Abstract
Biliary glycoprotein (Bgp) is a member of the immunoglobulin superfamily and the carcinoembryonic antigen family. Previous studies have shown that Bgp functions as an intercellular adhesion molecule and a canalicular bile salt transporter. Moreover, we and others demonstrated that Bgp can inhibit colonic and prostatic tumor cell growth in vivo, through a mechanism which depends on sequences present in its cytoplasmic domain. In this study, we have examined the possibility that the cytoplasmic domain of Bgp can interact with signal transduction molecules. We showed that tyrosine phosphorylated Bgp, expressed in mouse colon carcinoma CT51 cells, could reversibly associate with protein tyrosine phosphatase SHP-1. Mutation of either of two tyrosine residues present in the cytoplasmic domain of Bgp abrogated SHP-1 binding, suggesting that this association was mediated by both tyrosine residues. Similarly, we noted that either of the two SH2 domains of SHP-1 could bind tyrosine phosphorylated Bgp in vitro. It is therefore conceivable that some of the functions of Bgp are mediated through its ability to induce intracellular protein tyrosine dephosphorylation.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 50 print issues and online access
$259.00 per year
only $5.18 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Beauchemin, N., Kunath, T., Robitaille, J. et al. Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells. Oncogene 14, 783–790 (1997). https://doi.org/10.1038/sj.onc.1200888
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/sj.onc.1200888
Keywords
This article is cited by
-
Integrated analysis of gene expression, alteration and clinical significance of carcinoembryonic antigen-related cell adhesion molecule 1 in cancer
3 Biotech (2020)
-
CEACAM1 induces B-cell survival and is essential for protective antiviral antibody production
Nature Communications (2015)
-
Carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) in cancer progression and metastasis
Cancer and Metastasis Reviews (2013)
-
Osteopontin’s colocalization with the adhesion molecule CEACAM5 in cytoplasm of carcinoma of tongue and its correlation with the invasion of that diease
Cancer Cell International (2012)
-
The Possible Roles of OPN-Regulated CEACAM1 Expression in Promoting the Survival of Activated T Cells and the Apoptosis of Oral Keratinocytes in Oral Lichen Planus Patients
Journal of Clinical Immunology (2011)