Cause of Multiple Sclerosis is not well known yet. There are theories that oint out a viral origen that may initiate the autoimmune response. There are a lot of biological agents that could be causative. Among them is Epstein Barr Virus but there are controversies about this topic. With the evaluation of the specific antibody index developed by Reiber, perhaps it will be possible to find some evidences that sign Epstein Barr virus like the cause of the disease. The aim of this paper is to evaluate the antibody index anti‐Epstein Barr virus in 27 patients with multiple sclerosis and 19 control cases. There were significant differences between Qspecific (Specific antibodies in CSF/Specific antibodies in serum) between the sclerosis multiple group and the control group (p<0.0001). The antibody index( Qspecific/Q IgG or Q lim) between both groups was not significant differences (p=0.0519). Anti‐Epstein Barr Qspecific in Multiple Sclerosis could contribute to clarify the etiology of this disease but it is necessary to increase the total of patients involved in the sample in order to confirm that the antibody index in patients could be definitively a probe of Epstein Barr virus as the causative of the disease.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
IntroducctionMASP‐3 functions are not clarified totally, in spite of that it is a regulatory protein from the lectin pathway. It can be found as complexes and its molecular weight is around 105 KDa.Materials and methodsMASP‐3 and albumin from serum and cerebrospinal fluid were quantified by immune‐enzimatic test in a 60 control group without inflammatory process. Q (cerebrospinal fluid/serum) ratio was performed. QMASP‐3 was order and its relative frequency was calculated.ResultsFrom the different inflexion points of the relative frequency was found five different molecular orders and it's identified with a same number of aggregation forms. Blood‐cerebrospinal fluid allows the protein diffusion according to it molecular size and its relationship with their molecular flow.This five aggregation forms was associated with the molecular flow of this structures throughout blood‐cerebrospinal barrier. It takes into account that the structure that diffuses more rapidly should be the 105 KDa native structure y it is possible to associate this aggregation with native multiple structures and its molecular flow.
IntroductionMASP‐3, a protein of the innate immune response is attracting increasing interest, in particularly in relation to its regulatory function in the lectin pathway.ObjectiveProvide data that discriminate the source of MASP‐3 in cerebrospinal fluid.Materials and methods60 serum and cerebrospinal fluid samples from normal controls without organic disease with normal barrier function were obtained. MASP‐3 was assayed in samples of cerebrospinal fluid and serum with an ELISA, coated with anti MASP‐3 antibodies. It takes into account three variables: the molecular size‐dependent concentration gradient between CSF and blood, the variation in transfer between blood and CSF, and the CSF MASP‐3 concentration correlation with the albumin CSF/serum quotient (Qalb), i.e., with CSF flow rate.ResultsMASP‐3 concentration in CSF was lower than its serum concentration but MASP‐3 concentration in CSF was at least three‐fold higher than expected for a molecular‐size dependent passage from blood. The smaller inter‐individual variation of MASP‐3 concentrations in CSF of the control group (CV =0,396) compared to the MBL concentrations in serum (CV=0.413) indicate an independent source of MASP‐3 in CSF. The absolute MASP‐3 concentration in CSF increases with increasing Qalb. Among brain‐derived proteins in CSF only the leptomeningeal proteins showed a (linear) increase with decreasing CSF flow rate in comparison to neuronal and glial proteins that are invariant to changes of Qalb.ConclusionsMASP‐3 in CSF is predominantly brain‐derived and all results pointed to the leptomeningeal cells as the source of the protein.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Eosinophilic meningitis produced by Angiostrongylus cantonensis is an emerging disease in Western hemisphere. MBL and H‐ and M‐ficolins are starters of the lectin pathway.ObjectiveTo determine if MBL and H‐ and M‐ficolins can be synthesizedin central nervous system in patients suffering from eosinophilic meningitis due to Angiostrongylus cantonensis.Methods19 serum and CSF paired samples were obtained from pediatric patients with the diagnosis of eosinophilic meningitis by Angiostrongylus cantonensis. Cerebrospinal fluid was obtained by lumbar puncture and serum from blood was taken by venopuncture. Serum and CSF was stored frozen in aliquots at −80°C until analysis.The local ethics committee approved this study and all patients' tutors gave informed consent.CSF and serum albumin were quantified by immunochemical nephelometry with kinetic analysis. MBL and H‐ and M‐ficolins were measured by commercial enzyme‐linked immunosorbent assay (ELISA) kit.The MBL reibergram was employed in order to determine if MBL can be synthesized inthecentral nervous system or not. The H‐ and M‐ficolins regressions were employed in order to determine if H‐ and M‐ficolins can be synthesized in the central nervous system or not.Results8 patients do not have dysfunction of blood/CSF barrier and 4 patients have intratecal synthesis of MBL.One patient do not have intrathecal synthesis of H‐ficolin (Figure 2A) and all patients have intrathecal synthesis of M‐ficolin (Figure 2B).ConclusionsIntrathecal activation of the lectin pathway by at least one of the quantified starters in this group of patients with eosinophilic meningitis due to Angiostrongylus cantonensis.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
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