title: The chondroitin sulphate proteoglycan brevican is upregulated by astrocytes after entorhinal cortex lesions in adult rats.
abstract: The chondroitin sulphate proteoglycan brevican is one of the most abundant extracellular matrix molecules in the adult rat brain. It is primarily synthesized by astrocytes and is believed to influence astroglial motility during development and under certain pathological conditions. In order to study a potential role of brevican in the glial reaction after brain injury, its expression was analysed following entorhinal cortex lesion in rats (12 h, 1, 2, 4, 10, 14 and 28 days and 6 months post lesion). In situ hybridization and immunohistochemistry were employed to study brevican mRNA and protein, respectively, in the denervated outer molecular layer of the fascia dentata and at the lesion site. In both regions brevican mRNA was upregulated between 1 and 4 days post lesion. The combination of in situ hybridization with immunohistochemistry for glial fibrillary acidic protein demonstrated that many brevican mRNA-expressing cells are astrocytes. In the denervated zone of the fascia dentata, immunostaining for brevican was increased by 4 days, reached a maximum by 4 weeks and remained detectable up to 6 months post lesion. Electron microscopic immunocytochemistry showed that brevican is a component of the extracellular matrix compartment. At the lesion site a similar time course of brevican upregulation was observed. These data demonstrate that brevican is upregulated in areas of brain damage as well as in areas denervated by a lesion. They suggest a role of brevican in reactive gliosis and are compatible with the hypothesis that brevican is involved in the synaptic reorganization of denervated brain areas.
authors.affiliation: Institute of Anatomy, University of Freiburg, Germany.
authors.forename: N
authors.initials: N
authors.lastname: Thon
authors.forename: C A
authors.initials: CA
authors.lastname: Haas
authors.forename: U
authors.initials: U
authors.lastname: Rauch
authors.forename: T
authors.initials: T
authors.lastname: Merten
authors.forename: R
authors.initials: R
authors.lastname: Fässler
authors.forename: M
authors.initials: M
authors.lastname: Frotscher
authors.forename: T
authors.initials: T
authors.lastname: Deller
mesh_terms: D000110:Acetylcholinesterase / Q000032:analysis; D000367:Age Factors; D000818:Animals; D001253:Astrocytes / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D015153:Blotting, Western; D058581:Brevican; D002799:Cholinergic Fibers / Q000201:enzymology / Q000648:ultrastructure; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D003714:Denervation; D018891:Dentate Gyrus / Q000737:chemistry / Q000166:cytology / Q000378:metabolism; D018728:Entorhinal Cortex / Q000293:injuries* / Q000378:metabolism*; D004827:Epilepsy / Q000503:physiopathology; D005109:Extracellular Matrix / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D015870:Gene Expression / Q000502:physiology; D017403:In Situ Hybridization; D037181:Lectins, C-Type; D008297:Male; D008854:Microscopy, Electron; D009419:Nerve Tissue Proteins / Q000032:analysis / Q000235:genetics* / Q000378:metabolism; D009473:Neuronal Plasticity / Q000502:physiology; D012333:RNA, Messenger / Q000032:analysis; D051381:Rats; D017207:Rats, Sprague-Dawley; D015854:Up-Regulation / Q000235:genetics
chemical_list: C546939:Bcan protein, rat; D058581:Brevican; D011508:Chondroitin Sulfate Proteoglycans; D037181:Lectins, C-Type; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D000110:Acetylcholinesterase