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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) Binding capacity of mannose-binding lectin (MBL) is associated with the severity of chronic Chagas cardiomyopathy.[TOP]

Pubmed ID :29775825
Publication Date : //
Chagas disease (CD) is a global problem. Currently, it affects approximately 15 million individuals in Latin America. It is well know that the human immune response is related to different clinical manifestations. Mannose binding lectin (MBL) plays an important role in innate immunity, and it mediates the phagocytosis and complement-mediated destruction of pathogens. The binding capacity is enhanced by the oligomerization of MBL. In this study, we evaluated the serum concentration and the binding capacity of MBL in patients with chronic chagasic cardiomyopathy. A total of 77 patients with chronic CD were included with indeterminate (n = 19), mild cardiac (n = 29) and severe cardiac (n = 29) forms. The serum concentration and the binding capacity were measured using enzyme-linked immunosorbent assays (ELISA). There was no significant difference in the serum MBL levels between the groups of patients. However, we found a relationship between the binding capacity and the groups studied. Our results suggest that binding capacity of MBL could be an indicator of clinical manifestation in Chronic Chagas cardiomyopathy. Furthermore, combined with the Mannose Binding Index results in a useful clinical tool for management of Chronic Chagas Patients.

Authors : Azevedo Elisa de A N, Barreto Silvana, de Lima Raul Emídio, Teixeira Romero Henrique, Diniz George, Oliveira Wilson, Cavalcanti Maria da Glória A M, Gomes Yara M, Moura Patrícia M M de F, Morais Clarice N L,



(2) Human anti-thrombospondin type 1 domain-containing 7A antibodies induce membranous nephropathy through activation of lectin complement pathway.[TOP]

Pubmed ID :29769410
Publication Date : //
To investigate whether the human anti-thrombospondin type 1 domain-containing 7A (THSD7A) antibody-induced membranous nephropathy is mediated by activating lectin complement pathway. Automatic biochemical apparatus was used to assess renal function of mice. The serum levels of anti-THSD7A antibodies and complement were tested by using Enzyme-linked immunosorbent assay (ELISA). The expression level of THSD7A and Mannose-Binding Lectin (MBL) in clinical tissue, and the histological features of MN in mice were examined by immunochemical methods. We found that THSD7A, MBL and complement expression level from patients with circulating anti-THSD7A antibodies was significantly higher than that in normal group. Furthermore,difference of renal function in anti-THSD7A antibody-containing serum treatment groups and control groups was significant. Meanwhile, human anti-THSD7A autoantibodies activated the complement system and induced the histological features of MN in mice. In conclusion, human anti-THSD7A antibodies induce membranous nephropathy through activating MBL lectin complement pathway in mice.

Authors : Wang Zheng, Wen Lu, Dou Yanna, Zhao Zhanzheng,



(3) Low maternal serum concentrations of mannose-binding lectin (MBL) are associated with the risk of shorter duration of pregnancy and lower birth weight.[TOP]

Pubmed ID :29758096
Publication Date : //
Chronic inflammation has been implicated as the underlying mechanism responsible for the pathophysiology of preterm labor. Mannose-bindig lectin (MBL) plays a central role in the innate immune response and is thus an important component of the first line of defense. The aim of this study was to investigate whether serum concentrations of MBL correlated with the incidence of preterm birth and low birth weight in a cohort of women with signs of threatened preterm birth.

Authors : Koucký Michal, Malíčková Karin, Kopřivová Helena, Cindrová-Davies Tereza, Hrbáčková Hana, Černý Andrej, Šimják Patrik, Pařízek Antonín, Zima Tomáš,



(4) Progressive IgA Nephropathy Is Associated With Low Circulating Mannan-Binding Lectin-Associated Serine Protease-3 (MASP-3) and Increased Glomerular Factor H-Related Protein-5 (FHR5) Deposition.[TOP]

Pubmed ID :29725647
Publication Date : //
IgA nephropathy (IgAN) is characterized by glomerular deposition of galactose-deficient IgA1 and complement proteins and leads to renal impairment. Complement deposition through the alternative and lectin activation pathways is associated with renal injury.

Authors : Medjeral-Thomas Nicholas R, Troldborg Anne, Constantinou Nicholas, Lomax-Browne Hannah J, Hansen Annette G, Willicombe Michelle, Pusey Charles D, Cook H Terence, Thiel Steffen, Pickering Matthew C,



(5) Complement Activation in Patients With Diabetic Nephropathy.[TOP]

Pubmed ID :29725633
Publication Date : //
Complement activation plays a role in various organs in patients with diabetes. However, in diabetic nephropathy (DN), the role of complement activation is poorly understood. We examined the prevalence and clinical significance of complement deposits in the renal tissue of cases with type 1 and type 2 diabetes with and without DN.

Authors : Bus Pascal, Chua Jamie S, Klessens Céline Q F, Zandbergen Malu, Wolterbeek Ron, van Kooten Cees, Trouw Leendert A, Bruijn Jan A, Baelde Hans J,



(6) Effects of MASP2 haplotypes and MASP-2 levels in hepatitis C-infected patients.[TOP]

Pubmed ID :29675993
Publication Date : //
Mannan-binding lectin (MBL) and MBL-associated serine protease 2 (MASP-2) are components of the lectin pathway, which activate the complement system after binding to the HCV structural proteins E1 and E2. We haplotyped 11 MASP2 polymorphisms in 103 HCV patients and 205 controls and measured MASP-2 levels in 67 HCV patients and 77 controls to better understand the role of MASP-2 in hepatitis C susceptibility and disease severity according to viral genotype and fibrosis levels. The haplotype block MASP2*ARDP was associated with protection against HCV infection (OR = 0.49, p = .044) and lower MASP-2 levels in controls (p = .021), while haplotype block AGTDVRC was significantly increased in patients (OR = 7.58, p = .003). MASP-2 levels were lower in patients than in controls (p < .001) and in patients with viral genotype 1 or 4 (poor responders to treatment) than genotype 3 (p = .022) and correlated inversely with the levels of alkaline phosphatase, especially in individuals with fibrosis 3 or 4 (R = -.7, p = .005). MASP2 gene polymorphisms modulate basal gene expression, which may influence the quality of complement response against HCV. MASP-2 levels decrease during chronic disease, independently of MASP2 genotypes, most probably due to consumption and attenuation mechanisms of viral origin and by the reduced liver function, the site of MASP-2 production.

Authors : Silva Amanda A, Catarino Sandra J, Boldt Angelica B W, Pedroso Maria Lucia A, Beltrame Marcia H, Messias-Reason Iara J,



(7) MBL2 gene polymorphism rs1800450 and rheumatic fever with and without rheumatic heart disease: an Egyptian pilot study.[TOP]

Pubmed ID :29653582
Publication Date : //
Rheumatic fever (RF) is the result of an autoimmune response to pharyngitis caused by infection with Streptococcus pyogenes. RF is most prevalent in Africa and the Middle East. Rheumatic heart disease (RHD) is the most serious complication of RF. Mannose-binding lectin 2 gene (MBL2) has been reported to be correlated with different cardiac conditions. In Egyptian patients as a new studied ethnic population, it is the first time to evaluate the association between MBL2 gene polymorphism rs1800450 and RF with and without RHD.

Authors : Gomaa Maher Hassan, Ali Shawkey Sadik, Fattouh Aya Mohamed, Hamza Hala Salah, Badr Mohamed Mohamed,



(8) A Comprehensive Analysis of Regulatory SNPs of Human CLEC7A Gene and Its Validation as Genotypic and Phenotypic Disease Marker in Recurrent Vulvovaginal Infections.[TOP]

Pubmed ID :29616193
Publication Date : //
Recurrent Vulvovaginal infections (RVVI) are the commonly reported microbiological syndrome affecting millions of women globally. Various molecules of innate immune system are instrumental in clearance of these microbial pathogens, thus suggested as one of the most important contributing factor in determining the disease outcome. Dendritic cell-associated C-type lectin-1 (Dectin-1) is an important molecule of innate immunity that is primarily known for its role in antifungal defenses. However, role of dectin-1 in recognition of other pathogens is also documented. The intracellular expression of dectin-1 was shown to be up-regulated by Mannose Binding Lectin (MBL)-mediated opsonophagocytosis of pathogens. Dectin-1 is encoded by , postulated to be a candidate gene in modulating risk of developing RVVI. In this study, we identified causal variants using analysis. To assess their impact on susceptibility to RVVI, these causal variants along with serum dectin-1 levels (sDectin-1) were investigated using polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) and Enzyme Linked Immnosorbent Assay (ELISA) respectively, under a case-control design. Furthermore, effect of these polymorphisms was also assessed on sMBL levels. analysis revealed 9 putative functional conserved SNPs of . Association analysis revealed a significantly lower risk of developing RVVI and its types in carriers of rs3901533 G allele and its homozygous genotypes ( < 0.05). The heterozygous genotype was associated with significant protection against RVVI ( = 0.004). Haplotypes GGG and GTA showed significant protection against RVVI ( < 0.0001; = 0.0003), Bacterial Vaginosis ( = 0.03; = 0.002), Vulvovaginal Candidiasis ( = 0.03; = 0.01) and Mixed Infections ( = 0.007; = 0.04). Mean sDectin-1 levels were significantly high in RVVI and its types compared to controls ( < 0.05). Further, genotype-phenotype stratification showed significant differences within/between cases groups and controls. The rs3901533 polymorphism was also found to be associated with sMBL levels. The present study contributed novel insights into the role of dectin-1 in RVVI. rs3901533 polymorphism and high sDectin-1 levels along with low sMBL levels were found to be associated with RVVI susceptibility. Thus, screening of women with RVVI for these novel associations may lead to better diagnosis and treatment. Also genotyping method used in this study constitutes a simple and reliable assay, which can be confidently, used as a cheaper alternative for genotyping these variants in clinical settings. Finally, new restorative markers for other infectious diseases might be found by exploring nine functionally identified SNPs.

Authors : Kalia Namarta, Kaur Manpreet, Sharma Sujata, Singh Jatinder,



(9) The role of complement components C1q, MBL and C1 inhibitor in pathogenesis of endometriosis.[TOP]

Pubmed ID :29572748
Publication Date : //
The purpose of the work was to evaluate possible associations between the complement components C1q, mannose-binding lectin (MBL) and C1 inhibitor (C1INH) with pathogenesis of endometriosis.

Authors : Sikora Justyna, Wróblewska-Czech Agnieszka, Smycz-Kubańska Marta, Mielczarek-Palacz Aleksandra, Cygal Anna, Witek Andrzej, Kondera-Anasz Zdzisława,



(10) C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules.[TOP]

Pubmed ID :29563915
Publication Date : //
Complement receptor type 1 (CR1) is a multi modular membrane receptor composed of 30 homologous complement control protein modules (CCP) organized in four different functional regions called long homologous repeats (LHR A, B, C, and D). CR1 is a receptor for complement-opsonins C3b and C4b and specifically interacts through pairs of CCP modules located in LHR A, B, and C. Defense collagens such as mannose-binding lectin (MBL), ficolin-2, and C1q also act as opsonins and are involved in immune clearance through binding to the LHR-D region of CR1. Our previous results using deletion variants of CR1 mapped the interaction site for MBL and ficolin-2 on CCP24-25. The present work aimed at deciphering the interaction of C1q with CR1 using new CR1 variants concentrated around CCP24-25. CR1 bimodular fragment CCP24-25 and CR1 CCP22-30 deleted from CCP24-25 produced in eukaryotic cells enabled to highlight that the interaction site for both MBL and C1q is located on the same pair of modules CCP24-25. C1q binding to CR1 shares with MBL a main common interaction site on the collagen stalks but also subsidiary sites most probably located on C1q globular heads, contrarily to MBL.

Authors : Jacquet Mickaël, Cioci Gianluca, Fouet Guillaume, Bally Isabelle, Thielens Nicole M, Gaboriaud Christine, Rossi Véronique,