Results 311 to 320 of about 387,249 (358)
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Classical pathway complement activity in schizophrenia
Neuroscience Letters, 2005There is considerable evidence to suggest a role for complement in the pathogenesis of schizophrenia, but the data related to the classical pathway complement activity in patients with schizophrenia are conflicting. In the present study, the total hemolytic activity of the complement and the activities of individual complement components, C1, C2, C3 ...
Robert B. Sim+2 more
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Effect of Concanavalin A on the Classical Complement Pathway
The Journal of Immunology, 1977Abstract Lysis of sheep erythrocytes (E) sensitized with anti-Forssman antiserum (EA) is inhibited by the action of concanavalin A (Con A) on whole guinea pig complement (GPC). The degree of inhibition observed for a given quantity of GPC was dependent on the Con A concentration.
J J, Langone, M D, Boyle, T, Borsos
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Control of the classical and the MBL pathway of complement activation
Molecular Immunology, 2000The activation of complement via the mannan-binding lectin (MBL) pathway is initiated by the MBL complex consisting of the carbohydrate binding molecule, MBL, two associated serine proteases, MASP-1 and MASP-2, and a third protein, MAp19. In the present report we used an assay of complement activation specifically reflecting the physiological activity ...
Petersen, Steen Vang+5 more
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Interaction of fucoidan with the proteins of the complement classical pathway
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2003Fucoidan inhibits complement by mechanisms that so far remain to be unraveled, and the objective of this work was to delineate the mode of inhibition by this sulfated polysaccharide. For that purpose, low molecular weight fractions of algal (Ascophyllum nodosum) fucoidan containing the disaccharide unit [-->3)-alpha-L-Fuc(2SO3(-))-(1-->4)-alpha-L-Fuc(2,
Stéphanie Descroix+6 more
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A novel ELISA for the evaluation of the classical pathway of complement
Journal of Immunological Methods, 1998Assessment of the overall function of the classical pathway of complement is traditionally performed by the hemolytic titration assay CH50. In the present study, we established a novel method for the quantitation of complement activity by measuring the deposition of C1q, C4, C3 and C9 on solid-phase IgM by an enzyme-linked immunosorbent assay (ELISA ...
Otto Götze+3 more
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Will a hyperactive classical complement pathway exacerbate autoimmune diseases?
Autoimmunity Reviews, 2023Peer ...
Okrój, Marcin+1 more
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Activation of the classical complement pathway by BioRex-70
Immunology Letters, 1987The cation exchange resin BioRex-70 was able to activate the classical complement pathway in human serum at 37 degrees C over the resin concentration range 0-5% (v/v). Using zymosan-treated human serum, it was found that the activation proceeded as far as complement protein C3.
S.B. Easterbrook-Smith, R.J. Vandenberg
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The Classical Pathway of Complement [PDF]
Complement evolved in parallel with coagulation as part of the primordial explosion of life in the Cambrian era. Remnants of this connection still exist in vertebrate animals as well as invertebrates. A classic example is the horseshoe crab, Limulus polyphemus, still sought after by scientists today to test substances for traces of bacterial ...
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An immunofluorescence assay for complement activation by the classical pathway
Journal of Immunological Methods, 1981The functional integrity of classical complement pathway components was determined by an immunofluorescence (IFL) assay based on the capacity of cytoskeletal intermediate filaments (IMF) to bind C1q and to activate the complement pathway. The assay uses IMF-rich capillary endothelium of human term placentae as complement-activating substrate.
S. Meri, M. Rhen, Ewert Linder
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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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