J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion.

Pesheva, Penka; Spieß, Eberhard; Schachner, Melitta

doi:10.1083/jcb.109.4.1765

Cited by 258 publications

(328 citation statements)

References 49 publications

Supporting

Mentioning

316

Contrasting

Order By: Relevance

“…The HNK-1 monoclonal antibody was purchased from Becton Dickinson (Bedford, MA). Mouse monoclonal anti-tenascin-R antibody (clone 596) (24) and monoclonal anti-sulfatide antibody were gifts from Drs. Melitta Schachner (University of Hamburg, Hamburg, Germany) and Yoshio Hirabayashi (RIKEN, Wako, Japan), respectively.…”

Section: Methodsmentioning

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

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...

show abstract

Section: Methodsmentioning

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

show abstract

“…This exchange transforms the relatively loose embryonic and early postnatal ECM to a signiWcantly Wrmer meshwork, which is subsequently maintained throughout adulthood. The large majority of the early matrix components are along the conversion substituted by a diVerent, but homologous set of ECM proteins that include versican V2, aggrecan, brevican, phosphacan, tenascin-R and the brain link proteins HAPLN2/Bral1 and HAPLN4/Bral2 (Bekku et al 2003;Hirakawa et al 2000;Meyer-Puttlitz et al 1995;Milev et al 1998b;Pesheva et al 1989). …”

Section: Mature Matrix Typementioning

confidence: 99%

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

Zimmermann

Dours-Zimmermann

2008

Histochem Cell Biol

406

340

View full text Add to dashboard Cite

(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.

show abstract

“…A monoclonal antibody against the HNK-1 carbohydrate (mab 412), a polyclonal antibody against mouse EHS sarcoma laminin (pab LN) and an immunoaffinity-purified polyclonal antibody against the neural cell adhesion molecule NCAM from mouse brain (pab NCAM) were obtained and purified according to Kruse et al (1984), Pesheva et al (1989), and Martini and Schachner (1986), respectively. Fab fragments of mab 412 and pab NCAM were prepared by proteolytic digestion with papain (Porter, 1959).…”

Section: Antibodiesmentioning

confidence: 99%

Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion

Hall

Vorherr

Schachner³

1995

Glycobiology

View full text Add to dashboard Cite

The N-linked HNK-1 carbohydrate expressed by several recognition molecules mediates the adhesion of early postnatal cerebellar neurons to the G2 domain of the terminal globular domain of the laminin al chain (H.Hall et al., submitted). To define this binding site more precisely, G2-derived synthetic peptides were used for binding and competition studies. Peptide 5-G2, comprising the amino add residues 3431-3451 of G2, inhibited the interaction between the HNK-1-carrying glycolipid and laminin in a concentrationdependent and saturable manner. Peptides which overlap only partially with this sequence interfered less. Peptides comprising other amino acid sequences from G2, and peptides derived from Gl and G3 or a scrambled version of peptide 5-G2, did not show significant effects. Direct binding of peptide 5-G2 to the HNK-1 glycolipid was also demonstrated. Furthermore, peptide 5-G2 interfered in a concentration-dependent and saturable manner with the adhesion of early postnatal cerebellar neurons to laminin. These observations indicate that amino acid residues 3431-3451 of the laminin G2 domain are involved in HNK-1 carbohydratemediated cell adhesion.

show abstract

J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion.

Cited by 258 publications

References 49 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

Characterization of a 21 amino acid peptide sequence of the laminin G2 domain that is involved in HNK-1 carbohydrate binding and cell adhesion

Contact Info

Product

Resources

About