The L2/HNK-1 carbohydrate of neural cell adhesion molecules is involved in cell interactions.

Künemund, Volker Harald; Jungalwala, Firoze B.; Fischer, G.; Chou, Denise K. H.; Keilhauer, Gerhard; Schachner, Melitta

doi:10.1083/jcb.106.1.213

Cited by 363 publications

(168 citation statements)

References 46 publications

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“…The immunoaffinity-isolated AN2 antigen from brain (as well as from Oli-neu; data not shown) expresses the L2/HNK-1 carbohydrate epitope that is expressed by subpopulations of many cell adhesion molecules, including N-CAM, MAG, L1, and Tenascin-R, and has been shown to play a role in adhesion (Krüse et al, 1984;Keilhauer et al, 1985;Künemund et al, 1988). This observation supports a putative function of AN2 as an adhesion molecule.…”

Section: Carbohydrate Residues Including Glycosaminoglycan Chains Maysupporting

confidence: 63%

Cell-Surface Glycoprotein of Oligodendrocyte Progenitors Involved in Migration

et al. 1999

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Myelination by oligodendrocytes in the CNS involves the migration to and recognition and ensheathment of axons. These distinct developmental phases of myelination are assumed to involve the interplay of a precisely regulated set of cell adhesion molecules expressed by both neurons and glial cells. These molecules remain largely unelucidated. In this paper we have identified a large (330 kDa) glycoprotein expressed by murine oligodendrocyte progenitor cells in vitro and in vivo that is downregulated as oligodendrocytes mature. Antigen-positive oligodendrocyte progenitor cells purified by panning develop into myelin-associated glycoprotein-positive oligodendrocytes and also adhere to cultured neurons. Polyclonal antibodies directed against the protein reduce the migration of oligodendrocyte progenitor cells. The observations suggest that the AN2 antigen may play a role in early stages of myelination.

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Section: Carbohydrate Residues Including Glycosaminoglycan Chains Maysupporting

confidence: 63%

Cell-Surface Glycoprotein of Oligodendrocyte Progenitors Involved in Migration

et al. 1999

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“…The developmental pattern of BEN expression and the fact that it bears the HNK-1 epitope, which is thought to be implicated in adhesion phenomena in the nervous system (18), led us to speculate that BEN could be implicated in cell adhesion events such as axonal fasciculation or cell aggregation. We examined the distribution of BEN protein on the cell surface of E13 inferior olivary nucleus neurons cultured for 24 h by using confocal microscopy.…”

Section: Resultsmentioning

confidence: 99%

BEN, a surface glycoprotein of the immunoglobulin superfamily, is expressed in a variety of developing systems.

Pourquié

Corbel

Caer

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

111

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We have previously identified a 95-to 100-kDa cell surface glycoprotein, which we named BEN (for bursal epithelium and neurons), that is widely expressed during chicken embryonic development. In the central nervous system, it is restricted to subsets of neurons including the motoneurons and the inferior olivary nucleus neurons (which provide the cerebellum with the climbing fibers) where its expression occurs during the phase of axonogenesis and synaptogenesis. In the present work, we show that BEN expression extends to a variety of tissues originating from the three embryonic germ layers. We have found that BEN immunopurifled from neural, epithelial, and hemopoietic tissues is differently glycosylated and may or may not carry the HNK-1 epitope. We then cloned a full-length cDNA encoding this

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“…Roles for sulfatides and SGGLs in neural cell interactions have been proposed in earlier studies. For example, it has been suggested that SGGLs and sulfatides are involved in the adhesion of dissociated cerebellar cells and outgrowth of neurites and astrocytic processes (54). SGGLs have also been shown to have effects on Schwann cell adhesion (28,55).…”

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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The L2/HNK-1 carbohydrate of neural cell adhesion molecules is involved in cell interactions.

Cited by 363 publications

References 46 publications

Cell-Surface Glycoprotein of Oligodendrocyte Progenitors Involved in Migration

Cell-Surface Glycoprotein of Oligodendrocyte Progenitors Involved in Migration

BEN, a surface glycoprotein of the immunoglobulin superfamily, is expressed in a variety of developing systems.

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

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