Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.11.18 (MAP)
 7,412 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A clinical and electromyographic study was carried out to assess the therapeutic efficacy and general tolerance of a new mixture of internal ester gangliosides, with retarded neuropathy due to alcoholism. The study included the comparison between treatment for two months with internal ester gangliosides and traditional multi-vitamin treatment; the study was double-blind and randomised, and was performed according to an experimental plan using a double placebo technique. In order to assess damage to the PNS and the therapeutic efficacy of the two treatments, the following EMG tests were carried out: bilateral motory VDC, latency and width of MAP for SPE nerve, bilateral sensory VDC, latency and width of SAP for sural nerve. With regard to the clinical picture, statistical analyses were calculated using Mann-Whitney's test. Statistical evaluations for EMG tests were performed using Student's "t" test for unrelated groups in differences between the basal and final values of the variables taken into consideration. On the basis of results, it is possible to conclude that: a) the clinical variations and symptomatology showed a statistical significance in favour of the new ganglioside in comparison to the group treated with multi-vitamins; b) a statistically significant difference was observed in some electroneurographic parameters, namely VCM and latency of the SPE nerve, which was in favour of the group treated with the new ganglioside.
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PMID:[Clinical and electromyographic study of the therapeutic effectiveness and general tolerability of a new mixture of internal ester gangliosides in patients with peripheral neuropathy caused by alcoholism]. 217 22

In contrast with results obtained in experimental animals, antibodies to microtubule associated protein-2 (MAP2) preferentially label abnormal structures in human nervous system tissue samples, but the normal sites at which MAP2 is expressed are not well-defined. To determine the distribution of MAP2 in the human central (CNS) and peripheral (PNS) nervous systems, we prepared monoclonal antibodies (MAbs) specific to MAP2, and compared the localization of this MAP in postmortem bovine and human tissues as well as in several human neural cell lines that express either neurofilament (NF) or glial filament (GF) proteins. Eight MAbs specific for phosphate-independent epitopes in bovine and human MAP2 were obtained, and those that performed well in tissues produced immunoreactivity confined to the somatodendritic domain of neurons in bovine and human CNS and PNS tissues. Other neural cells (e.g. astrocytes) did not express MAP2 immunoreactivity using these MAbs. Postmortem delays of less than 24 h prior to tissue denaturation did not affect the distribution of MAP2 immunoreactivity. However, microwave denaturation of these tissues preserved MAP2 immunoreactivity better than fixation with Bouin's solution or formalin. Microwave treatment also improved the immunoreactivity of several MAbs for NF and GF proteins. Finally, MAP2 was not detected in human neural cell lines that express NF (2) or GF (1) proteins. We conclude that microwave denaturation provides an effective means to preserve the immunoreactivity of normal human neuronal cytoskeletal proteins, and that this method of tissue denaturation allows the normal distribution of MAP2 to be defined in postmortem samples of human CNS and PNS tissues.
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PMID:Distribution of phosphate-independent MAP2 epitopes revealed with monoclonal antibodies in microwave-denatured human nervous system tissues. 247 25

Of the axonal signals influencing myelination, adhesion molecules expressed at the axonal surface are strong candidates to mediate interactions between myelinating cells and axons. The recognition cell-adhesion molecule L1, a member of the immunoglobulin superfamily has been shown to play important roles in neuronal migration and survival, and in PNS myelination. We have investigated the role of axonally expressed L1 in CNS myelination. In co-cultures of myelinating oligodendrocytes and neurons derived from murine brain, we demonstrate that, before myelination, L1 immunoreactivity is confined to neurites. After myelination commences, L1 expression is downregulated on myelinated axons and adjacent, but not yet myelinated, internodes.Interfering with L1 before the onset of myelination, by adding either anti-L1 antibody or L1-Fc fusion proteins to the culture medium, inhibits myelination. In addition, in purified cultures of oligodendrocytes, L1-Fc fusion protein prevents lysophosphatidic acid-induced activation of the mitogen-activated kinase (MAP)-kinase pathway. Together, our data indicate that L1 is involved in the initiation of CNS myelination, and that this effect might involve the dephosphorylation of oligodendroglial phosphoproteins.
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PMID:Axonal cell-adhesion molecule L1 in CNS myelination. 1863 7