an Ability to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate...

... to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway. ... to Form Complexes with Mannose-Binding Lectin-Associated Serine Proteases and Activate Complement through the Lectin Pathway," ...
more infohttps://www.hindawi.com/journals/bmri/2012/105891/cta/

Low mannose-binding lectin (MBL) genotype is associated with future cardiovascular events in type 2 diabetic south asians. a...Low mannose-binding lectin (MBL) genotype is associated with future cardiovascular events in type 2 diabetic south asians. a...

Mannose-Binding Lectin (MBL), which activates the lectin pathway of complement activation, has been introduced as a risk marker ... alternative or lectin pathway, which is activated when Mannose-Binding Lectin (MBL) binds to its target molecule. MBL binds ... Antibody-mediated activation of the classical pathway of complement may compensate for mannose-binding lectin deficiency. Eur J ... Low mannose-binding lectin (MBL) genotype is associated with future cardiovascular events in type 2 diabetic south asians. a ...
more infohttps://cardiab.biomedcentral.com/articles/10.1186/1475-2840-10-60

mannose-binding lectin pathway - meddicmannose-binding lectin pathway - meddic

Mannose-binding lectin (MBL) is a pattern recognition receptor of the lectin pathway of complement system. MBL binds to ... the lectin pathway does not recognize an antibody bound to its target. The lectin pathway starts with mannose-binding lectin or ... Activation of the alternative complement pathway by mannose-binding lectin via a C2-bypass pathway ... In this pathway, mannose-binding lectin binds to mannose, glucose or other sugars with 3- and 4-OH groups placed in the ...
more infohttp://meddic.jp/mannose-binding_lectin_pathway

Frontiers | Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic...Frontiers | Extensive Basal Level Activation of Complement Mannose-Binding Lectin-Associated Serine Protease-3: Kinetic...

The lectin pathway of the complement system is initiated by mannose-binding lectin (MBL)-associated serine proteases, MASP-1, ... The third serine protease of the lectin pathway, MASP-3, was recently shown to be the major activator, and the exclusive ... The third serine protease of the lectin pathway, MASP-3, was recently shown to be the major activator, and the exclusive ... The lectin pathway of the complement system is initiated by mannose-binding lectin (MBL)-associated serine proteases, MASP-1, ...
more infohttps://www.frontiersin.org/articles/10.3389/fimmu.2017.01821/full

Selective Inhibition of the Lectin Pathway of Complement with Phage Display Selected Peptides against Mannose-Binding Lectin...Selective Inhibition of the Lectin Pathway of Complement with Phage Display Selected Peptides against Mannose-Binding Lectin...

mannose-binding lectin-associated serine protease. MBL. mannose-binding lectin. PT. prothrombin time. SFMI. sunflower mannose- ... Mannose-binding lectin (MBL)-associated serine protease (MASP)-1 contributes to activation of the lectin complement pathway. J ... Selective Inhibition of the Lectin Pathway of Complement with Phage Display Selected Peptides against Mannose-Binding Lectin- ... Selective Inhibition of the Lectin Pathway of Complement with Phage Display Selected Peptides against Mannose-Binding Lectin- ...
more infohttp://www.jimmunol.org/content/185/7/4169

Cholesterol Crystals Activate the Lectin Complement Pathway via Ficolin-2 and Mannose-Binding Lectin - Research - RigshospitaletCholesterol Crystals Activate the Lectin Complement Pathway via Ficolin-2 and Mannose-Binding Lectin - Research - Rigshospitalet

Cholesterol Crystals Activate the Lectin Complement Pathway via Ficolin-2 and Mannose-Binding Lectin: Implications for the ... We investigated the binding of the PRMs mannose-binding lectin (MBL), ficolin-1, ficolin-2, and ficolin-3, the associated ... CC activate the classical and the alternative complement pathways, but the role of the lectin pathway is unknown. We ... Plasma levels of mannose-binding lectin and future risk of venous thromboembolism. Research output: Contribution to journal › ...
more infohttps://research.regionh.dk/rigshospitalet/en/publications/cholesterol-crystals-activate-the-lectin-complement-pathway-via-ficolin2-and-mannosebinding-lectin

Reduced Mannose-Binding Lectin-Associated Serine Protease (MASP)-1 is Associated with Disturbed Coagulation in Septic Shock.Reduced Mannose-Binding Lectin-Associated Serine Protease (MASP)-1 is Associated with Disturbed Coagulation in Septic Shock.

The mannose-binding lectin-associated serine proteases (MASP)-1... ... Activation of the complement system is part of the dysregulated immune response in sepsis. ... It binds to carbohydrate groups on invading pathogens and plays a key role in the MANNOSE-BINDING LECTIN COMPLEMENT PATHWAY. ... The mannose-binding lectin-associated serine proteases (MASP)-1 and -2 activate the lectin pathway of the complement system. ...
more infohttps://www.bioportfolio.com/resources/pmarticle/2345804/Reduced-Mannose-Binding-Lectin-Associated-Serine-Protease-MASP-1-is-Associated-with.html

Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition | Infection...Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition | Infection...

1992) Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine ... Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition. Olaf Neth, ... Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition ... Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition ...
more infohttps://iai.asm.org/content/68/2/688?ijkey=96037c05e02ff63648c6385eac452d984ff7adeb&keytype2=tf_ipsecsha

Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition | Infection...Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition | Infection...

1992) Activation of the classical complement pathway by mannose-binding protein in association with a novel C1s-like serine ... Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition. Olaf Neth, ... Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition ... Mannose-Binding Lectin Binds to a Range of Clinically Relevant Microorganisms and Promotes Complement Deposition ...
more infohttps://iai.asm.org/content/68/2/688?ijkey=99e4ba34f1c1f31d1d271ec48a3a9e0935db5db3&keytype2=tf_ipsecsha

Secondary cell wall polymers of Enterococcus faecalis are critical for resistance to complement activation via mannose-binding...Secondary cell wall polymers of Enterococcus faecalis are critical for resistance to complement activation via mannose-binding...

... we found an increased binding of the key lectin pathway components mannose-binding lectin and mannose-binding lectin-associated ... cell wall polymers of Enterococcus faecalis are critical for resistance to complement activation via mannose-binding lectin.. [ ... Our studies indicated that complement activation via the lectin pathway was much stronger on the tagB mutant compared with wild ... To understand the mechanism of lectin pathway inhibition by E. faecalis, we purified and characterized cell wall carbohydrates ...
more infohttps://www.sigmaaldrich.com/catalog/papers/22908219

Impact of mannose-binding lectin on susceptibility to infectious diseases.  - PubMed - NCBIImpact of mannose-binding lectin on susceptibility to infectious diseases. - PubMed - NCBI

... microbial surface carbohydrates and mediates opsonophagocytosis directly and by activation of the lectin complement pathway. A ... Mannose-binding lectin (MBL) is a C-type serum lectin that plays a central role in the innate immune response. MBL binds ... Impact of mannose-binding lectin on susceptibility to infectious diseases.. Eisen DP1, Minchinton RM. ... wide variety of clinical isolates of bacteria, fungi, viruses, and parasites are bound by MBL. Three polymorphisms in the ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/14614673?dopt=Abstract

Properdin Binds to Late Apoptotic and Necrotic Cells Independently of C3b and Regulates Alternative Pathway Complement...Properdin Binds to Late Apoptotic and Necrotic Cells Independently of C3b and Regulates Alternative Pathway Complement...

... and lectin pathway (via mannose-binding lectin (MBL) and ficolin) (10, 11, 12, 13, 14). It has been suggested that the main ... and lectin pathway (via mannose-binding lectin and ficolin). Herein we report that the only known naturally occurring positive ... To prove that cell-bound properdin can activate complement independently of the classical and lectin pathways, we used C4ds as ... Human IgA activates the complement system via the mannan-binding lectin pathway. J. Immunol. 167: 2861-2868. ...
more infohttp://www.jimmunol.org/content/180/11/7613?ijkey=4c7ecf4340af5dabcca70ddb98a75f3703f2602d&keytype2=tf_ipsecsha

Hytönen J[au] - PubMed - NCBIHytönen J[au] - PubMed - NCBI

Lyme Borreliosis and Deficient Mannose-Binding Lectin Pathway of Complement.. Sajanti EM, Gröndahl-Yli-Hannuksela K, Kauko T, ... Predicting the ligand-binding properties of Borrelia burgdorferi s.s. Bmp proteins in light of the conserved features of ... Decorin binding by DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi sensu Stricto. ... Decorin binding proteins of Borrelia burgdorferi promote arthritis development and joint specific post-treatment DNA ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed?cmd=search&term=Hyt%C3%B6nen+J%5Bau%5D&dispmax=50

High Rate of Early Restenosis After Carotid Eversion Endarterectomy in Homozygous Carriers of the Normal Mannose-Binding Lectin...High Rate of Early Restenosis After Carotid Eversion Endarterectomy in Homozygous Carriers of the Normal Mannose-Binding Lectin...

On binding to a ligand, MBL may activate the lectin pathway of complement via the MBL-associated serine protease 2.7-9 Human ... Matsushita M, Fujita T. Activation of the classical complement pathway by mannose-binding protein in association with a novel ... Complement activation after oxidative stress: role of the lectin complement pathway. Am J Pathol. 2000; 156: 1549-1556. ... because MBL-associated serine protease 2 initiates activation of the lectin pathway of complement.9 Complement has been ...
more infohttp://stroke.ahajournals.org/content/36/5/944

Cytokines etc for Immunology Flashcards by Anna Cushing | BrainscapeCytokines etc for Immunology Flashcards by Anna Cushing | Brainscape

What complement pathways involve C4? - classical. - mannose-binding lectin 26 How is complement a bridge to adaptive immunity ... 1. IgG bound to pathogen-infected cell binds NK cell, Nk cell releases cytokines like IFN-gamma and kills cell. 2. IgE bound to ... CD28 on naive T cell binds B7 on APC. - CD40L on activated T cell binds CD40 on APC ... C3b binds Cr1/2 on B cell and lowers activation threshold and enhances Ab production. - upregulations co-stimulation molecules ...
more infohttps://www.brainscape.com/flashcards/cytokines-etc-for-immunology-1801811/packs/3895324

Immunology Flashcards by  | BrainscapeImmunology Flashcards by | Brainscape

Describe initiation of the MBL complement pathway. MBL: mannose binding lectin. Produced by the liver in response to infection ... Formation of antigen-antibody complexes activates which complement pathway? Starts with which protein? ... Binds to carbohydrates found on many pathogens including multiple bacteria, viruses and yeasts. In blood MBL is complexed with ... SLE: The classical pathway clears necrotic and apoptotic cells. Failure leads to build up of self antigens especially nuclear ...
more infohttps://www.brainscape.com/flashcards/immunology-4870435/packs/7066822

Mannose Binding Lectin, SerumMannose Binding Lectin, Serum

When bound, this lectin will trigger the complement pathway resulting in opsonization. Mannose-binding protein is also an acute ... Mannose-binding protein is a component of the innate or natural immune system which binds to mannose residues on a variety of ... This test is used as an initial screening for suspected deficiency in the lectin complement pathway. ... Abnormal mannose-binding protein concentrations have been found in patients with infectious disorders such as tuberculosis, ...
more infohttps://www.healthcare.uiowa.edu/path_handbook/handbook/test2669.html

Association Study of Mannose-Binding Lectin Levels and Genetic Variants in Lectin Pathway Proteins with Susceptibility to Age...Association Study of Mannose-Binding Lectin Levels and Genetic Variants in Lectin Pathway Proteins with Susceptibility to Age...

However, the involvement of the lectin pathway of complement, a key mediator of oxidative damage, is controversial. This study ... Association Study of Mannose-Binding Lectin Levels and Genetic Variants in Lectin Pathway Proteins with Susceptibility to Age- ... investigated whether mannose-binding lectin (MBL) levels and genetic variants in lectin pathway proteins, are associated with ... SNPs of lectin pathway proteins investigated in this study were not associated with AMD or AMD severity. However, MBL levels ...
more infohttps://www.sigmaaldrich.com/catalog/papers/26207622

The Role of Complement System in Septic ShockThe Role of Complement System in Septic Shock

T. Sprong, T. E. Mollnes, C. Neeleman et al., "Mannose-binding lectin is a critical factor in systemic complement activation ... Involvement of Complement Lectin Pathway in Septic Shock. Specific factors in complement lectin pathway include MBL and ficolin ... M. Matsushita and T. Fujita, "Activation of the classical complement pathway by mannose-binding protein in association with a ... Involvement of Complement Classical Pathway in Septic Shock. Specific factors in complement classical pathway include ...
more infohttps://www.hindawi.com/journals/jir/2012/407324/

KAKEN - Research Projects | Studies on a nocal sevine protease and the activation mechanism of the lectin complement pathway ...KAKEN - Research Projects | Studies on a nocal sevine protease and the activation mechanism of the lectin complement pathway ...

Origin of mannose-binding lectin-associated serine protease (MASP)-1 and MASP-3 involued in the lectin complement pathway ... Origion of mannose-binding lectin-associated serine protrease (MASP)-1 and MASP-3 involved in the lectin complement pathway ... Origin of mannose-binding lectin-associated serine Protease (MASP)-1 and MASP-3 involved in the lectin complement pathway ... complement / Lectin pathway / MBL / ficolin / MASP / Servine protease / レクチン / ficolin. Research Abstract. Mannose-binding ...
more infohttps://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-13670321/

Lack of the Pattern Recognition Molecule Mannose-Binding Lectin Increases Susceptibility to Influenza A Virus InfectionLack of the Pattern Recognition Molecule Mannose-Binding Lectin Increases Susceptibility to Influenza A Virus Infection

The anti-viral mechanisms of MBL include activation of the lectin complement pathway and coagulation, requiring serum factors. ... Background: Mannose-binding lectin (MBL), a pattern recognition innate immune molecule, inhibits influenza A virus infection in ... Lack of the Pattern Recognition Molecule Mannose-Binding Lectin Increases Susceptibility to Influenza A Virus Infection. ... Lack of the pattern recognition molecule mannose-binding lectin increases susceptibility to influenza A virus infection. BMC ...
more infohttps://dash.harvard.edu/handle/1/4875898

Lectin pathway - WikipediaLectin pathway - Wikipedia

The lectin pathway starts with mannose-binding lectin (MBL) or ficolin binding to certain sugars. In this pathway, mannose- ... Classical complement pathway Alternative complement pathway Mannan-binding lectin Wallis R, Mitchell DA, Schmid R, Schwaeble WJ ... In contrast to the classical complement pathway, the lectin pathway does not recognize an antibody bound to its target. ... are bound by MBL. Mannan-binding lectin, also called mannose-binding protein, is a protein belonging to the collectin family ...
more infohttps://en.wikipedia.org/wiki/Lectin_pathway

Pinkbook | Meningococcal | Epidemiology of Vaccine Preventable Diseases | CDCPinkbook | Meningococcal | Epidemiology of Vaccine Preventable Diseases | CDC

Certain genetic factors (such as polymorphisms in the genes for mannose-binding lectin and tumor necrosis factor) may also be ... Risk factors for the development of meningococcal disease include deficiencies in the terminal common complement pathway, ... Persons with complement component deficiency, functional or anatomic asplenia or HIV infection who have already received 1 dose ... Persons with persistent complement component deficiency, and persons with functional or anatomic asplenia should receive a 2- ...
more infohttp://www.cdc.gov/vaccines/pubs/pinkbook/mening.html

MBL2 gene polymorphism rs1800450 and rheumatic fever with and without rheumatic heart disease: an Egyptian pilot study |...MBL2 gene polymorphism rs1800450 and rheumatic fever with and without rheumatic heart disease: an Egyptian pilot study |...

Mannose-binding lectin binds to a range of clinically relevant microorganisms and promotes complement deposition. Infect Immun ... Complement activation after oxidative stress: role of the lectin complement pathway. Am J Pathol. 2000;156(5):1549-56.CrossRef ... Association of mannose-binding lectin gene polymorphism but not of mannose-binding serine protease 2 with chronic severe aortic ... with complement cascade activation. Mannose-binding lectin (MBL) is an acute phase inflammatory protein and functions as a ...
more infohttps://link.springer.com/article/10.1186/s12969-018-0245-x

Plus itPlus it

... the mannose-binding lectin (MBL), and alternative pathways. All 3 pathways converge on the C3 protein. C3 cleavage products ... complement factor H; MASP: mannose-binding lectin-associated serine protease. After Wang, et al, Nat Med 2011;17:1674-935 and ... The complement system. The complement cascade is a complex system that can become activated by any of 3 separate pathways: the ... The extracellular matrix and inflammation: fibromodulin activates the classical pathway of complement by directly binding C1q. ...
more infohttp://www.jrheum.org/content/42/3/363
  • When the carbohydrate-recognising heads of MBL bind to specifically arranged mannose residues on the surface of a pathogen, MASP-1 and MASP-2 are activated to cleave complement components C4 and C2 into C4a, C4b, C2a, and C2b. (wikipedia.org)
  • This carbohydrate-binding protein, an opsonin and lectin pathway activator, binds through multiple lectin domains to the repeating sugar arrays displayed on the surface of a wide range of clinically relevant microbial species. (beds.ac.uk)
  • This pathway can be activated mainly by mannose-binding lectin (MBL) interacting with carbohydrate structures on microbial surfaces and by ficolins with different fine carbohydrate binding specificity. (uniprot.org)
  • Mannose-binding lectin, soluble DC-SIGN and DC-SIGNR, and surfactant protein D, were tested for carbohydrate binding in the presence of glucose concentrations typical of diabetes, via surface plasmon resonance and affinity chromatography. (wellnessresources.com)
  • D-Mannose is a carbohydrate. (hmdb.ca)
  • Furthermore the carbohydrate recognition domains of DC-SIGN and DC-SIGNR were prepared in 15N stable isotope medium and analysed via solution NMR spectroscopy, providing a gateway to understanding the molecular dynamics of these lectins. (warwick.ac.uk)
  • Botto M, Fong KY, So AK, Koch C, Walport MJ (1990) Molecular basis of polymorphisms of human complement component C3. (springer.com)
  • MBL has the potential to express multiple biological effector functions, but a prerequisite for all such activity is primary binding to multiple arrays of sugar ligands such as those expressed on microbial surfaces. (asm.org)
  • MBL binds microbial surface carbohydrates and mediates opsonophagocytosis directly and by activation of the lectin complement pathway. (nih.gov)
  • Microbial colonization of germ-free mice triggers epithelial expression of RegIIIγ, a secreted C-type lectin. (sciencemag.org)
  • We measured levels of immunoglobulins (Igs) and complement in 257 hospitalized adults with CAP and examined the association of low levels of Igs or complement to microbial etiology, disease severity, and short-term and long-term outcome. (lu.se)
  • In hospitalized adults with CAP, low admission levels of Igs or complement were in general not associated with microbial etiology, disease severity, short-term outcome, or long-term outcome. (lu.se)
  • It has been suggested that the main product of complement activation, iC3b, facilitates the removal of dead material and mediates peripheral tolerance ( 10 , 15 , 16 ). (jimmunol.org)
  • MBL also binds and mediates clearance of apoptotic cells and cell debris. (ithanet.eu)
  • The strategies used by Enterococcus faecalis to evade recognition by human complement are incompletely understood. (sigmaaldrich.com)
  • In the early 20th century, this controversy was resolved when it became understood that complement can act in combination with specific antibodies, or on its own in a non-specific way. (wikipedia.org)
  • Test your therapeutic antibodies in immunohistochemistry against a broad panel of normal frozen human tissue types in order to determine potential unintended binding. (lsbio.com)
  • Complement-mediated clearance of apoptotic cells has been well documented both in vitro ( 10 ) and in vivo ( 11 ). (jimmunol.org)
  • Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating their uptake by macrophages (By similarity). (uniprot.org)