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- 저자 : Blackshear, Perry J. (검색결과 2 건)
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Jamal Uddin, Md.,Joe, Yeonsoo,Zheng, Min,Blackshear, Perry J.,Ryter, Stefan W.,Park, Jeong Woo,Chung, Hun Taeg Elsevier 2013 FREE RADICAL BIOLOGY AND MEDICINE Vol.65 No.-
<P><B>Abstract</B></P> <P>Nicotine stimulates the cholinergic anti-inflammatory pathway and prevents excessive inflammation by inhibiting the release of inflammatory cytokines from macrophages. We have previously reported that heme oxygenase-1 (HO-1) and tristetraprolin (TTP) are induced by nicotine and mediate the anti-inflammatory function of nicotine in macrophages. However, it was not clear whether the two molecules are functionally linked. In this study, we sought to determine whether HO-1 associates with TTP to mediate the anti-inflammatory effects of nicotine. Inhibition of HO-1 activity or HO-1 expression attenuated the effects of nicotine on STAT3 activation, TTP induction, and TNF-α production in LPS-treated macrophages. Induction of HO-1 expression increased the level of TTP in the absence of nicotine. In an LPS-induced endotoxemia model, HO-1 deficiency blocked the effects of nicotine on the STAT3 phosphorylation, TTP induction, and LPS-induced TNF-α production in the liver. Downregulation of STAT3 by siRNA attenuated the effect of nicotine on TTP expression and TNF-α production but did not affect the nicotine-mediated induction of HO-1. In TTP knockout mice, nicotine treatment enhanced HO-1 expression and STAT3 activation but failed to inhibit LPS-induced TNF-α production. Our results suggest that HO-1 and TTP are functionally linked in mediating the anti-inflammatory effects of nicotine; HO-1 is necessary for the induction of TTP by nicotine. This novel nicotine–HO-1–TTP signaling pathway provides new possibilities for the treatment of inflammatory diseases.</P>
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은수용,김은혜,강기석,김화정,안상미,김순종,조수현,김상정,Perry J. Blackshear,김준 생화학분자생물학회 2006 Experimental and molecular medicine Vol.38 No.3
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.
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