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http://purl.uniprot.org/citations/7592978http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7592978http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7592978http://www.w3.org/2000/01/rdf-schema#comment"cDNA clones encoding proteins related to the aggrecan/versican family of proteoglycan core proteins have been isolated with antisera against rat brain synaptic junctions. Two sets of overlapping cDNAs have been characterized that differ in their 3'-terminal regions. Northern analyses with probes derived from unique regions of each set were found to hybridize with two brain-specific transcripts of 3.3 and 3.6 kilobases (kb). The 3.6-kb transcript encodes a polypeptide that exhibits 82% sequence identity with bovine brevican and is thought to be the rat ortholog of brevican. Interestingly, the polypeptide deduced from the open reading frame of the 3.3-kb transcript is truncated just carboxyl-terminal of the central domain of brevican and instead contains a putative glypiation signal. Antibodies raised against a bacterially expressed glutathione S-transferase-brevican fusion protein have been used to show that both soluble and membrane-bound brevican isoforms exist. Treatment of the crude membrane fraction and purified synaptic plasma membranes with phosphatidylinositol-specific phospholipase C revealed that isoforms of brevican are indeed glycosylphosphatidylinositol-anchored to the plasma membrane. Moreover, digestions with chondroitinase ABC have indicated that rat brevican, like its bovine ortholog, is a conditional chondroitin sulfate proteoglycan. Immunohistochemical studies have shown that brevican is widely distributed in the brain and is localized extracellularly. During postnatal development, amounts of both soluble and phosphatidylinositol-specific phospholipase C-sensitive isoforms increase, suggesting a role for brevican in the terminally differentiating and the adult nervous system."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.45.27206"xsd:string
http://purl.uniprot.org/citations/7592978http://purl.org/dc/terms/identifier"doi:10.1074/jbc.270.45.27206"xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Richter K."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Richter K."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Gundelfinger E.D."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Gundelfinger E.D."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Faessler R."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Faessler R."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Garner C.C."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Garner C.C."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Seidenbecher C.I."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Seidenbecher C.I."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Rauch U."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/author"Rauch U."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/pages"27206-27212"xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/pages"27206-27212"xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/title"Brevican, a chondroitin sulfate proteoglycan of rat brain, occurs as secreted and cell surface glycosylphosphatidylinositol-anchored isoforms."xsd:string
http://purl.uniprot.org/citations/7592978http://purl.uniprot.org/core/title"Brevican, a chondroitin sulfate proteoglycan of rat brain, occurs as secreted and cell surface glycosylphosphatidylinositol-anchored isoforms."xsd:string
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