Tissue specific O-linked glycosylation of the neural cell adhesion molecule (N-CAM)

Development ◽  
1989 ◽  
Vol 105 (4) ◽  
pp. 803-811
Author(s):  
F.S. Walsh ◽  
R.B. Parekh ◽  
S.E. Moore ◽  
G. Dickson ◽  
C.H. Barton ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Alternative Splicing ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Lectin Binding ◽  
Peanut Lectin ◽  
3T3 Fibroblasts ◽  
Extracellular Region ◽  
Neural Cell Adhesion ◽  
A Site

We have shown previously that the predominant N-CAM isoform in skeletal muscle myotubes contains as a result of alternative splicing a novel domain (MSD1) in its extracellular region. Here we show that this region represents a site for O-linked carbohydrate attachment. The lipid tailed N-CAM in myotubes was found to bind peanut lectin while the transmembrane isoform from myoblasts lacking MSD1 did not. In addition, N-CAM from a variety of neural sources failed to bind the lectin. Analysis of 3T3 fibroblasts transfected with various N-CAM cDNAs, showed that peanut lectin binding was correlated specifically with the expression of the MSD1 region. The oligosaccharides isolated from a purified preparation of myotube N-CAM were shown to contain an O-linked oligosaccharide whose core structure was a sialylated version of Gal beta 1—3GalNac which is the structure recognized specifically by peanut lectin. These data provide the first evidence for the expression of O-linked carbohydrate on any N-CAM isoform and more specifically target this oligosaccharide to the MSD1 region of myotube N-CAM.

Alternative splicing of neural-cell-adhesion molecule mRNA in human small-cell lung-cancer cell line H69

1992 ◽  
Vol 51 (2) ◽  
pp. 238-243 ◽  
Author(s):  
C. E. C. Moolenaar ◽  
Cynthia Pieneman ◽  
Frank S. Walsh ◽  
Wolter J. Mooi ◽  
Rob J. A. M. Michalides
Keyword(s):  
Lung Cancer ◽  
Alternative Splicing ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Cancer Cell Line ◽  
Lung Cancer Cell Line ◽  
Small Cell ◽  
Lung Cancer Cell ◽  
Small Cell Lung ◽  
Neural Cell Adhesion

scholarly journals At least 27 alternatively spliced forms of the neural cell adhesion molecule mRNA are expressed during rat heart development.

1991 ◽  
Vol 11 (3) ◽  
pp. 1654-1661 ◽  
Author(s):  
A A Reyes ◽  
S J Small ◽  
R Akeson
Keyword(s):  
Cell Adhesion ◽  
Alternative Splicing ◽  
Adhesion Molecule ◽  
Heart Development ◽  
Rat Heart ◽  
Cell Adhesion Molecule ◽  
Neural Cell Adhesion Molecule ◽  
Neural Cell ◽  
Neural Cell Adhesion ◽  
Alternatively Spliced

The major membrane-associated or transmembrane isoforms of the neural cell adhesion molecule (NCAM) are generated by alternative splicing at the 3' end of the mRNA. Further diversity in NCAM structure is observed in the extracellular region of the polypeptide, where the insertion of additional amino acid residues can result from alternative splicing events occurring at the exon 7-exon 8 and exon 12-exon 13 junctions. Here we report the characterization of tissue-specific patterns of alternative splicing at the exon 12-exon 13 junction by using the polymerase chain reaction. Nine alternatively spliced sequences in rat heart between exon 12 and exon 13 were identified. Each sequence consisted of different combinations of the three small exons (15, 48, and 42 bp in length) and the AAG triplet that make up MSD1, the 108-bp muscle-specific sequence found in human skeletal muscle NCAM (G. Dickson, H.J. Gower, C. H. Barton, H. M. Prentice, V. L. Elsom, S. E. Moore, R. D. Cox, C. Quinn, W. Putt, and F. S. Walsh, Cell 50:1119-1130, 1987). Although the rat equivalent of MSD1 (designated 15+ 48+ 42+ 3+) was detected in all ages of heart examined, it was only one of four or five major splice combinations at any given age. The only alternatively spliced sequence found in the exon 7-exon 8 junction of heart NCAM mRNA was the 30-bp variable alternatively spliced exon previously identified in rat brain. Twenty-seven NCAM forms with distinct sequences were found by analysis of individual NCAM transcripts from postnatal day 1 heart tissue for alternative splicing at the exon 7-exon 8 junction, the exon 12-exon 13 junction and the 3' end. Several combinations of splicing patterns in these three different regions of the gene appeared to be preferentially expressed. The observation that the expression of alternatively spliced forms of NCAM is developmentally regulated suggests a role for NCAM diversity in cardiac development.

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