Differential expression of neuropsin and protease M/neurosin in oligodendrocytes after injury to the spinal cord.
Neuropsin and protease M/neurosin are serine proteases expressed by neurons and glial cells, and serve a variety of functions in the central nervous system (CNS). The current study demonstrates changes in the expression of these proteases following hemisection of the mouse spinal cord. Within unlesioned spinal cord, neuropsin mRNA expression was occasionally observed in the gray but not white matter, while the level of protease M/neurosin mRNA was higher in the white matter. After injury to the spinal cord, neuropsin mRNA expression was induced in the white matter in the area immediately adjacent to the lesion, peaking at 4 days post-injury and disappearing by 14 days. Enhanced expression of protease M/neurosin mRNA was observed throughout the white and gray matter surrounding the lesion, peaking at 4 days and persisting for 14 days. Neuropsin mRNA was expressed predominantly by CNPase-positive oligodendrocytes. Furthermore, most of these cells were also associated with immunoreactivity for protease M/neurosin protein. Within unlesioned spinal cord, most protease M/neurosin mRNA-expressing cells were CNPase-positive oligodendrocytes, and a substantial fraction of these cells also showed immunoreactivity for NG2, a marker for oligodendrocyte progenitors. After injury, protease M/neurosin mRNA expression within NG2-positive cells was significantly decreased, while the constitutive expression in CNPase-positive oligodendrocytes appeared to be preserved. These findings suggest that each subpopulation of oligodendrocytes based on the expression of neuropsin and protease M/neurosin has different roles in the response of the spinal cord to injury as well as in normal homeostasis.
Terayama
Ryuji
R
Department of Anatomy, Asahikawa Medical College, Asahikawa 078-8510, Japan. rjt001@asahikawa-med.ac.jp
Bando
Yoshio
Y
Takahashi
Takayuki
T
Yoshida
Shigetaka
S
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000378:metabolism; D000818:Animals; D000941:Antigens / Q000378:metabolism; D015415:Biomarkers; D004195:Disease Models, Animal; D015536:Down-Regulation / Q000235:genetics; D006706:Homeostasis / Q000235:genetics; D007150:Immunohistochemistry; D007610:Kallikreins / Q000235:genetics* / Q000378:metabolism; D051379:Mice; D008807:Mice, Inbred BALB C; D009413:Nerve Fibers, Myelinated / Q000201:enzymology / Q000473:pathology; D009416:Nerve Regeneration / Q000235:genetics; D009836:Oligodendroglia / Q000166:cytology / Q000201:enzymology*; D011509:Proteoglycans / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics*; D013116:Spinal Cord / Q000201:enzymology* / Q000473:pathology / Q000503:physiopathology; D013119:Spinal Cord Injuries / Q000201:enzymology* / Q000235:genetics*; D013234:Stem Cells / Q000166:cytology / Q000201:enzymology; D013997:Time Factors; D015854:Up-Regulation / Q000235:genetics; D000099216:Chondroitin Sulfate Proteoglycan 4
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases; D000941:Antigens; D015415:Biomarkers; D007610:Kallikreins; D011509:Proteoglycans; D012333:RNA, Messenger; D012697:Serine Endopeptidases; D000099216:Chondroitin Sulfate Proteoglycan 4; C103551:KLK6 protein, human; C094799:KLK8 protein, human; C491223:Prss18 protein, mouse; C114664:Prss19 protein, mouse