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.
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 ...
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
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.. ...
FDA granted Omeros lead human monoclonal antibody (mAb) OMS721 breakthrough therapy designation for the treatment of immunoglobulin A (IgA) nephropathy. The antibody targets mannan-binding lectin-associated serine protease-1 (MASP-2). Omeros holds global rights to MASP-2 and therapeutics targeting the lectin pathway effector enzyme.
Tytu : Mannan-binding lectin-associated serine protease-2 (MASP-2) in a large cohort of neonates and its clinical associations. ...
Heja D, Harmat V, Fodor K, Wilmanns M, Dobo J, Kekesi KA, Zavodszky P, Gal P, Pal G: Monospecific inhibitors show that both mannan-binding lectin-associated serine protease (MASP)-1 and -2 are essential for lectin pathway activation and reveal structural plasticity of MASP-2., JOURNAL OF BIOLOGICAL CHEMISTRY 287: (24) pp. 20290-20300 ...
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
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-
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 ...
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 ...
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. ...
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 ...
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.. ...
Mannose-binding lectin (MBL), a serum protein belonging to the collectin family, is considered to be a pattern recognition molecule designed to detect pathogen-associated molecular patterns (5). MBL exists in serum as multimeric trimers of 32-kDa polypeptide chains; each chain has a carbohydrate recognition domain (CRD) and a collagen-like region for trimeric assembly. The CRD has been shown to bind mannose, fucose, and N-acetylglucosamine (4), and the cluster of CRDs rendered by oligomerization is thought to be suitable for binding polymeric sugars found on microbes (19, 42). Indeed, MBL has been shown to bind a host of pathogens, including subsets of gram-positive and gram-negative bacteria, Mycobacterium tuberculosis, and Candida albicans (5, 31). Once bound to microbes, MBL is believed to act as an opsonin for phagocytosis (17) and to activate the complement cascade via mannose-binding lectin-associated protein 2 (MASP-2) for microbial lysis (28, 34, 39).. MBL is encoded by a single gene in ...
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 ...
Principal Investigator:MATSUSHITA Misao, Project Period (FY):1996 - 1997, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Immunology
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
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).
To investigate the point mutation at codon 54 of mannose binding lectin (MBL) gene, detect the plasma MBL level, and analyze the correlation between the gene mutation frequency and plasma MBL concentration. A method for detecting MBL gene point mutation (PCR-RFLP) was established with self-designed primers according to MBL genomic sequence. The plasma MBL concentration was detected by MBL Oliger ELISA kit. The PCR-RFLP for detecting the point mutation at codon 54 of MBL gene was established. Frequency of point mutation at codon 54 of MBL gene in healthy Mongolians was 0.18. The plasma MBL concentration was (2.53+/-1.96)mg/L. There was negative correlation between plasma MBL concentration and MBL gene mutation frequency in Mongolians (r = -0.641). The established method of PCR-RFLP was proved to have high specificity, excellent reproducibility and high sensitivity. The relationship between frequency of mutation at codon 54 of MBL gene and the plasma MBL concentration in healthy Mongolians is ...
Individuals with low levels of mannan-binding lectin (MBL) appear to be susceptible to infectious diseases. This suggests that substitution therapy with MBL might be a beneficial treatment of patients with MBL deficiency. A production process for an MBL product has been developed from a fraction II+III precipitate obtained by ethanol fractionation of plasma. The MBL process includes three chromatographic steps, where the first and key step is affinity chromatography on a cross-linked agarose matrix selecting for oligomeric, carbohydrate-binding MBL. The yield from the production process is about 25% of the plasma MBL content, and the purity is about 65%. The MBL product shows mannan-binding activity and complement-activating ability. A safety study has shown this plasma-derived MBL to be safe and well tolerated in adult MBL-deficient volunteers. ...
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
TY - JOUR. T1 - Identification and characterisation of porcine mannan-binding lectin (pMBL-A) and determination of serum concentration heritability. AU - Juul-Madsen, H. R.. AU - Krogh-Meibom, T.. AU - Henryon, M. AU - Palaniyar, N.. AU - Heegaard, Peter M. H.. AU - Purup, S.. AU - Willis, A. C.. AU - Tornøe, I.. AU - Ingvartsen, K. L.. AU - Hansen, S.. AU - Holmskov, U.. PY - 2006. Y1 - 2006. M3 - Journal article. VL - 58. SP - 129. EP - 137. JO - Immunogenetics. JF - Immunogenetics. SN - 0093-7711. ER - ...
Ficolins are a group of proteins mainly consisting of collagen-like and fibrinogen-like domains and are thought to play a role in innate immunity via their carbohydrate-binding activities. Two types of ficolins have been identified in mice, ficolin A, and ficolin B. However, their structure and func …
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 ...
The authors show the highly homologous N proteins from SARS-CoV, SARS-CoV2 and MERS interact with MASP-2. MASP-2 is a protease critical to complement activation by the lectin pathway. In an in vivo murine infection model the N protein of SARS-CoV expressed from an adenoviral vector enhances LPS induced lung injury; a phenotype lost by blocking N protein: MASP2 interaction and by suppressing complement activation. Serum C5a levels were significantly increased in severe COVID-19 patients. 2 of these COVID-19 patients treated with recombinant anti-C5a antibody show clinical improvement. This indicates that targeting complement pathways offers therapeutic potential for pneumonia induced by coronaviruses. ...
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].
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
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。. ...
Activation of complement involves the sequential proteolysis of proteins to generate enzyme complexes with proteolytic activity. Proteolytic cascades allow tremendous amplification because each enzyme molecule activated at one step can generate multiple activated enzyme molecules at the next step. The … Read more. ...
Gentaurs MASP1 CLIA kit utilizes the Sandwich- CLIA principle. The micro CLIA plate provided in this kit has been pre-coated with an antibody specific to Human MASP1 . Standards or samples are added to the micro CLIA plate wells and combined with ...
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 ...
Structural and functional characterization of two mannan-binding lectin homologues from the urochordate species Ciona intestinalis: Insight to the origin and evolution of the lectin complement ...
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 ...
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 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 ...
(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
RATIONALE: Recombinant human mannose-binding lectin (MBL) may be effective in preventing infection in young patients with fever and neutropenia receivin
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…
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 ...
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.
The inhibition obtained by the number of molecules in 1 µg rCCP1-CCP2-SP per ml was. thus said to be equivalent to the number of molecules in 1·76 (79 247/45 073) µg MASP-1 per ml. We added the rCCP1-CCP2-SP to 10% fetal calf serum before performing the dilutions in order to obtain a similar matrix and to obtain comparable slopes of the dilution curve of the standard plasma and the recombinant material (the antibodies employed do not cross-react with bovine MASP-1). To test for the specificity of the assay, purified rMAp44 or rMASP-3 (produced and purified as described in Degn et al. [21]) was added to the MASP-1 assay at a concentration of 10 µg/ml for rMAp44 Erismodegib ic50 and 2·5 µg/ml for rMASP-3 at the highest concentration and dilutions thereof. The addition of rMAp44 or rMASP-3 did not influence the signal. To characterize the assay further and to study the association of MASP-1 with other serum components, serum was subjected to gel. permeation chromatography (GPC) on a 1 × 30 ...
Hemodialysis patients have higher rates of cardiovascular morbidity and mortality compared to the general population. Mannose-binding lectin (MBL) plays an important role in the development of cardiovascular disease. In addition, hemodialysis alters MBL concentration and functional activity. The present study determines the predictive value of MBL levels for future cardiac events (C-event), cardiovascular events (CV-event) and all-cause mortality in HD patients. We conducted a prospective study of 107 patients on maintenance hemodialysis. Plasma MBL, properdin, C3d and sC5b-9 was measured before and after one dialysis session. The association with future C-events, CV-events, and all-cause mortality was evaluated using Cox regression models. During median follow-up of 27 months, 36 participants developed 21 C-events and 36 CV-events, whereas 37 patients died. The incidence of C-events and CV-events was significantly higher in patients with low MBL levels (|319 ng/mL, lower quartile). In fully adjusted
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.
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
Seit Jahrhunderten kennen und nutzen einige Naturvölker natürliche Spinnenseide als Material mit herausragender Mechanik, Bioverträglichkeit und Bioabbaubarkeit. Von den bis zu sechs verschiedenen Spinnenseidenarten, die von weiblichen Vertretern der echten Radnetzspinnen in dafür spezialisierten Drüsen produziert werden können, ist die Dragline- Seide in den letzten Jahren in den Fokus der Wissenschaft gerückt. Diese Seidenart bildet sowohl den Rahmen als auch die Speichen des Radnetzes. Die zugrundeliegenden Proteine werden Major Ampullate Spidroin 1 und 2 (MaSp1, MaSp2) genannt, wobei sich MaSp1 und MaSp2 hauptsächlich im Prolingehalt unterscheiden. Alle bislang beschriebenen und charakterisierten MaSp Proteine besitzen ein Molekulargewicht zwischen 200 und 350 kDa mit einer aus bis zu 100 Wiederholungseinheiten bestehenden repetitiven Kerndomäne, welche von nicht-repetitiven und über unterschiedliche Spinnen- und Seidenarten stark konservierten terminalen Domänen flankiert wird. ...