Upregulated expression of N-syndecan, a transmembrane heparan sulfate proteoglycan, in differentiated neural stem cells

Inatani, Masaru; Haruta, Masatoshi; Honjo, Megumi; Oohira, Atsuhiko; Kido, Noriaki; Takahashi, Masayo; Honda, Yoshio; Tanihara, Hidenobu

doi:10.1016/s0006-8993(01)02856-6

Cited by 31 publications

(43 citation statements)

References 20 publications

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“…Members of the pan-retina cell-cell adhesion molecules group are expressed in many cell types in the retina to mediate nonspecific retinal cell adhesion. Examples of this group include the neural cell adhesion molecule (N-CAM) (Daniloff et al, 1986), L1 (Chung et al, 2004), P84 and its interacting partner Integrin Associated Protein (IAP) (Mi et al, 2000), N-cadherin (Malicki et al, 2003), Neuroligin (von Kriegstein and Schmitz, 2003), N-Syndecan (Inatani et al, 2002), and LAMP, an isoform of IgLON (Lodge et al, 2000). Members of the specific cell-cell adhesional molecules group display regional expression patterns in the retina and are likely involved in regional adhesion functions that are important for specific retinal layers.…”

Section: Introductionmentioning

confidence: 99%

Nok plays an essential role in maintaining the integrity of the outer nuclear layer in the zebrafish retina

Wei

Zou

Takechi

et al. 2006

Experimental Eye Research

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Proper visual function of the vertebrate retina requires the maintenance of the integrity of the retinal outer nuclear layer (ONL), which is often affected in many blinding human retinal diseases.While the structural integrity of the ONL has long been considered to be maintained primarily through the outer limiting membrane (OLM), we have little knowledge on the development and maintenance of the OLM itself. Here, by analyzing the adhering properties of photoreceptors in zebrafish N-cad and nok mutants, we demonstrated for the first time that the nok gene is essential for the establishment and/or maintenance of the OLM. In addition, our results imply the possibility that Nok, Crumbs, and their associated proteins may constitute a type of photoreceptor-photoreceptor junctional complex that has not been described before. Thus, our study provides novel insights into the mechanisms by which the integrity of the ONL is maintained in the vertebrate retina.

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Section: Introductionmentioning

confidence: 99%

Nok plays an essential role in maintaining the integrity of the outer nuclear layer in the zebrafish retina

Wei

Zou

Takechi

et al. 2006

Experimental Eye Research

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“…ADAMTS expression has been detected in the CNS [1], [17], [37] and is known to be altered in disease states [10], [22], [23]. 4 The chondroitin sulphate proteoglycans (CSPGs), aggrecan, brevican, neurocan, phosphacan, appican and versican are expressed in the brain [3], [12], [26], [28], [46] and are potential substrates for ADAMTSs. These CSPGs are important to brain structure through maintenance of the correct hydrodynamics and in their interactions with other ECM components.…”

Section: Introductionmentioning

confidence: 99%

“…They also contribute to disease processes and their synthesis is modulated by injury [14]. As a group, CSPGs are known to inhibit neurite outgrowth and axonal regeneration and promote neural cell death [2], [12], [15], [19], [39]. Therefore alterations in levels of CSPGs are relevant to neuronal survival and regeneration after an ischaemic event.…”

Section: Introductionmentioning

confidence: 99%

ADAMTS-1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes

et al. 2006

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ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) enzymes are a recently described group of metalloproteinases. The substrates degraded by ADAMTS-1, -4 and -5 suggests that they play a role in turnover of extracellular matrix in the central nervous system (CNS). ADAMTS-1 is also known to exhibit anti-angiogenic activity. Their main endogenous inhibitor is tissue inhibitor of metalloproteinases (TIMP)-3.The present study was designed to investigate ADAMTS-1, -4 and -5 and TIMP-3 expression after experimental cerebral ischaemia and to examine whether cytokines known to be up-regulated in stroke could alter their expression by astrocytes in vitro.Focal cerebral ischaemia was induced by transient middle cerebral artery occlusion in the rat using the filament method.Our results demonstrate a significant increase in expression of ADAMTS-1 and -4 in the occluded hemisphere but no significant change in TIMP-3. This was accompanied by an increase in mRNA levels for interleukin (IL)-1β, IL-1 receptor antagonist (IL1ra) and tumour necrosis factor (TNF). ADAMTS-4 mRNA and protein was upregulated by TNF in primary human astrocyte cultures. The increased ADAMTS-1 and -4 in experimental stroke, together with no change in TIMP-3, may promote ECM breakdown after stroke, enabling infiltration of inflammatory cells and contribute to brain injury. In vitro studies suggest that the in vivo modulation of ADAMTS-1 and -4 may be controlled in part by TNF.3

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“…It is expressed in axon and synapserich areas of the nervous system and was shown to be important for neurite formation (1,4). CALEB/NGC is a type I transmembrane protein, the extracellular part of which contains the following domains.…”

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confidence: 99%

CALEB/NGC Interacts with the Golgi-associated Protein PIST

Hassel

Schreff

Stübe

et al. 2003

Journal of Biological Chemistry

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CALEB/NGC is a neural member of the epidermal growth factor protein family expressed in axon and synapse-rich areas of the nervous system and shown to be important for neurite formation. It can bind to the extracellular matrix proteins tenascin-R and tenascin-C. Here we show that CALEB/NGC interacts with the Golgiassociated protein PIST. PIST was originally described as an interaction partner of the small GTPase TC10 and was then found to be Golgi-associated by binding to syntaxin-6 and to be important for the transport of frizzled proteins and the cystic fibrosis transmembrane conductance regulator to the plasma membrane. In addition, PIST was demonstrated to be involved in autophagy and linked to processes of neurodegeneration. CALEB/NGC interacts with PIST in the yeast two-hybrid system. This interaction can be confirmed by co-immunoprecipitations and co-localization studies. The juxtamembrane cytoplasmic peptide segment of CALEB/ NGC, highly conserved during evolution, mediates the binding to PIST. CALEB/NGC co-localizes with PIST in the Golgi apparatus of transfected COS7 cells and in Golgi-derived vesicles after brefeldin A or nocodazole treatment. Co-localization studies in primary hippocampal cells and analysis of Purkinje cells of colchicinetreated rats, serving as an in vivo model system to block microtubule-dependent transport processes, support the view that PIST is an interaction partner of CALEB/ NGC and implicate that this interaction may play a role in the intracellular transport of CALEB/NGC.

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Upregulated expression of N-syndecan, a transmembrane heparan sulfate proteoglycan, in differentiated neural stem cells

Cited by 31 publications

References 20 publications

Nok plays an essential role in maintaining the integrity of the outer nuclear layer in the zebrafish retina

Nok plays an essential role in maintaining the integrity of the outer nuclear layer in the zebrafish retina

ADAMTS-1 and -4 are up-regulated following transient middle cerebral artery occlusion in the rat and their expression is modulated by TNF in cultured astrocytes

CALEB/NGC Interacts with the Golgi-associated Protein PIST

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