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Mannan Binding Lectin (MBL), Clone 182_01, Mab anti_Chicken, ELISA_WB_IH

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[#HYB182-01] Mannan Binding Lectin (MBL), Clone 182_01, Mab anti_Chicken, ELISA_WB_IH

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HYB182-01 | Mannan Binding Lectin (MBL), Clone 182_01, Mab anti_Chicken, ELISA_WB_IH, 200 µg.
More informations about Mannan Binding Lectin (MBL), Clone 182_01, Mab anti_Chicken, ELISA_WB_IH in Antibody-antibodies.com

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(1) Interaction of mannose binding lectin and other pattern recognition receptors in human corneal epithelial cells during Aspergillus fumigatus infection.[TOP]

Pubmed ID :30096599
Publication Date : //
Mannose binding lectin (MBL), a member of C-type lectin superfamily, plays a significant role in the innate immune system as one of the Pattern-Recognition Receptors (PRRs). This study investigated the relationship between MBL and other PRRs including Dectin-1and TLR2, and detected the reaction of MBL towards the expression of cytokines in human corneal epithelial cells (HCECs) and murine corneas upon Aspergillus fumigatus (A. fumigatus) hyphae infection. We found that MBL was significantly up-regulated in C57BL/6 corneas infected with A. fumigatus and HCECs incubated with A. fumigatus hyphae. Moreover, both of mRNA and protein levels of Dectin-1, TLR2, IL-1β and TNF-α were increased dramatically to peak point with the pretreatment of exogenous MBL, while decreased significantly with the pretreatment of MBL monoclonal antibody in HCECs. Pretreatment with laminarin and TLR2 neutralizing antibody decreased both of mRNA and protein levels of MBL and proinflammatory mediators (IL-1β and TNF-α) in A. fumigatus hyphae infected HCECs. These data demonstrate that A. fumigatus introduce the expression of MBL in human corneas, C57BL/6 corneas and HCECs. MBL, Dectin-1 and TLR2 interact with each other upon the treatment of A. fumigatus, and MBL contributes to the innate immune responses by regulating proinflammatory mediators, such as IL-1β and TNF-α.

Authors : Peng Xudong, Zhao Guiqiu, Lin Jing, Li Cui,



(2) Molecular profile of mannan-binding lectin in hepatitis C patients with MBL gene polymorphisms by a modified mannan-coated nitrocellulose assay.[TOP]

Pubmed ID :30056939
Publication Date : //
The aim of this study was to develop an assay to analyze the serum profile of Mannose-binding lectin (MBL) through a simple and "in-house" method (called "dot-N-man"). Furthermore, the study attempted to associate molecular masses of MBL to the profile of MBL gene polymorphisms in patients with hepatitis C. Heterogeneity in molecular masses of MBL is due to the impairment of oligomers formation, which is linked to genetic polymorphisms in the MBL gene. Individuals with AA genotype (wild-type) produce high-molecular-mass proteins, whereas AO and OO individuals produce intermediate and low-molecular-mass proteins, respectively. Sera of thirty patients carrying the hepatitis C virus (HCV) were investigated using MBL binding assay with mannan-coated nitrocellulose (dot-N-man). Purified MBL was evaluated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Western blotting. Dot-N-Man assay yielded MBL with molecular masses ranging between 55 and 320 kDa, comparable to low and high molecular mass forms of MBL. Nonreducing SDS-PAGE showed high molecular mass bands in all AA individuals while bands of 270 and 205 kDa were observed in sera for a number of patients with AO and OO genotypes, respectively. Immunoblotting confirmed the MBL samples obtained from the dot-N-man. These results provide new insights to understand the MBL molecular forms profile in patients infected with HCV- which could be useful in future investigations on the influence of the MBL structure/genotype on both the progression of infection and the response to hepatitis C therapy.

Authors : Albuquerque Diego A P, Cavalcanti Igor T, Vasconcelos Luydson R S, Montenegro Francisco, Pereira Leila M M B, Cavalcanti Maria S M, Moura Patrícia, Júnior Luiz B C, de Almeida Sinara Mônica Vitalino, Beltrão Eduardo I C,



(3) Associations between complement pathways activity, mannose-binding lectin, and odds of unprovoked venous thromboembolism.[TOP]

Pubmed ID :30015228
Publication Date : //
Deep vein thrombosis (DVT) originates in the valvular sinuses of large veins in a local milieu characterized by stasis and severe hypoxia. This may induce complement- and coagulation activation, which potentially increases the risk of venous thromboembolism (VTE). The aim of the present study was to investigate whether the activity of the complement pathways, the level of mannose-binding lectin (MBL) and tissue-factor (TF) induced thrombin generation were associated with risk of unprovoked VTE.

Authors : Høiland Ina Isabella, Liang Robin Amanda, Hindberg Kristian, Latysheva Nadezhda, Brekke Ole-Lars, Mollnes Tom Eirik, Hansen John-Bjarne,



(4) Interaction of Mannose-Binding Lectin With Lipopolysaccharide Outer Core Region and Its Biological Consequences.[TOP]

Pubmed ID :30008719
Publication Date : //
Lipopolysaccharide (LPS, endotoxin), the main surface antigen and virulence factor of Gram-negative bacteria, is composed of lipid A, core oligosaccharide, and O-specific polysaccharide (O-PS) regions. Each LPS region is capable of complement activation. We have demonstrated that LPS of , an opportunistic human pathogen, reacts strongly with human and murine mannose-binding lectins (MBLs). Moreover, MBL-LPS interactions were detected for the majority of other Gram-negative species investigated. was used as a model pathogen to investigate the biological consequences of these interactions. The core oligosaccharide region of LPS was identified as the main target for human and murine MBL, especially l--d--heptose (Hep) and -acetyl-d-glucosamine (GlcNAc) residues within the outer core region. MBL-binding motifs of LPS are accessible to MBL on the surface of bacterial cells and LPS aggregates. Generally, the accessibility of outer core structures for interaction with MBL is highest during the lag phase of bacterial growth. The LPS core oligosaccharide-MBL interactions led to complement activation and also induced an anaphylactoid shock in mice. Unlike O3 LPS, robust lectin pathway activation of LPS was mainly the result of outer core recognition by MBL; involvement of the O-PS is not necessary for anaphylactoid shock induction. Our results contribute to a better understanding of MBL-LPS interaction and may support development of therapeutic strategies against sepsis based on complement inhibition.

Authors : Man-Kupisinska Aleksandra, Swierzko Anna S, Maciejewska Anna, Hoc Monika, Rozalski Antoni, Siwinska Malgorzata, Lugowski Czeslaw, Cedzynski Maciej, Lukasiewicz Jolanta,



(5) Substitution of Mannan-Binding Lectin (MBL)-Deficient Serum With Recombinant MBL Results in the Formation of New MBL/MBL-Associated Serine Protease Complexes.[TOP]

Pubmed ID :29997613
Publication Date : //
The lectin pathway (LP) of complement activation depends on the activation of the MBL-associated serine proteases (MASPs) circulating in complex with mannan-binding lectin (MBL). MBL deficiency is the most common complement deficiency and has been associated with several pathological conditions. As we had previously shown, plasma-derived MBL (pdMBL) contains pre-activated MASPs that upon pdMBL substitution results in restoration of MBL concentrations but no LP functionality due to immediate inactivation of pdMBL-MASP complexes upon infusion. In this study, we analyzed MBL-sufficient and -deficient serum by size-exclusion chromatography for complexes of LP activation. In both sera, we identified non-bound free forms of MASP-2 and to lesser extent MASP-1/3. After addition of recombinant MBL (rMBL) to MBL-deficient serum, these free MASPs were much less abundantly present, which is highly suggestive for the formation of high-molecular complexes that could still become activated upon subsequent ligand binding as shown by a restoration of C4-deposition of MBL-deficient serum. Ficolin (FCN)-associated MASPs have been described to redistribute to ligand-bound MBL, hereby forming new MBL/MASP complexes. However, reconstitution of MBL-deficient serum with rMBL did not change the relative size of the FCN molecules suggestive for a limited redistribution in fluid phase of already formed complexes. Our findings demonstrate that rMBL can associate with free non-bound MASPs in fluid phase while preserving full restoration of LP functionality. In contrast to pdMBL products containing pre-activated MASPs which become inactivated almost immediately, these current data provide a rationale for substitution studies using rMBL instead.

Authors : Keizer Mischa P, Kamp Angela, van Mierlo Gerard, Kuijpers Taco W, Wouters Diana,



(6) Cardiovascular risk and mannose binding lectin in patients with rheumatoid arthritis from southern Brazil.[TOP]

Pubmed ID :29992184
Publication Date : //
Mannose binding lectin (MBL) appears to be involved in susceptibility to rheumatoid arthritis (RA), in the inflammatory process and in the genesis of atherosclerotic disease.

Authors : Kahlow Barbara S, Nisihara Renato, Petisco Roberta, Utiyama Shirley R R, Messias-Reason Iara J, Goeldner Isabela, Skare Thelma L,



(7) The Complement System of Agnathans.[TOP]

Pubmed ID :29967624
Publication Date : //
Agnathans (lamprey and hagfish) are a group of primitive jawless fish. Jawed vertebrates possess adaptive immunity including immunoglobulins, while agnathans lack immunoglobulins but have alternative adaptive immunity in which variable lymphocyte receptors (VLRs) function as antibodies. The complement system consists of many proteins involved in the elimination of pathogens. In mammals, it is activated the three different pathways, resulting in the generation of C3b followed by the lytic pathway. Complement components including C3, mannose-binding lectin (MBL), and MBL-associated serine proteases (MASP) of the lectin pathway and factor B of the alternative pathway have been identified from lamprey and/or hagfish, while lytic pathway components have not been identified. In mammals, C1q binds to IgM/IgG-antigen complexes and activates the classical pathway in association with C1r and C1s. Lamprey also has C1q (LC1q), but its function differs from that of mammalian C1q. LC1q acts as a lectin and activates C3 in association with MASP the lectin pathway. Furthermore, LC1q may interact with a secreted type of VLR (VLRB) in complex with antigens and mediate activation of C3, potentially MASP, leading to cytolysis. Cytolysis is mediated by a newly identified serum protein named lamprey pore-forming protein (LPFP). In conclusion, lamprey has a complement activation pathway, which could be regarded as the classical pathway and also has a cytolytic system that is distinct from the mammalian lytic pathway. Thus, it appears that the complement system of agnathans is very unique and may have developed independently from jawed vertebrates.

Authors : Matsushita Misao,



(8) Dibutyryl cAMP- or Interleukin-6-induced astrocytic differentiation enhances mannose binding lectin (MBL)-associated serine protease (MASP)-1/3 expression in C6 glioma cells.[TOP]

Pubmed ID :29963999
Publication Date : //
Mannose-binding lectin (MBL)-Associated Serine Proteases (MASP)-1 and 3, key enzymes in the lectin complement pathway of innate immune response, are also expressed in glioma cell lines. We investigated MASP-1 and MASP-3 expression during dibutyryl cyclic AMP (dbcAMP)- or Interleukin-6 (rIL-6)-induced astrocytic differentiation of C6 glioma cells. Our results demonstrate that C6 cells express basal levels of MASP-1 and MASP-3 and following exposure to dbcAMP or IL-6, a consistent MASP-1 and MASP-3 mRNA up-regulation was found, with a behavior similar to that showed by the fibrillary acidic protein (GFAP). Furthermore, in cell conditioned media, rIL-6 stimulated MASP-3 secretion which reached levels similar to those obtained by dbcAMP treatment. Moreover, the detection of a 46-kDa MASP-3 suggested its processing to the mature form in the extracellular cell medium. Interestingly, the H89 PKA inhibitor, mostly affected dbcAMP-induced MASP-1 and MASP-3 mRNA levels, compared to that of rIL-6, suggesting that cAMP/PKA pathway contributes to MASP-1 and MASP-3 up-regulation. MASP-1 and MASP-3 expression increase was concomitant with dbcAMP- or rIL-6-induced phosphorylation of STAT3. Our findings suggest that the increase in intracellular cAMP concentration or rIL-6 stimulation can play a role in innate immunity enhancing MASP-1 and MASP-3 expression level in C6 glioma cells.

Authors : Pagliara Valentina, Parafati Maddalena, Adornetto Annagrazia, White Misti C, Masullo Mariorosario, Grimaldi Maurizio, Arcone Rosaria,



(9) Mannose Binding Lectin and Pentraxin 3 in Patients with Diabetic Retinopathy.[TOP]

Pubmed ID :29961608
Publication Date : //
Mannose binding lectin (MBL) is a protein of the complement system and pentraxin-3 (PTX3) is an acute phase protein both with an important role in inflammatory diseases, such as diabetic retinopathy (DR).

Authors : Hokazono Kenzo, Belizário Fernando Sakata, Portugal Vanessa, Messias-Reason Iara, Nisihara Renato,



(10) S100B immunization triggers NFκB and complement activation in an autoimmune glaucoma model.[TOP]

Pubmed ID :29959432
Publication Date : //
In glaucoma, latest studies revealed an involvement of the complement system with and without an elevated intraocular pressure. In the experimental autoimmune glaucoma model, immunization with antigens, such as S100B, lead to retinal ganglion cell (RGC) loss and optic nerve degeneration after 28 days. Here, we investigated the timeline of progression of the complement system, toll-like-receptor 4 (TLR4), and the transcription factor nucleus factor-kappa B (NFκB). Therefore, rats were immunized with S100B protein (S100) and analyzed at 3, 7, and 14 days. RGC numbers were comparable at all points in time, whereas a destruction of S100 optic nerves was noted at 14 days. A significant increase of mannose binding lectin (MBL) was observed in S100 retinas at 3 days. Subsequently, significantly more MBL cells were seen in S100 optic nerves at 7 and 14 days. Accordingly, C3 was upregulated in S100 retinas at 14 days. An increase of interleukin-1 beta was noted in S100 aqueous humor samples at 7 days. In this study, activation of complement system via the lectin pathway was obvious. However, no TLR4 alterations were noted in S100 retinas and optic nerves. Interestingly, a significant NFκB increase was observed in S100 retinas at 7 and 14 days. We assume that NFκB activation might be triggered via MBL leading to glaucomatous damage.

Authors : Reinehr Sabrina, Reinhard Jacqueline, Gandej Marcel, Gottschalk Ivo, Stute Gesa, Faissner Andreas, Dick H Burkhard, Joachim Stephanie C,