title: Expressions of neuropilin-1, neuropilin-2 and semaphorin 3A mRNA in the rat brain after middle cerebral artery occlusion.
abstract: This study investigated the spatial and temporal expressions of mRNA encoding neuropilin (Npn)-1, Npn-2 and semaphorin3A (Sema3A) in the rat brain after occlusion of the middle cerebral artery (MAC) distal to the striate branches. The expression of Npn-1 mRNA was transiently upregulated in layers V and VI of the parietal cortex not entering infarction on the lesion side from 3 to 6 h after MCA occlusion. The transient up-regulation of Npn-1 mRNA expression was presumably accompanied by an increase in Npn-1 protein as shown by immunohistochemistry in combination with in situ hybridization histochemistry. Intense Npn-2 mRNA expression was noted temporarily in layer II of the parietal cortex on the lesion side from 1 to 6 h after MCA occlusion. The expression of Sema3A mRNA was upregulated in layer VI of the non-infarcted parietal cortex on the lesion side at 6 h after MCA occlusion. The above increases in mRNA expression were no longer observed at 12 h after MCA occlusion. The expressions of Npn-1, -2 and Sema3A mRNA were not detected in the ventroposterior thalamic nucleus undergoing secondary degeneration after MCA occlusion. In the infarct lesion or ischemic core, neuronal expressions of Npn-1, -2 and Sema3A disappeared by 3 days after MCA occlusion as the neurons in situ entered apoptosis or necrosis. In contrast, ED-1-positive microglia/macrophages with Npn-1 and Npn-2 mRNA were observed in the infarct lesion at 1 week after MCA occlusion. These findings suggest that the temporal up-regulation of Npn-1 and Sema 3A mRNA expressions in the non-infarcted parietal cortex on the lesion side is insufficient to induce neuronal cell death possibly because the up-regulated mRNA molecules are not fully translated and that the overexpression of Npn-1 and/or Npn-2 in the ischemic core with degenerating neurons enables activated microglial cells to contact the damaged neurons in situ for phagocytosis.
authors.affiliation: Department of Anatomy, Ehime University School of Medicine, Shigenobu, 791-0295, Ehime, Japan. hiroko@m.ehime-u.ac.jp
authors.forename: H
authors.initials: H
authors.lastname: Fujita
authors.forename: B
authors.initials: B
authors.lastname: Zhang
authors.forename: K
authors.initials: K
authors.lastname: Sato
authors.forename: J
authors.initials: J
authors.lastname: Tanaka
authors.forename: M
authors.initials: M
authors.lastname: Sakanaka
mesh_terms: D000818:Animals; D001253:Astrocytes / Q000378:metabolism; D001921:Brain / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D002545:Brain Ischemia / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D002470:Cell Survival / Q000235:genetics; D002478:Cells, Cultured / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D005786:Gene Expression Regulation / Q000502:physiology; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D006023:Glycoproteins / Q000235:genetics*; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D020244:Infarction, Middle Cerebral Artery / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D017628:Microglia / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000378:metabolism; D009410:Nerve Degeneration / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D009419:Nerve Tissue Proteins / Q000235:genetics*; D009474:Neurons / Q000378:metabolism; D039942:Neuropilin-1; D009836:Oligodendroglia / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D051381:Rats; D011918:Rats, Inbred SHR; D040121:Semaphorin-3A; D013997:Time Factors; D015854:Up-Regulation / Q000235:genetics; D020651:Ventral Thalamic Nuclei / Q000378:metabolism / Q000473:pathology / Q000503:physiopathology
chemical_list: D005904:Glial Fibrillary Acidic Protein; D006023:Glycoproteins; D008869:Microtubule-Associated Proteins; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D040121:Semaphorin-3A; D039942:Neuropilin-1