Chondroitin sulfate proteoglycans in the developing central nervous system. II. Immunocytochemical localization of neurocan and phosphacan

Meyer-Puttlitz, Birgit; Junker, Ernst; Margolis, Richard U.; Margolis, Renée K.

doi:10.1002/(sici)1096-9861(19960226)366:1<44::aid-cne4>3.0.co;2-k

Cited by 143 publications

(105 citation statements)

References 23 publications

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“…SGGLs are particularly abundant in embryonic cerebral cortex and adult cerebellum (31). Neurocan and brevican are highly expressed in embryonic brain and adult cerebellum, respectively (21,47). Sulfatides are a major component of myelin (48) and are expressed in oligodendrocytes and Schwann cells in culture (49,50).…”

Section: Discussionmentioning

confidence: 99%

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

Miura

Aspberg

Ethell

et al. 1999

Journal of Biological Chemistry

107

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The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784 -7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides. Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo.The lecticans are a family of chondroitin sulfate proteoglycans (CSPGs) 1 characterized by the presence of a C-type lectin domain in their core proteins (1, 2). The C-terminal globular domains of lecticans, or "proteoglycan lectin domain" (PLD), consist of one or two epidermal growth factor (EGF)-like domains, a C-type lectin domain, and a complement regulatory protein (CRP) domain. This arrangement of domains is similar to that of selectins, suggesting that lecticans are also involved in the recognition of carbohydrate ligands.Lecticans are the most abundantly expressed family of proteoglycans in the nervous system. The lectican family includes aggrecan (3), versican (4), neurocan (5), and brevican (6), all of which are expressed in the nervous system at certain stages of development (1, 7). Although aggrecan and versican were initially characterized as connective tissue proteoglycans, their expression in the nervous system has been demonstrated in a number of reports (8 -12). Brevican and neurocan are specifically expressed in the nervous system (6, 13-15). Structural similarities with selectins and the abundant expression in the nervous system suggest that lecticans play major roles in carbohydrate recognition in the nervous system.The identity of the ligand to PLDs has been a focus of our interest. We previously showed that the PLD of versican binds tenascin-R, an extracellular matrix (ECM) protein predominantly expressed in the nervous system (16). More recently, we demonstrated that the PLDs of all lecticans bind tenascin-R, and that brevican and tenascin-R indeed form a complex in adult rat brain e...

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Section: Discussionmentioning

confidence: 99%

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

Miura

Aspberg

Ethell

et al. 1999

Journal of Biological Chemistry

107

View full text Add to dashboard Cite

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“…3) (MeyerPuttlitz et al 1995;Milev et al 1998a). Preferential accumulations are the marginal zone and the subplate of the neocortex, parts of the hypothalamus, the amygdala and the developing hippocampus and dentate gyrus (Meyer-Puttlitz et al 1996;Miller et al 1995;Popp et al 2003). Early postnatally, neurocan and the versican isoforms V0 and V1 are also found in the presumptive white matter and in the internal granule cell layer of the cerebellum (Meyer-Puttlitz et al 1996;Popp et al 2003).…”

Section: Juvenile Matrix Typementioning

confidence: 99%

Extracellular matrix of the central nervous system: from neglect to challenge

Zimmermann

Dours-Zimmermann

2008

Histochem Cell Biol

406

340

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(aggrecan, versican, neurocan, brevican, phosphacan), link proteins and tenascins (Tn-R, Tn-C) can regulate cellular migration and axonal growth and thus, actively participate in the development and maturation of the nervous system, has in recent years gained rapidly expanding experimental support. The swift assembly and remodeling of these matrices have been associated with axonal guidance functions in the periphery and with the structural stabilization of myelinated fiber tracts and synaptic contacts in the maturating central nervous system. Particular interest has been focused on the putative role of chondroitin sulfate proteoglycans in suppressing central nervous system regeneration after lesions. The axon growth inhibitory properties of several of these chondroitin sulfate proteoglycans in vitro, and the partial recovery of structural plasticity in lesioned animals treated with chondroitin sulfate degrading enzymes in vivo have significantly contributed to the increased awareness of this long time neglected structure. Abstract The basic concept, that specialized extracellular matrices rich in hyaluronan, chondroitin sulfate proteoglycans (aggrecan, versican, neurocan, brevican, phosphacan), link proteins and tenascins (Tn-R, Tn-C) can regulate cellular migration and axonal growth and thus, actively participate in the development and maturation of the nervous system, has in recent years gained rapidly expanding experimental support. The swift assembly and remodeling of these matrices have been associated with axonal guidance functions in the periphery and with the structural stabilization of myelinated Wber tracts and synaptic contacts in the maturating central nervous system. Particular interest has been focused on the putative role of chondroitin sulfate proteoglycans in suppressing central nervous system regeneration after lesions. The axon growth inhibitory properties of several of these chondroitin sulfate proteoglycans in vitro, and the partial recovery of structural plasticity in lesioned animals treated with chondroitin sulfate degrading enzymes in vivo have signiWcantly contributed to the increased awareness of this long time neglected structure.

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“…In early postnatal and adult cerebellum, neurocan and phosphacan show immunoreactivities that follow different developmental time courses. Neurocan is seen in the prospective white matter and in granule cells, Purkinje cells, and molecular layer, whereas phosphacan is associated with Bergmann glial fibers in the molecular layer and their cell bodies below the Purkinje cells (44). Besides the chondroitin sulfate proteoglycans, tenascins also bind heparin through their fifth fibronectin type III domain, although it is not clear if this in vitro binding capacity is also valid for binding to heparan sulfates that would be found in vivo, and if this is somehow related to neuronal migration (45).…”

Section: Active Signaling Molecules: Reelin Tenascin and Netrinmentioning

confidence: 99%

The extracellular matrix provides directional cues for neuronal migration during cerebellar development

Porcionatto

2006

Braz J Med Biol Res

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Normal central nervous system development relies on accurate intrinsic cellular programs as well as on extrinsic informative cues provided by extracellular molecules. Migration of neuronal progenitors from defined proliferative zones to their final location is a key event during embryonic and postnatal development. Extracellular matrix components play important roles in these processes, and interactions between neurons and extracellular matrix are fundamental for the normal development of the central nervous system. Guidance cues are provided by extracellular factors that orient neuronal migration. During cerebellar development, the extracellular matrix molecules laminin and fibronectin give support to neuronal precursor migration, while other molecules such as reelin, tenascin, and netrin orient their migration. Reelin and tenascin are extracellular matrix components that attract or repel neuronal precursors and axons during development through interaction with membrane receptors, and netrin associates with laminin and heparan sulfate proteoglycans, and binds to the extracellular matrix receptor integrins present on the neuronal surface. Altogether, the dynamic changes in the composition and distribution of extracellular matrix components provide external cues that direct neurons leaving their birthplaces to reach their correct final location. Understanding the molecular mechanisms that orient neurons to reach precisely their final location during development is fundamental to understand how neuronal misplacement leads to neurological diseases and eventually to find ways to treat them.

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Chondroitin sulfate proteoglycans in the developing central nervous system. II. Immunocytochemical localization of neurocan and phosphacan

Cited by 143 publications

References 23 publications

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion

Extracellular matrix of the central nervous system: from neglect to challenge

The extracellular matrix provides directional cues for neuronal migration during cerebellar development

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