Tuyển tập các báo cáo nghiên cứu khoa học quốc tế về bệnh thú y đề tài: Expression of PSD95 in the rat sciatic nerve | J. Vet. Sci. 2003 4 2 113-116 Veterinary Science Expression of PSD95 in the Rat Sciatic Nerve Hyun-jin Yoo Ik-hyun Cho Jong-hwan Lee Nong-hoon Choe1 Tae-young Kang2 and Byung-joon Chang Department of Anatomy and Histology and Public Health College of Veterinary Medicine Konkuk University Seoul 143-701 Korea 2Department of Veterinary Medicine Cheju National University Jeju 690-756 Korea Received April 13 2003 Accepted July 30 2003 Abstract This study was designed to elucidate the existence of PSD95 in the rat sciatic nerve. Immunohistochemical stains of cryosection and teased fiber of sciatic nerves were performed with goat polyclonal antibody against PSD95. Western blot analysis was also accomplished with the same antibody. We got an interesting result that the rat sciatic nerve obviously showed PSD95 immunoreactivity especially in the nodal and paranodal regions and we also identified a distinct band of PSD95 by western blot. These results suggest PSD95 exists in the sciatic nerve as well as it does in the central nervous system. We suppose PSD95 may have some important roles in ion channel clustering junctional plasticity and signal transduction in the peripheral nerves as well. Key words PSD95 sciatic nerve immunocytochemistry western blot Introduction Postsynaptic density 95 PSD95 was first identified as an abundant cytoskeleton-associated protein found in the post-synaptic density fraction of rat synaptosomes 2 . Recent studies have suggested that it plays an important role in the assembly and organization of excitatory postsynaptic architecture 3 10 13 PSD95 has been identified to the dendrites of hippocampal neurons 2 to the presynaptic plexus of cerebellar basket cells 8 and to the basket cell terminal pinceau of cerebellar cortex and postsynaptic dendrites in both intact and lysed forebrain synaptosomes 5 . This molecule is characterized by three N-terminal PDZ domains an SH3 domains and a C-termianl guanylate kinase GK -like domain thus making that .
