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Robert1bombe

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On observed. We saw reduced degradation of I B in these cells, which likely accounts for less nuclear NF- B. Newly synthesized I B can terminate the inflammatory signal by entering the nucleus and binding to NF- B to cause its export to the cytoplasm (88, 89). Thus the rate of I B recovery determinesJOURNAL OF BIOLOGICAL CHEMISTRYStathmin Reduction in Macrophage Activationthe length of interaction
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On observed. We saw reduced degradation of I B in these cells, which likely accounts for less nuclear NF- B. Newly synthesized I B can terminate the inflammatory signal by entering the nucleus and binding to NF- B to cause its export to the cytoplasm (88, 89). Thus the rate of I B recovery determinesJOURNAL OF BIOLOGICAL CHEMISTRYStathmin Reduction in Macrophage Activationthe length of interaction
1
Ation of stathmin, indicating that LPS activation of Cdk1 kinase is the major contributing factor for rapid stathmin destruction. Our studies focused on early time points of macrophage classical activation when the major morphological and phenotypic events are occurring. We demonstrate that the classically activated macrophages adopt distinct cell morphologies and that stathmin reduction is requir
1
Ation of stathmin, indicating that LPS activation of Cdk1 kinase is the major contributing factor for rapid stathmin destruction. Our studies focused on early time points of macrophage classical activation when the major morphological and phenotypic events are occurring. We demonstrate that the classically activated macrophages adopt distinct cell morphologies and that stathmin reduction is requir
1
IONS FOR HEAT SHOCK PROTEIN 70 (Hsp70)-Hsp40 MODE OF FUNCTIONSReceived for publication, December 7, 2011, and in revised form, April 9, 2012 Published, JBC Papers in Press, April 10, 2012, DOI 10.1074/jbc.M111.Hirotaka Suzuki, Ayami Ikeda, Sachie Tsuchimoto, Ko-ichi Adachi, Aki Noguchi, Yoshihiro Fukumori, and Masaaki Kanemori1 From the School of Natural System, College of Science and Engineering,
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Ls of stathmin-GFP compared with cells expressing high levels of stathmin-GFP. Cytoskeleton integrity is necessary for the nuclear translocation of NF- B (90, 91), and stathmin down-regulation in activated macrophages is crucial for the stabilization of MTs. Our results indicate that MT disruption due to stathmin overexpression would expectedly blunt this movement. In closing, we have revealed a k
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IONS FOR HEAT SHOCK PROTEIN 70 (Hsp70)-Hsp40 MODE OF FUNCTIONSReceived for publication, December 7, 2011, and in revised form, April 9, 2012 Published, JBC Papers in Press, April 10, 2012, DOI 10.1074/jbc.M111.Hirotaka Suzuki, Ayami Ikeda, Sachie Tsuchimoto, Ko-ichi Adachi, Aki Noguchi, Yoshihiro Fukumori, and Masaaki Kanemori1 From the School of Natural System, College of Science and Engineering,
1
Ation of stathmin, indicating that LPS activation of Cdk1 kinase is the major contributing factor for rapid stathmin destruction. Our studies focused on early time points of macrophage classical activation when the major morphological and phenotypic events are occurring. We demonstrate that the classically activated macrophages adopt distinct cell morphologies and that stathmin reduction is requir
1
Ation of stathmin, indicating that LPS activation of Cdk1 kinase is the major contributing factor for rapid stathmin destruction. Our studies focused on early time points of macrophage classical activation when the major morphological and phenotypic events are occurring. We demonstrate that the classically activated macrophages adopt distinct cell morphologies and that stathmin reduction is requir
1
On observed. We saw reduced degradation of I B in these cells, which likely accounts for less nuclear NF- B. Newly synthesized I B can terminate the inflammatory signal by entering the nucleus and binding to NF- B to cause its export to the cytoplasm (88, 89). Thus the rate of I B recovery determinesJOURNAL OF BIOLOGICAL CHEMISTRYStathmin Reduction in Macrophage Activationthe length of interaction