Cell type-specific upregulation of myristoylated alanine-rich C kinase substrate and protein kinase C-α, -β I, -β II, and -δ in microglia following kainic acid-induced seizures

• Published in: Experimental & molecular medicine 2006, 38(3), , pp.310-319
• Main Authors: 은수용, 김은혜, 강기석, 김화정, 안상미, 김순종, 조수현, 김상정, Perry J. Blackshear, 김준
• Format: Article
• Language: Korean
• Subjects: 생화학
• ISSN: 1226-3613; 2092-6413

Myristoylated alanine-rich C kinase substrate (MARCKS) is a (PKC) substrate and has been implicated in actin cytoskeletal rearrangement in response to extra-cellular stimuli. Although MARCKS was extensively examined in various cell culture systems, the physiological function of MARCKS in the central nervous system has not been clearly understood. We investigated alterations of cellular distribution and phosphorylation of MARCKS in the hippocampus following kainic acid (KA)-induced seizures. KA (25 mg/kg, i.p.) was administered to eight to nine week-old C57BL/6 mice. Behavioral seizure activity was observed for 2 h after the onset of seizures and was terminated with diazepam (8 mg/kg, i.p.). The animals were sacrificed and analyzed at various points in time after the initiation of seizure activity. Using double-labeling immunofluorescence analy-phosphorylation of MARCKS was dramatically upregulated specifically in microglial cells after KA-induced seizures, but not in other types of glial cells. PKC α, β I, β II and δ, from various PKC isoforms examined, also were markedly upregulated, speci-fically in microglial cells. Moreover, immunore-activities of phosphorylated MARCKS were co- localized in the activated microglia with those of the above isoforms of PKC. Taken together, our in vivo data suggest that MARCKS is closely linked to microglial activation processes, which are important mation and neurodegeneration. KCI Citation Count: 8