Localization of chondroitin sulfate proteoglycan versican in adult brain with special reference to large projection neurons

Horii-Hayashi, Noriko; Okuda, Hiromichi; Tatsumi, Kouko; Ishizaka, Shigeaki; Yoshikawa, Masahide; Wanaka, Akio

doi:10.1007/s00441-008-0698-1

Cited by 18 publications

(19 citation statements)

References 34 publications

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“…2E). In accordance with the findings reported previously (Horii-Hayashi et al, 2008), we found versican GAG labeling to be expressed on neurons, as staining often overlapped with -III-tubulin (Fig. 5K, Supplementary Fig.…”

Section: Cspgs Are Differentially Localized In the Cerebral Cortexsupporting

confidence: 92%

“…This antibody particularly detects versican GAG (versican V2 and V0) domain of mouse versican (manufacturer's webpage) and not GAG domain (V1, V3). On the gel, the antibody detects a high molecular weight band at around 400kDa from cerebral cortex homogenate (Horii-Hayashi et al, 2008). Immunofluorescence staining demonstrated that this antibody labels cortical neurons (Horii-Hayashi et al, 2008).…”

Section: Antibody Characterizationmentioning

confidence: 98%

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Alterations in sulfated chondroitin glycosaminoglycans following controlled cortical impact injury in mice

Katagiri

Susarla

et al. 2012

J of Comparative Neurology

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Chondroitin sulfate proteoglycans (CSPGs) play a pivotal role in many neuronal growth mechanisms including axon guidance and the modulation of repair processes following injury to the spinal cord or brain. Many actions of CSPGs in the central nervous system (CNS) are governed by the specific sulfation pattern on the glycosaminoglycan (GAG) chains attached to CSPG core proteins. To elucidate the role of CSPGs and sulfated GAG chains following traumatic brain injury (TBI), controlled cortical impact injury of mild to moderate severity was performed over the left sensory motor cortex in mice. Using immunoblotting and immunostaining, we found that TBI resulted in an increase in the CSPGs neurocan and NG2 expression in a tight band surrounding the injury core, which overlapped with the presence of 4-sulfated CS GAGs but not with 6-sulfated GAGs. This increase was observed as early as 7 days post injury (dpi), and persisted up to 28 dpi. Labeling with markers against microglia/macrophages, NG2 + cells, fibroblasts and astrocytes showed that these cells were all localized in the area, suggesting multiple origins of chondroitin-4-sultate increase. TBI also caused a decrease in the expression of aggrecan and phosphacan in the pericontusional cortex with a concomitant reduction in the number of perineuronal nets. In summary, we describe a dual response in CSPGs where they may be actively involved in complex repair processes following TBI. INDEXING TERMSChondroitin sulfate proteoglycan; traumatic brain injury; extracellular matrix; perineuronal nets

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Section: Cspgs Are Differentially Localized In the Cerebral Cortexsupporting

confidence: 92%

Section: Antibody Characterizationmentioning

confidence: 98%

Alterations in sulfated chondroitin glycosaminoglycans following controlled cortical impact injury in mice

Katagiri

Susarla

et al. 2012

J of Comparative Neurology

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“…Monoclonal antibody 5D5 to versican G3 domain was kindly supplied as ascites fluid by Prof Firoz Rahemtulla, University of Birmingham, Alabama, USA. Rabbit polyclonal antibodies to the GAG-a (amino acids 535-598) and GAG-b (amino acids 1,360-1,439) core protein domains of mouse versican (Horii-Hayashi et al 2008) were purchased from Chemicon Australia through Invitrogen, Sydney, Australia. Anti type I collagen (clone I-8H5), anti type II collagen (clone II-4CII) were purchased from MP Biomedicals, Ohio, USA.…”

Section: Methodsmentioning

confidence: 99%

Topographical variation in the distributions of versican, aggrecan and perlecan in the foetal human spine reflects their diverse functional roles in spinal development

Smith

Whitelock

Iozzo

et al. 2009

Histochem Cell Biol

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We evaluated the immunohistochemical distribution of three major proteoglycans of cartilage, i.e., aggrecan, versican and perlecan vis-a-vis collagens I and II in the developing human spine of first-trimester foetuses. Aggrecan and perlecan were prominently immunolocalised in the cartilaginous vertebral body rudiments and to a lesser extent within the foetal intervertebral disc. In contrast, versican was only expressed in the developing intervertebral disc interspace. Using domain-specific monoclonal antibodies against the various modules of versican, we discovered the V0 isoform as the predominant form present. Versican immunolocalisations conducted with antibodies directed to epitopes in its N and C termini and GAG-alpha and GAG-beta core protein domains provided evidence that versican in the nucleus pulposus was either synthesised devoid of a G3 domain or this domain was proteolytically removed in situ. The V0 versican isoform was localised with prominent fibrillar components in the annular lamellae of the outer annulus fibrosus. Perlecan was a notable pericellular proteoglycan in the annulus fibrosus and nucleus pulposus but poorly immunolocalised in the marginal tissues of the developing intervertebral disc, apparently delineating the intervertebral disc-vertebral body interface region destined to become the cartilaginous endplate in the mature intervertebral disc. The distribution of collagens I and II in the foetal spine was mutually exclusive with type I present in the outer annulus fibrosus, marginal tissues around the vertebral body rudiment and throughout the developing intervertebral disc, and type II prominent in the vertebral rudiment, absent in the outer annulus fibrosus and diffusely distributed in the inner annulus fibrosus and nucleus pulposus. Collectively, our findings suggest the existence of an intricate and finely balanced interplay between various proteoglycans and collagens and the spinal cell populations which synthesise and assemble these components during spinal development.

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“…Changes in versican expression and distribution during embryonic development have also been reported in the CNS, where the V1 and V0 isoforms predominate during embryonic development and decrease rapidly at birth (Landolt et al 1995;Milev et al 1998;Schmalfeldt et al 1998;Horii-Hayashi et al 2008). Less is known about versican expression during lung development.…”

Section: Research-article2015mentioning

confidence: 98%

“…The structure of versican is characterized by an approximately 550-kDa core protein consisting of an amino-terminal (G1) hyaluronan binding domain, a carboxy-terminal (G3) domain, and two central chondroitin sulfate glycosaminoglycan attachment domains, the α-GAG and β-GAG domains (Zimmermann and Ruoslahti 1989;Zako et al 1995;Horii-Hayashi et al 2008;Hatano et al 2012). Versican has four different isoforms that differ in the central GAG attachment domain: V0 (contains both α and β GAG domains), V1 (contains only the β domain), V2 (contains only the α domain) and V3 (devoid of both GAG domains) (Zako et al 1995;Gu et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Correlation of Versican Expression, Accumulation, and Degradation during Embryonic Development by Quantitative Immunohistochemistry

Snyder

Washington

Birkland

et al. 2015

J Histochem Cytochem.

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SummaryVersican, a chondroitin sulfate proteoglycan, is important in embryonic development, and disruption of the versican gene is embryonically lethal in the mouse. Although several studies show that versican is increased in various organs during development, a focused quantitative study on versican expression and distribution during lung and central nervous system development in the mouse has not previously been performed. We tracked changes in versican (Vcan) gene expression and in the accumulation and degradation of versican. Vcan expression and quantitative immunohistochemistry performed from embryonic day (E) 11.5 to E15.5 showed peak Vcan expression at E13.5 in the lungs and brain. Quantitative mRNA analysis and versican immunohistochemistry showed differences in the expression of the versican isoforms in the embryonic lung and head. The expression of Vcan mRNA and accumulation of versican in tissues was complementary. Immunohistochemistry demonstrated co-localization of versican accumulation and degradation, suggesting distinct roles of versican deposition and degradation in embryogenesis. Very little versican mRNA or protein was found in the lungs of 12-to 16-week-old mice but versican accumulation was significantly increased in mice with Pseudomonas aeruginosa lung infection. These data suggest that versican plays an important role in fundamental, overlapping cellular processes in lung development and infection. (J Histochem Cytochem 63:952-967, 2015)

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Localization of chondroitin sulfate proteoglycan versican in adult brain with special reference to large projection neurons

Cited by 18 publications

References 34 publications

Alterations in sulfated chondroitin glycosaminoglycans following controlled cortical impact injury in mice

Alterations in sulfated chondroitin glycosaminoglycans following controlled cortical impact injury in mice

Topographical variation in the distributions of versican, aggrecan and perlecan in the foetal human spine reflects their diverse functional roles in spinal development

Correlation of Versican Expression, Accumulation, and Degradation during Embryonic Development by Quantitative Immunohistochemistry

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