Downregulation of Map Kinase Activity Signalled by HIV-1-gp120 Coat Protein in Granular Neurons and Glial Cells from Rat Cerebellum |
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| Institution: | 1. DIBIT San Raffaele Scientific Institute, “B. Ceccarelli” and CNR Cellular and Molecular Pharmacology Centers, Department of Medical Pharmacology, University of Milan;2. Department of Experimental Medicine, University of Rome “Tor Vergata,” Italy;1. Dermatopatóloga, Centro Dermatológico Dr. Ladislao de la Pascua, Cd de México 06780;2. Dermatooncologa, Centro Dermatológico Dr. Ladislao de la Pascua, Cd de México 06780;3. Dermatológo, Centro Dermatológico Dr. Ladislao de la Pascua, Cd de México 06780;4. Residente de dermatooncología, Centro Dermatológico Dr. Ladislao de la Pascua, Cd de México 06780;5. Residente de tercer año de dermatología, Centro Dermatológico Dr. Ladislao de la Pascua, Cd de México 06780;1. Division of Biomedical Sciences, School of Medicine, University of California, Riverside, 900 University Ave, Riverside, CA, 92521, USA;2. Infectious and Inflammatory Disease Center, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA 92037, USA;3. Animal Models Core, The Scripps Research Institute, 10550 North Torrey Pines Road, MB6, La Jolla, CA 92037, USA |
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| Abstract: | We have studied the effect of gp120 coat protein from HIV-1 on tyrosine phosphorylation processes in primary cultures of granular neurons or glial cells from the cerebellum of neonatal rats. The extracellular application of recombinant gp120 (200 pM) was able to reduce the phosphotyrosine content and the immunoreactivity for active form-specific antibodies of MAP kinase. Whereas in neurons MAP kinase appeared to be the only protein whose phosphotyrosine content was decreased, in glial cultures the inhibitory effect of gp120 on tyrosine phosphorylation processes appeared to be more widespread. In neuronal cultures, the effect of the viral protein was prevented by the concomitant treatment with depolarizing agents. |
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