Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells

Beauchemin, Nicole; Kunath, Tilo; Robitaille, Julie; Chow, Bernard; Turbide, Claire; Daniels, Eugene; Veillette, André

doi:10.1038/sj.onc.1200888

Cited by 132 publications

(128 citation statements)

References 30 publications

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“…However, its expression on normal tissues is limited to the luminal surface of the gut, where it is not accessible to mAbs (Kinugasa et al, 1998). Several CEA subgroup members possess cell adhesion properties (Zhou et al, 1993) and a function in signal transduction or regulation of signal transduction has also been suggested (Beauchemin et al, 1997). CEA has been targeted by mAbs in several clinical trials for a variety of applications, including radioimmunotherapy, ADEPT and radioimmuno-guided surgery (Juweid et al, 1999;Francis et al, 2002;Sharkey et al, 2005b).…”

Section: Ceamentioning

confidence: 99%

Novel antibodies as anticancer agents

2007

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In recent years antibodies, whether generated by traditional hybridoma technology or by recombinant DNA strategies, have evolved from Paul Ehrlich's 'magic bullets' to a modern age 'guided missile'. In the recent years of immunologic research, we are witnessing development in the fields of antigen screening and protein engineering in order to create specific anticancer remedies. The developments in the field of recombinant DNA, protein engineering and cancer biology have let us gain insight into many cancer-related mechanisms. Moreover, novel techniques have facilitated tools allowing unique distinction between malignantly transformed cells, and regular ones. This understanding has paved the way for the rational design of a new age of pharmaceuticals: monoclonal antibodies and their fragments. Antibodies can select antigens on both a specific and a high-affinity account, and further implementation of these qualities is used to target cancer cells by specifically identifying exogenous antigens of cancer cell populations. The structure of the antibody provides plasticity resonating from its functional sites. This review will screen some of the many novel antibodies and antibody-based approaches that are being currently developed for clinical applications as the new generation of anticancer agents.

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Section: Ceamentioning

confidence: 99%

Novel antibodies as anticancer agents

2007

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“…13 The long form of CEACAM1 protein has 2 ITIMs that preferentially recruit SHP-1 protein-tyrosine phosphatase and, to a lesser extent, SHP-2 protein-tyrosine phosphatase. 14,15 Based on recent studies in T cells, CEACAM1 functions as a negative regulator via its recruitment and activation of SHP-1 protein-tyrosine phosphatase. 16 However, little is known about the presence and functional role of CEACAM1 in regulating platelet-collagen interactions and thrombus formation in vitro and in vivo.…”

Section: Introductionmentioning

confidence: 99%

CEACAM1 negatively regulates platelet-collagen interactions and thrombus growth in vitro and in vivo

Wong

Liu

Yip

et al. 2009

Blood

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Carcinoembryonic antigen cell adhesion molecule-1 (CEACAM1) is a surface glycoprotein expressed on various blood cells, epithelial cells, and vascular cells. CEACAM1 possesses adhesive and signaling properties mediated by its intrinsic immunoreceptor tyrosine-based inhibitory motifs that recruit SHP-1 protein-tyrosine phosphatase. In this study, we demonstrate that CEACAM1 is expressed on the surface and in intracellular pools of platelets. In addition, CEACAM1 serves to negatively regulate signaling of platelets by collagen through the glycoprotein VI (GPVI)/Fc receptor (FcR)-␥-chain. ceacam1 ؊/؊ platelets displayed enhanced type I collagen and GPVI-selective ligand, collagen-related peptide (CRP), CRPmediated platelet aggregation, enhanced platelet adhesion on type I collagen, and elevated CRP-mediated alpha and dense granule secretion. Platelets derived from ceacam1 ؊/؊ mice form larger thrombi when perfused over a collagen matrix under arterial flow compared with wild-type mice. Furthermore, using intravital microscopy to ferric chloride-injured mesenteric arterioles, we show that thrombi formed in vivo in ceacam1 ؊/؊ mice were larger and were more stable than those in wild-type mice. GPVI depletion using monoclonal antibody JAQ1 treatment of ceacam1 ؊/؊ mice showed a reversal in the more stable thrombus growth phenotype. ceacam1 ؊/؊ mice were more susceptible to type I collagen-induced pulmonary thromboembolism than wild-type mice. Thus, CEACAM1 acts as a negative regulator of platelet-collagen interactions and of thrombus growth involving the collagen GPVI receptor in vitro and in vivo. (Blood.

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“…The distal N-terminal domain, an IgVlike domain, mediates its cell-cell adhesion properties (3). The 73-aa-long cytoplasmic domain contains two immunoreceptor tyrosine-based inhibitory motifs (ITIM) that have been shown to mediate inhibitory functions in epithelial cells (4). The long cytoplasmic domain has been shown to associate with actin and signal via the rho family of GTPases (5).…”

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confidence: 99%

The Cell-Cell Adhesion Molecule Carcinoembryonic Antigen-Related Cellular Adhesion Molecule 1 Inhibits IL-2 Production and Proliferation in Human T Cells by Association with Src Homology Protein-1 and Down-Regulates IL-2 Receptor

Chen

Shively

2004

The Journal of Immunology

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The cell adhesion molecule, carcinoembryonic Ag-related cellular adhesion molecule 1, shown by others to both activate and inhibit T cell proliferation, exhibits a reciprocal relationship to IL-2R expression over the time course of activation of PBMCs, and upon Ab ligation, inhibits both the production of IL-2 and cell proliferation. Carcinoembryonic Ag-related cellular adhesion molecule 1 associates with CD3 and is found in lipid rafts of PBMCs, is phosphorylated on the immunoreceptor tyrosine-based inhibitory motifs (ITIMs) of the -4L isoform, and associates with Src homology protein-1, providing an explanation for its inhibitory activity. When the ITIM-containing -4L and non-ITIM-containing -4S isoforms are transfected into Jurkat cells that produce, but do not depend on IL-2 for growth, both IL-2 production and cell proliferation are differentially inhibited, demonstrating that the two isoforms signal via different pathways. When the two isoforms are transfected into Kit-225 cells that depend on IL-2 for growth, IL-2Rβ and γ, but not α subunits are down-regulated, and the -4L, but not the -4S isoform inhibits cell proliferation by 6-fold in an IL-2 dose-response study.

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Association of biliary glycoprotein with protein tyrosine phosphatase SHP-1 in malignant colon epithelial cells

Cited by 132 publications

References 30 publications

Novel antibodies as anticancer agents

Novel antibodies as anticancer agents

CEACAM1 negatively regulates platelet-collagen interactions and thrombus growth in vitro and in vivo

The Cell-Cell Adhesion Molecule Carcinoembryonic Antigen-Related Cellular Adhesion Molecule 1 Inhibits IL-2 Production and Proliferation in Human T Cells by Association with Src Homology Protein-1 and Down-Regulates IL-2 Receptor

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