Intercellular adhesion mediated by human muscle neural cell adhesion molecule: effects of alternative exon use.

Pizzey, John; Rowett, L H; Barton, Chris; Dickson, George; Walsh, Frank S.

doi:10.1083/jcb.109.6.3465

Cited by 35 publications

(23 citation statements)

References 60 publications

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“…In the system of muscle differentiation, the NCAM plays a role in mediating the homophilic interaction of myoblasts, and a substantial part of NCAM is present as the GPI-linked isoform in this case (18). Furthermore, transfection experiments showed participation of the NCAMin cell-cell aggregation (25), neuron-glia adhesion (8) and promotion of myogenesis (6).…”

mentioning

confidence: 99%

Transitional Expression of Neural Cell Adhesion Molecule Isoforms During Chicken Embryonic Myogenesis.

Yoshimi

Mimura

Aimoto

et al. 1993

Cell Struct. Funct.

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Keywords: neural cell adhesion molecule/muscle-specific domain/myogenesis/antipeptide antibody ABSTRUCT. The neural cell adhesion molecule, NCAM, is known to be expressed in chicken muscle as at least three principal molecular forms (molecular masses of 155 kDa, 145 kDa, and 120 kDa). They are generated from a single gene by alternative splicing. To distinguish these molecular species and to investigate their expressions in muscle differentiation during chicken embryonic development, we prepared antipeptide antibodies against three different domains of the NCAM.The antibody named MSD<+ > was designed to detect musclespecific domain (MSD)which was inserted into a muscle-specific NCAM by alternative splicing. The locus encompassing the MSDinsertion site was detected with the antibody named MSD<->, and cytoplasmic sites near the transmembrane region were detected with the antibody named CYT.Immunoblot analysis utilizing the peptide antibodies prepared here revealed that, of three NCAMs, two isoforms, 155 kDa and 120 kDa, were recognized with the antibody MSD<+ > and the same 155-kDa and the other 145-kDa molecule were recognized with the antibody CYT. The antibody MSD<-> was capable of detecting all three isoforms of the NCAM.Expression of the 120-kDa form with MSDbut lacking a cytoplasmic tail increased but that of the 145-kDa form with cytoplasmic tail but lacking MSDdeclined during embryonic day 5 to day 18. The 155-kDa form NCAMwith both MSDand cytoplasmic tail was expressed specifically and transiently during embryonic day ll to day 14 in chick muscle; this period coincides with the period of extensive myotube formation. Thus, this largest isotype seems to play an important role in muscle differentiation.

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mentioning

confidence: 99%

Transitional Expression of Neural Cell Adhesion Molecule Isoforms During Chicken Embryonic Myogenesis.

Yoshimi

Mimura

Aimoto

et al. 1993

Cell Struct. Funct.

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“…None of the transfected cell lines aggregated as well as WC5 cells cultured at the non-permissive temperature, but this was not the result of insufficient N-CAM expression because the levels of chicken N-CAM in the transfected cells were similar to the level of rat N-CAM in WC5 cells at the non-permissive temperature. The aggregation values we obtained with transfected WC5 cells are similar to or greater than the aggregation levels seen when N-CAM was transfected into fibroblast [39,40] or neuronal cell lines (Akeson, personal communication). In this connection, it is significant that fibroblasts transfected with N-CAM [40] show levels of cell-cell adhesion that are significantly lower than those seen here, yet the expressed N-CAM has dramatic effects on PC12 cell neurite extension and differentiation [41][42][43].…”

Section: Discussionmentioning

confidence: 56%

“…The aggregation values we obtained with transfected WC5 cells are similar to or greater than the aggregation levels seen when N-CAM was transfected into fibroblast [39,40] or neuronal cell lines (Akeson, personal communication). In this connection, it is significant that fibroblasts transfected with N-CAM [40] show levels of cell-cell adhesion that are significantly lower than those seen here, yet the expressed N-CAM has dramatic effects on PC12 cell neurite extension and differentiation [41][42][43]. These considerations suggest that the levels of N-CAM expression and function in the transfected WC5 cells were sufficient to produce effects on invasion.…”

Section: Discussionmentioning

confidence: 56%

Increasing N-CAM-mediated cell-cell adhesion does not reduce invasion of RSV-transformed WC5 rat cerebellar cells

et al. 1993

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The WC5 rat cerebellar cell line, infected with a Rous sarcoma virus (RSV) that is temperature-sensitive for pp60v-src transformation, expresses high levels of the neural cell adhesion molecule, N-CAM, when grown at the non-permissive temperature for pp60v-src activity. At the permissive temperature, N-CAM expression is 4- to 10-fold reduced and the cells aggregate poorly. To evaluate the effects of variations in N-CAM expression, we compared the invasive ability of transformed WC5 cells that express low levels of N-CAM with transformed cells in which N-CAM-mediated adhesion was restored. WC5 cells were transfected with expression vectors containing cDNAs encoding the 120 or 180 kDa forms of chicken N-CAM linked to constitutive promoters. Several permanently transfected lines that expressed chicken N-CAM at the cell surface were isolated. These cell lines showed enhanced aggregation at the permissive temperature relative to untransfected WC5 cells or cells transfected with control constructs. By comparing the ability of control and transfected WC5 cells to invade reconstituted extracellular matrix, we tested the effect of variations in N-CAM-mediated adhesion on invasion. Clones that expressed high levels of N-CAM showed invasion rates that were similar to control cells, indicating that increasing N-CAM-mediated adhesion does not inhibit the invasiveness of RSV-transformed WC5 cells.

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“…rocyte acetylcholine esterase and bovine cerebral cortex 5'-nucleotidase have identical activities (Barton et al, 1985;Vogel et al, 1992), and transmembrane and GPI-anchored forms of N-CAM mediate cell adhesion of transfected mouse fibroblasts in a similar fashion (Pizzey et al, 1989). It appears that GPI anchorage does, in most cases, not significantly modulate the properties of the anchored protein.…”

Section: Discussionmentioning

confidence: 83%

Glucose induces lipolytic cleavage of a glycolipidic plasma membrane anchor in yeast

Müller

Bandlow

1993

The Journal of Cell Biology

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Abstract. In the yeast Saccharomyces cerevisiae an amphiphilic cAMP-binding protein has been found recently to be anchored to plasma membranes by virtue of a glycolipid structure Bandlow, 1991a, 1992). The cAMP-binding parameters of this protein are affected by the lipolytic removal of the glycosylphosphatidylinositol (GPI) membrane anchor by exogenous (G)PI-specific phospholipases C or D (PLC or PLD) (Miiller and Bandlow, 1993) suggesting a regulatory role of glycolipidic membrane anchorage. Here we report that transfer of yeast cells from lactate to glucose medium results in the conversion of the amphiphilic form of the cAMP receptor protein into a hydrophilic version accompanied by the rapid loss of fatty acids from the GPI anchor of the [14C]palmitic acid-labeled protein. Analysis of the cleavage site identifies [~4C]inositol phosphate as the major product after treatment of the soluble, [t4C]inositol-labeled protein with nitrous acid which destroys the glucosamine constituent of the anchor. Together with the observed cross-reactivity of the hydrophilic fragment with antibodies directed against the cross-reacting determinant of soluble trypanosomal variable surface glycoproteins (i.e., myo-inositol-l,2-cyclic phosphate) this demonstrates that, in membrane release, the initial cleavage event is catalyzed by an intrinsic GPI-PLC activated upon transfer of cells to glucose medium. Release from the plasma membrane in soluble form requires, in addition, the presence of high salt or or-methyl mannopyranoside, or the removal of the carbohydrate moieties, because otherwise the protein remains associated with the membrane presumably at least in part via its N-glycosidic carbohydrate side chains. The data point to the possibility that cleavage of the anchor could play a role in the transfer of the signal for the nutritional situation to the interior of the cell.

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Intercellular adhesion mediated by human muscle neural cell adhesion molecule: effects of alternative exon use.

Cited by 35 publications

References 60 publications

Transitional Expression of Neural Cell Adhesion Molecule Isoforms During Chicken Embryonic Myogenesis.

Transitional Expression of Neural Cell Adhesion Molecule Isoforms During Chicken Embryonic Myogenesis.

Increasing N-CAM-mediated cell-cell adhesion does not reduce invasion of RSV-transformed WC5 rat cerebellar cells

Glucose induces lipolytic cleavage of a glycolipidic plasma membrane anchor in yeast

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