Decreased Activity in Neuropathic Pain Form and Gene Expression of Cyclin-Dependent Kinase5 and Glycogen Synthase Kinase-3 Beta in Soleus Muscle of Wistar Male Rats

作者: Masoud Rahmati , Seyed Jalal Taherabadi , Mahmoud Mehrabi

DOI: 10.5812/IRCMJ.23324

关键词:

摘要: Background: The relationship between decreased activity/neuropathic pain and gene expression alterations in soleus muscle has remained elusive. Objectives: In this experimental study, we investigated the effects of activity neuropathic form on Cyclin-Dependent Kinase 5 (CDK5) Glycogen Synthase Kinase-3 β (GSK-3β) rats. Materials Methods: Twelve male Wistar rats were randomly divided into three groups: (1) tight ligation L spinal nerve (SNL: n = 4); (2) sham surgery (Sham: 4), (3) control (C: 4). threshold to produce a withdrawal response mechanical thermal stimulus was measured using von Frey filaments radiation heat apparatus, respectively. Following 4 weeks after surgery, left removed mRNA levels determined by real-time Polymerase Chain Reaction (PCR). Results: Compared animals, ligated animals developed hypersensitivity during total period study. Soleus weight as well CDK5 (less than ~ 0.4 fold) GSK-3β (up 7 folds) increased animals. Conclusions: These results showed enhanced atrophy processes following peripheral damage might provide useful approach study underlying mechanisms associated with clinical syndromes.

参考文章(52)
Gavin I Welsh, Christa M Miller, A Jane Loughlin, Nigel T Price, Christopher G Proud, Regulation of eukaryotic initiation factor eIF2B: glycogen synthase kinase-3 phosphorylates a conserved serine which undergoes dephosphorylation in response to insulin FEBS Letters. ,vol. 421, pp. 125- 130 ,(1998) , 10.1016/S0014-5793(97)01548-2
Darren A. E. Cross, Dario R. Alessi, Philip Cohen, Mirjana Andjelkovich, Brian A. Hemmings, Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B Nature. ,vol. 378, pp. 785- 789 ,(1995) , 10.1038/378785A0
Philipp Gobrecht, Marco Leibinger, Anastasia Andreadaki, Dietmar Fischer, Sustained GSK3 activity markedly facilitates nerve regeneration. Nature Communications. ,vol. 5, pp. 4561- 4561 ,(2014) , 10.1038/NCOMMS5561
Karlie Jones, Christina Wei, Polina Iakova, Enrico Bugiardini, Christiane Schneider-Gold, Giovanni Meola, James Woodgett, James Killian, Nikolai A. Timchenko, Lubov T. Timchenko, GSK3β mediates muscle pathology in myotonic dystrophy Journal of Clinical Investigation. ,vol. 122, pp. 4461- 4472 ,(2012) , 10.1172/JCI64081
David J. Glass, Skeletal muscle hypertrophy and atrophy signaling pathways The International Journal of Biochemistry & Cell Biology. ,vol. 37, pp. 1974- 1984 ,(2005) , 10.1016/J.BIOCEL.2005.04.018
James DR Knight, Rashmi Kothary, The myogenic kinome: protein kinases critical to mammalian skeletal myogenesis Skeletal Muscle. ,vol. 1, pp. 29- 29 ,(2011) , 10.1186/2044-5040-1-29
Cheng-Hui Fang, Bing-Guo Li, J. Howard James, Jy-Kung King, Amy R. Evenson, Glenn D. Warden, Per-Olof Hasselgren, Protein Breakdown in Muscle from Burned Rats Is Blocked by Insulin-Like Growth Factor I and Glycogen Synthase Kinase-3β Inhibitors Endocrinology. ,vol. 146, pp. 3141- 3149 ,(2005) , 10.1210/EN.2004-0869
M. W. Pfaffl, A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Research. ,vol. 29, pp. 0- 0 ,(2001) , 10.1093/NAR/29.9.E45
Gerhard Dürnberger, Bahar Z. Camurdanoglu, Matthias Tomschik, Michael Schutzbier, Elisabeth Roitinger, Otto Hudecz, Karl Mechtler, Ruth Herbst, Global analysis of muscle-specific kinase signaling by quantitative phosphoproteomics Molecular & Cellular Proteomics. ,vol. 13, pp. 1993- 2003 ,(2014) , 10.1074/MCP.M113.036087