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The Lectin Pathway of Complement and Biocompatibility [PDF]
Advances in Experimental Medicine and Biology, 2015 In modern health technologies the use of biomaterials in the form of stents, haemodialysis tubes, artificial implants, bypass circuits etc. is rapidly expanding. The exposure of synthetic, foreign surfaces to the blood and tissue of the host, calls for strict biocompatibility in respect to contact activation, the coagulation system and the complement ...
Hein, Estrid, Garred, Peter
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Ficolins and the lectin complement pathway [PDF]
Immunological Reviews, 2001 Summary:Ficolins, found in various tissues, are a group of proteins containing both a collagen‐like and a fibrinogen‐like domain. Recently, it was shown that ficolins present in serum are lectins with a common binding specificity for N‐acetylglucosamine (GlcNAc). The fibrinogen‐like domain is responsible for the carbohydrate binding.
Teizo Fujita, Misao Matsushita
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Nephron, 2020
IgA vasculitis can present as a glomerulonephritis histologically indistinguishable from IgA nephropathy (IgAN). In IgAN, the alternative and lectin pathways mediate glomerular injury and contribute to kidney function decline. Narsoplimab is a monoclonal
H. Selvaskandan +6 more
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IgA vasculitis can present as a glomerulonephritis histologically indistinguishable from IgA nephropathy (IgAN). In IgAN, the alternative and lectin pathways mediate glomerular injury and contribute to kidney function decline. Narsoplimab is a monoclonal
H. Selvaskandan +6 more
semanticscholar +1 more source
Assays for the Mannan‐Binding Lectin Pathway
Current Protocols in Immunology, 2003AbstractThis unit contains protocols that can be used to measure mannan‐binding lectin (MBL) levels and MBL pathway activity in human plasma or serum. Using a modification of the conventional ELISA, the detection reagent used in the methods described (e.g., an antibody or streptavidin) is labeled with Eu3+ instead of an enzyme.
Gadjeva, Mihaela +2 more
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Activation of the lectin complement pathway by ficolins
International Immunopharmacology, 2001Mannose-binding lectin (MBL), a serum lectin specific for mannose or N-acetylglucosamine (GlcNAc), which contains both a collagen-like domain and a carbohydrate-recognition domain (CRD), plays a role in innate immunity by acting as an opsonin and activating complement in association with MBL-associated serine protease (MASP) via the lectin pathway ...
Naotaka Hamasaki +3 more
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The Lectin Pathway of the Complement System
Microbiology and Immunology, 1996One of the activities of animal lectins is the elimination of pathogens from a host. Serum mannose (or mannan)-binding protein (MBP) (25), in this capacity, recognizes mannose or N-acetylglucosamine on the surfaces of microorganisms. MBP is a member of the 'collectin' family (6), a group of C-type Ca2+-denendent animal lectins (3) which includes two ...
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complement classical and lectin pathways
2010The classical and lectin pathways of complement are major recognition systems of innate immunity that are found in mammals and other animal species. By means of several multimolecular proteases – C1, the mannan-binding lectin (MBL)–MBL-associated serine protease 2 (MBL–MASP-2) and the ficolin–MASP-2 complexes – each comprising a recognition protein and
Thielens, Nicole +2 more
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Immunopharmacology, 1999
Lysis via the newly discovered lectin pathway of complement activation is reviewed. Mannan-coated erythrocytes sensitized with MBL are lysed in human serum containing Mg-EGTA via the lectin pathway by a process which requires alternative pathway amplification.
Henry Gewurz +4 more
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Lysis via the newly discovered lectin pathway of complement activation is reviewed. Mannan-coated erythrocytes sensitized with MBL are lysed in human serum containing Mg-EGTA via the lectin pathway by a process which requires alternative pathway amplification.
Henry Gewurz +4 more
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Lectins and protein traffic early in the secretory pathway
Biochemical Society Symposia, 2002Lectins of the early secretory pathway are involved in selective transport of newly synthesized glycoproteins from the endoplasmic reticulum (ER) to the ER–Golgi intermediate compartment (ERGIC). The most prominent cycling lectin is the mannose-binding type I membrane protein ERGIC-53 (ERGIC protein of 53 kDa), a marker for the ERGIC, which functions ...
Hauri, Hans-Peter +4 more
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Derivatives of the lectin complement pathway in Lophotrochozoa
Developmental & Comparative Immunology, 2019A plethora of non-overlapping immune molecular mechanisms in metazoans is the most puzzling issue in comparative immunobiology. No valid evolutionary retrospective on these mechanisms has been developed. In this study, we aimed to reveal the origin and evolution of the immune complement-like system in Lophotrochozoa.
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