Proteomic Profiling in the Spinal Cord and Sciatic Nerve in a Global Cerebral Ischemia-Induced Mechanical Allodynia Mouse Model

• Published in: Biological & pharmaceutical bulletin Vol. 39; no. 2; pp. 230 - 238
• Main Authors: Harada, Shinichi, Matsuura, Wataru, Takano, Masaoki, Tokuyama, Shogo
• Format: Journal Article
• Language: English
• Published: Japan Pharmaceutical Society of Japan 01.02.2016; Japan Science and Technology Agency
• Subjects: Animals; Brain Ischemia - metabolism; Electrophoresis, Gel, Two-Dimensional; Gene Expression Regulation - physiology; Hyperalgesia - metabolism; Male; Mice; Proteomics; Sciatic Nerve - metabolism; Spinal Cord - metabolism; Time Factors; Transcriptome
• ISSN: 0918-6158; 1347-5215
• DOI: 10.1248/bpb.b15-00647

Central post-stroke pain (CPSP) is one of the complications of cerebral ischemia and neuropathic pain syndrome. At present, there are few studies of pain in regions such as the spinal cord or sciatic nerve in cerebral ischemic animal models. To identify proteomic changes in the spinal cord and sciatic nerve in global cerebral ischemic model mice, in the present study we performed an investigation using proteomic methods. In a comparison between the intensity of protein spots obtained from a sham and that from a bilateral carotid artery occulusion (BCAO) in spinal cord and sciatic nerve, the levels of 10 (spinal cord) and 7 (sciatic nerve) protein spots were altered. The protein levels in the spinal cord were significantly increased in NG,NG-dimethylarginine dimethylaminohydrolase 1 (DDAH1), 6-phosphogluconolactonase isoform 1, and precursor apoprotein A-I and decreased in dihydropyrimidinase-related protein 2 (CRMP-2), enolase 1B, rab guanosine 5'-diphosphate (GDP) dissociation inhibitor beta, septin-2 isoform a, isocitrate dehydrogenase subunit alpha, cytosolic malate dehydrogenase, and adenosine triphosphate synthase. The protein levels in the sciatic nerve were significantly increased in a mimecan precursor, myosin light chain 1/3, and myosin regulatory light chain 2 (MLC2), and decreased in dihydropyrimidinase-related protein 3 (CRMP-4), protein disulfide-isomerase A3, 3-hydroxy-3-methylglutaryl-coenzyme A synthase 1, and B-type creatine kinase. In addition, CRMP-2 and CRMP-4 protein levels were decreased, and DDAH1 and MLC2 protein levels were increased on day 1 after BCAO using Western blotting. These results suggested that changes in these proteins may be involved in the regulation of CPSP.