The J1 glycoprotein—a novel nervous system cell adhesion molecule of the L2/HNK-1 family

Kruse, Jan; Keilhauer, Gerhard; Faissner, Andréas; Timpl, Rupert; Schachner, Melitta

doi:10.1038/316146a0

Cited by 570 publications

(387 citation statements)

References 15 publications

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“…To date three members of the family have been identified in mammals: tenascin-C (TN-C), tenascin-R (TN-R), and tenascin-X (TN-X). TN-C, variably identified as myotendinous antigen (Chiquet and Fambrough, 1984), GMEM (Bourdon et al, 1985), cytotactin (Grumet et al, 1985), J1 (Kruse et al, 1985), hexabrachion (Erickson and Iglesias, 1984), or simply tenascin, is the prototype of this gene family. TN-C has widespread developmental expression and a variety of postulated morphogenetic functions (Chiquet-Ehrismann et al, 1986;Ruegg et al, 1989;Crossin and Hoffman, 1991;Tan et al, 1991;Julian et al, 1994;Young et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

Embryonic expression of tenascin‐X suggests a role in limb, muscle, and heart development

Burch

Bedolli

McDonough

et al. 1995

Developmental Dynamics

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Tenascin-X (TN-X) is the newest member of the tenascin family of extracellular matrix proteins and it is highly expressed in muscular tissues during development. To gain insight into the possible functions of TN-X during development, we evaluated its expression in the rat embryo. Using an 800 bp cDNA encoding the fibrinogen-like domain of TN-X, we show that TN-X expression begins in migrating cells of the epicardium in the El2 heart. The epicardium provides progenitors of fibrous and vascular tissue to the developing heart. After the epicardium is complete, TN-X is expressed in the sub-epicardial space in association with developing blood vessels, and later by non-myocytes dispersed through the myocardial wall. A similar pattern of TN-X expression, first in connective tissue surrounding muscle, and then by a subset of cells within muscle, was seen in para-axial, body wall, craniofacial, and appendicular muscle. This pattern suggests a role in connective tissue cell migration and late muscle morphogenesis. TN-X is also highly expressed in the interdigital space at El5 and surrounding developing tendons, suggesting an additional role in cell fate determination. Although the pattern of TN-X expression is distinct from that of tenascin C, they are frequently expressed in close proximity. Indirect genetic evidence in humans suggests an essential function for TN-X, and the pattern of TN-X expression in heart, skeletal muscle, and limb is consistent with this hypothesis.

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Section: Introductionmentioning

confidence: 99%

Embryonic expression of tenascin‐X suggests a role in limb, muscle, and heart development

Burch

Bedolli

McDonough

et al. 1995

Developmental Dynamics

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“…The HNK-1 epitope has been shown to be present in various other glycoproteins, many of which are known to be involved in adhesive phenomena among neural cells. Among these are the neural cell adhesion molecules N-CAM (Kruse et al 1984), cytotactin (Grumet et al 1985), L1, L2, and Jl (Rathjen and Schachner 1984;Kruse et al 1985), and the myelinassociated glycoprotein (Poltorak et al 1987). In fish, the epitope has been shown to be present in a group of glycoproteins, called ependymins, that are secreted into the cerebrospinal fluid of goldfish during learning (Shashoua et al 1986) and in a subset of acetylcholinesterase molecules present in the electric organ of Electrophorus and Torpedo spp.…”

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confidence: 99%

Characterization of a monoclonal antibody directed against a sulphoglycolipid that is evolutionarily conserved and developmentally regulated in rat brain

1989

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Summary. Monoclonal antibodies (MABs) have been raised against acidic glycolipids extracted from the electric organ of Torpedo marmorata. One of these, designated L9, appears to recognize acidic glycolipids in adult T. marmorata electric organ, electromotor nerves and brain, adult rat sciatic nerve, and in embryonic and neonatal rat brain, starting at embryonic day (ED) 15 and disappearing by the 20th day of post-natal life. The epitope is present in growth cones isolated from 4-day-old rats; its proportion relative to total gangliosides is, however, no higher than that found in whole neonatal brain membranes. Desialidation of the acidic glycolipid fraction modifies neither the immunoreactivity nor the Rv value following thin-layer chromatography (TLC) of the antigen; it is concluded that the antigen is not a ganglioside. The MAB, HNK-I, recognizes the L9 antigen. Both HNK-1 and L9 recognize a sulphoglycolipid of the same Rv in TLC. The function of the L9 antigen is not known but its evolutionary conservation, presence in growth cones and its developmental regulation in the mammalian central nervous system indicate that it plays an important role in nervous system maturation.

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“…Another common trait shared by N-CAM, LI, and MAG is the presence of the L2/HNK-1 carbohydrate determinant . This sugar moiety is also found on cell adhesion molecules from nervous tissue not belonging to the Ig superfamily and may directly participate in cell-cell or cell-matrix adhesion (Kruse et al, 1985;Keilhauer et al, 1985;Riopelle et al, 1986;Hoffman and Edelman, 1987;Kiinemund et al, 1988).…”

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confidence: 99%

The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin.

Gennarini

Cibelli

Rougon

et al. 1989

The Journal of Cell Biology

259

166

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Abstract. Several members of the Ig superfamily are expressed on neural cells where they participate in surface interactions between cell bodies and processes. Their Ig domains are more closely related to each other than to Ig variable and constant domains and have been grouped into the C2 set. Here, we report the cloning and characterization of another member of this group, the mouse neuronal cell surface antigen F3. The F3 eDNA sequence contains an open reading frame that could encode a 1,020-amino acid protein consisting of a signal sequence, six Ig-like domains of the C2 type, a long premembrane region containing two segments that exhibit sequence similarity to fibronectin type III repeats and a moderately hydrophobic COOH-terminal sequence. The protein does not contain a typical transmembrane segment but appears to be attached to the membrane by a phosphatidylinositol anchor. Antibodies against the F3 protein recognize a prominent 135-kD protein in mouse brain. In fetal brain cultures, they stain the neuronal cell surface and, in cultures maintained in chemically defined medium, most prominently neurites and neurite bundles. The mouse f3 gene maps to band F of chromosome 15. The gene transcripts detected in the brain by F3 cDNA probes are developmentally regulated, the highest amounts being expressed between 1 and 2 wk after birth.The F3 nucleotide and deduced amino acid sequence show striking similarity to the recently published sequence of the chicken neuronal cell surface protein contactin. However, there are important differences between the two molecules. In contrast to F3, contactin has a transmembrane and a cytoplasmic domain. Whereas contactin is insoluble in nonionic detergent and is tightly associated with the cytoskeleton, about equal amounts of F3 distribute between buffer-soluble, nonionic detergent-soluble, and detergent-insoluble fractions. Among other neural cell surface proteins, F3 most resembles the neuronal cell adhesion protein L1, with 25 % amino acid identity between their extracellular domains. Based on its structural similarity with known cell adhesion proteins of nervous tissue and with L1 in particular, we propose that F3 mediates cell surface interactions during nervous system development.

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The J1 glycoprotein—a novel nervous system cell adhesion molecule of the L2/HNK-1 family

Cited by 570 publications

References 15 publications

Embryonic expression of tenascin‐X suggests a role in limb, muscle, and heart development

Embryonic expression of tenascin‐X suggests a role in limb, muscle, and heart development

Characterization of a monoclonal antibody directed against a sulphoglycolipid that is evolutionarily conserved and developmentally regulated in rat brain

The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin.

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