title: Occurrence of a N-terminal proteolytic fragment of neurocan, not a C-terminal half, in a perineuronal net in the adult rat cerebrum.
abstract: Neurocan is a nervous tissue-unique chondroitin sulfate proteoglycan (CSPG) whose expression and proteolytic cleavage are developmentally regulated. In the adult rat brain, neurocan is completely cleaved into some proteoglycan fragments including the C-terminal half known as neurocan-C and a N-terminal fragment with a 130 kDa core glycoprotein (neurocan-130). We describe here the differential distribution of these two neurocan-derived CSPGs in the adult rat cerebrum and the occurrence of neurocan-130 as a new member of a perineuronal net-constituting molecule. At the light microscopic level, neurocan-130 exhibited pericellular localization around a subset of neurons in addition to diffuse distribution in the neuropil. In contrast, neurocan-C was distributed only diffusely in the neuropil. Double staining with anti-neurocan-130 and anti-synaptophysin antibodies suggested that neurocan-130 was localized in the vicinity of the synapses, but not at the synapses. Immunoelectron microscopy showed that neurocan-130 was mainly localized in the cytoplasm of glial cell processes, the so-called glial perineuronal net, encompassing the cell bodies of certain neurons. The presence of neurocan-130 in a limited number of glial cells may reflect some functional heterogeneity of the glia.
authors.affiliation: Department of Perinatology, Institute for Developmental Research, Kasugai, Aichi 480-0392, Japan. i45365u@nucc.cc.nagoya-u.ac.jp
authors.forename: F
authors.initials: F
authors.lastname: Matsui
authors.forename: M
authors.initials: M
authors.lastname: Nishizuka
authors.forename: Y
authors.initials: Y
authors.lastname: Yasuda
authors.forename: S
authors.initials: S
authors.lastname: Aono
authors.forename: E
authors.initials: E
authors.lastname: Watanabe
authors.forename: A
authors.initials: A
authors.lastname: Oohira
mesh_terms: D000367:Age Factors; D000818:Animals; D001923:Brain Chemistry / Q000502:physiology*; D002540:Cerebral Cortex / Q000737:chemistry / Q000166:cytology / Q000254:growth & development; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D006624:Hippocampus / Q000737:chemistry / Q000166:cytology / Q000254:growth & development; D037181:Lectins, C-Type; D016253:Microscopy, Immunoelectron; D017072:Neostriatum / Q000737:chemistry / Q000166:cytology / Q000254:growth & development; D009419:Nerve Tissue Proteins / Q000032:analysis* / Q000737:chemistry* / Q000378:metabolism; D058580:Neurocan; D009457:Neuroglia / Q000737:chemistry* / Q000648:ultrastructure; D009474:Neurons / Q000737:chemistry / Q000648:ultrastructure; D019581:Neuropil / Q000737:chemistry* / Q000648:ultrastructure; D010446:Peptide Fragments / Q000032:analysis*; D011817:Rabbits; D051381:Rats; D017207:Rats, Sprague-Dawley; D016708:Synaptophysin / Q000032:analysis
chemical_list: D011508:Chondroitin Sulfate Proteoglycans; D037181:Lectins, C-Type; D009419:Nerve Tissue Proteins; D058580:Neurocan; D010446:Peptide Fragments; D016708:Synaptophysin; C076817:NCAN protein, human