Complete sequence and<i>in vitro</i>expression of a tissue-specific phosphatidylinositol-linked N-CAM isoform from skeletal muscle

Barton, Chris; Dickson, George; Gower, Hilary J.; Rowett, L H; Putt, Wendy; Elsom, V.E.; Moore, Stephen E.; Goridis, Christo; Walsh, Frank S.

doi:10.1242/dev.104.1.165

Cited by 61 publications

(1 citation statement)

References 34 publications

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“…Pi-specific phospholipase C has been identified in skeletal muscle (Barton et al, 1988). In view of the findings that other isoforms of phospholipase may be substrates of the EGF receptor (Wahl et al, 1989;Margolis et al, 1989), one might speculate that the hepatic ppl20 is a phospholiase or cell adhesion molecule.…”

Section: Resultsmentioning

confidence: 99%

Epidermal growth factor stimulated phosphorylation of a 120-kilodalton endogenous substrate protein in rat hepatocytes

Okamoto

Karasik²,

Mf³

et al. 1990

Biochemistry

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Endogenous substrates of the EGF receptor have been described in transformed cells; however, little is known about substrates in normal tissue. To characterize epidermal growth factor (EGF) receptor phosphorylation and search for endogenous substrates in normal rat hepatocytes, cells were labeled with [32P]orthophosphate, and phosphotyrosine-containing proteins were sought by using a high-affinity, specific anti-phosphotyrosine antibody. Exposure of 32P-labeled freshly isolated hepatocytes to 1 microgram/mL EGF caused phosphorylation of several proteins of Mr 185K, 160K, and 120K. The 185- and 160-kDa proteins (pp185 and pp160) were identified as the intact and proteolyzed forms of the EGF receptor by virtue of their immunoprecipitation with anti-EGF receptor antibody. This antibody failed to recognize the 120-kDa phosphoprotein (pp120). The phosphopeptide map derived from pp120 was by trypsinization and HPLC separation different from that of pp185, further indicating that pp120 is distinct from the EGF receptor. This pp120 was also immunologically distinct from the pp120 substrate of the insulin receptor kinase and from ATP-citrate lyase. Phosphoamino acid analysis revealed pp120 to be phosphorylated on both tyrosine and serine residues. Autophosphorylation of EGF receptor and phosphorylation of pp120 were almost maximal within 1 min of EGF stimulation. The dose-response curves for phosphorylation of the EGF receptor and pp120 were identical (ED50 = 30 ng/mL) and were superimposable with the fractional occupancy of the EGF receptor. In A431 cells, a transformed cell line whose growth is inhibited by EGF, EGF produced a decrease in pp120 phosphorylation. These data suggest that pp120 is an endogenous substrate for the EGF receptor in hepatocytes whose phosphorylation may be closely related to EGF stimulation of cell growth.

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Section: Resultsmentioning

confidence: 99%

Epidermal growth factor stimulated phosphorylation of a 120-kilodalton endogenous substrate protein in rat hepatocytes

Okamoto

Karasik²,

Mf³

et al. 1990

Biochemistry

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Generation of multiple N‐CAM polypeptides from a single gene

Walsh

Dickson

1989

BioEssays

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The neural cell adhesion molecule (N-CAM) is believed to be a key regulator of adhesive events in the nervous system and skeletal muscle. The recent isolation of N-CAM cDNAs from different tissues has identified a high degree of diversity in primary amino acid sequence between different isoforms. In this article, we review these recent studies and discuss methods for unravelling the functional consequences of the generation of multiple N-CAM polypeptides using gene transfection approaches.

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Splicing of the vase exon of neural cell adhesion molecule (NCAM) in human small‐cell lung carcinoma (SCLC)

Duijnhoven

Helfrich²,

Leij³

et al. 1992

Intl Journal of Cancer

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Expression of the neural cell adhesion molecule (NCAM) on small-cell lung carcinoma (SCLC) cell lines and tumour tissue has been investigated. Cell lines were found to express highly sialylated NCAM. Neuraminidase treatment revealed the presence of the 140- and 120-kDa isoforms with differential expression of a 95-kDa protein. Similar data were obtained with SCLC tumour tissues. These results were corroborated by Northern blotting where mRNA of 6.7 and 5.5 kb coding for the 140- and 120-kDa isoforms, respectively, were identified. In a few tumours, a weaker band of 7.4-kb mRNA coding for the 180-kDa NCAM was also identified. This result could not be confirmed biochemically due to shortage of material. Finally, a 5-kb transcript was identified in all SCLC samples examined. The NCAM isoform coded by this mRNA remains unknown. Using the polymerase chain reaction (PCR), we have demonstrated the presence of the VASE mini-exon in some isoforms of SCLC NCAM. The VASE mini-exon sequence in human SCLC differs from the published murine sequence by only one base change. This substitution does not result in altered amino-acid sequence.

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Complete sequence andin vitroexpression of a tissue-specific phosphatidylinositol-linked N-CAM isoform from skeletal muscle

Cited by 61 publications

References 34 publications

Epidermal growth factor stimulated phosphorylation of a 120-kilodalton endogenous substrate protein in rat hepatocytes

Epidermal growth factor stimulated phosphorylation of a 120-kilodalton endogenous substrate protein in rat hepatocytes

Generation of multiple N‐CAM polypeptides from a single gene

Splicing of the vase exon of neural cell adhesion molecule (NCAM) in human small‐cell lung carcinoma (SCLC)

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