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      CEA adhesion molecules: multifunctional proteins with signal-regulatory properties

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          Abstract

          The carcinoembryonic antigen family comprises a large number of complex molecules, several of which possess cell adhesion activities. The primordial adhesion molecules of this family are the cell—cell adhesion molecules (C-CAMs), which have been found to be multifunctional, signal-regulatory proteins. C-CAMs inhibit tumor growth, interact with calmodulin, protein tyrosine kinases and protein tyrosine phosphatases, and are subject to specific dimerization reactions. These new insights indicate that C-CAMs are important regulators of cellular functions.

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          A family of proteins that inhibit signalling through tyrosine kinase receptors.

          A Kharitonenkov, Hongwei Wang, A Ullrich … (1997)
          Phosphotyrosine phosphatases are critical negative or positive regulators in the intracellular signalling pathways that result in growth-factor-specific cell responses such as mitosis, differentiation, migration, survival, transformation or death. The SH2-domain-containing phosphotyrosine phosphatase SHP-2 is a positive signal transducer for several receptor tyrosine kinases (RTKs) and cytokine receptors. To investigate its mechanism of action we purified a tyrosine-phosphorylated glycoprotein which in different cell types associates tightly with SHP-2 and appears to serve as its substrate. Peptide sequencing in conjunction with complementary DNA cloning revealed a new gene family of at least fifteen members designated signal-regulatory proteins (SIRPs). They consist of two subtypes distinguished by the presence or absence of a cytoplasmic SHP-2-binding domain. The transmembrane polypeptide SIRP alpha1 is a substrate of activated RTKs and in its tyrosine-phosphorylated form binds SHP-2 through SH2 interactions and acts as its substrate. It also binds SHP-1 and Grb2 in vitro and has negative regulatory effects on cellular responses induced by growth factors, oncogenes or insulin. Our findings indicate that proteins belonging to the SIRP family generally regulate signals defining different physiological and pathological processes.
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            Recruitment of tyrosine phosphatase HCP by the killer cell inhibitor receptor.

            Andrew Scharenberg, Deborah N. Burshtyn, T. Yi … (1995)
            Cytolysis of target cells by natural killer (NK) cells and by some cytotoxic T cells occurs unless prevented by inhibitory receptors that recognize MHC class I on target cells. Human NK cells express a p58 inhibitory receptor specific for HLA-C. We report association of the tyrosine phosphatase HCP with the p58 receptor in NK cells. HCP association was dependent on tyrosine phosphorylation of p58. Phosphotyrosyl peptides corresponding to the p58 tail bound and activated HCP in vitro. Furthermore, introduction of an inactive mutant HCP into an NK cell line prevented the p58-mediated inhibition of target cell lysis. These data imply that the inhibitory function of p58 is dependent on its tyrosine phosphorylation and on recruitment and activation of HCP.
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              The N-domain of the human CD66a adhesion molecule is a target for Opa proteins of Neisseria meningitidis and Neisseria gonorrhoeae.

              Charlotte Barker, Ian Watt, R Doyonnas … (1996)
              Using COS (African green monkey kidney) cells transfected with cDNAs encoding human cell surface molecules, we have identified human cellular receptors for meningococcal virulence-associated Opa proteins, which are expressed by the majority of disease and carrier isolates. These receptors belong to the immunoglobulin superfamily of adhesion molecules and are expressed on epithelial, endothelial and phagocytic cells. Using soluble chimeric receptor molecules, we have demonstrated that meningococcal Opa proteins bind to the N-terminal domain of biliary glycoproteins (classified as BGP or CD66a) that belong to the CEA (CD66) family. Moreover, the Opa proteins of the related pathogen Neisseria gonorrhoeae, responsible for urogenital infections, also interact with this receptor, making CD66a a common target for pathogenic neisseriae. Over 95% of Opa-expressing clinical and mucosal isolates of meningococci and gonococci were shown to bind to the CD66 N-domain, demonstrating the presence of a conserved receptor-binding function in the majority of neisserial Opa proteins.
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                Author and article information

                Contributors
                Björn Öbrink
                Journal
                Journal ID (nlm-ta): Curr Opin Cell Biol
                Journal ID (iso-abbrev): Curr. Opin. Cell Biol
                Title: Current Opinion in Cell Biology
                Publisher: Published by Elsevier Ltd.
                ISSN (Print): 0955-0674
                ISSN (Electronic): 1879-0410
                Publication date PMC-release: 25 February 2002
                Publication date (Print): October 1997
                Publication date (Electronic): 25 February 2002
                Volume: 9
                Issue: 5
                Pages: 616-626
                Affiliations
                Department of Cell and Molecular Biology, Medical Nobel Institute, Karolinska Institute, Stockholm S-171 77, Sweden
                Article
                Publisher ID: S0955-0674(97)80114-7
                DOI: 10.1016/S0955-0674(97)80114-7
                PMC ID: 7135799
                PubMed ID: 9330864
                SO-VID: ab09135c-a034-4a74-bd5e-6aea6b30e1c2
                Copyright © Copyright © 1997 Published by Elsevier Ltd.
                License:

                Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.

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                Subject: Article

                ScienceOpen disciplines: Cell biology
                Keywords: bgp biliary glycoprotein in mouse,bgp biliary glycoprotein in man,c-cam cell—cell adhesion molecule,cea carcinoembryonic antigen,cgm cea gene family member,gpi glycosylphosphatidylinositol,ig immunoglobulin,igsf ig gene superfamily,itam immunoreceptor tyrosine-based activation motif,itim immunoreceptor tyrosine-based inhibition motif,l long,nca nonspecific cross-reactive antigen,ptk protein tyrosine kinase,ptp protein tyrosine phosphatase,s short,sh src homology,shp sh2-domain-containing ptp,sirp signal-regulatory protein
                Data availability:
                ScienceOpen disciplines: Cell biology
                Keywords: bgp biliary glycoprotein in mouse, bgp biliary glycoprotein in man, c-cam cell—cell adhesion molecule, cea carcinoembryonic antigen, cgm cea gene family member, gpi glycosylphosphatidylinositol, ig immunoglobulin, igsf ig gene superfamily, itam immunoreceptor tyrosine-based activation motif, itim immunoreceptor tyrosine-based inhibition motif, l long, nca nonspecific cross-reactive antigen, ptk protein tyrosine kinase, ptp protein tyrosine phosphatase, s short, sh src homology, shp sh2-domain-containing ptp, sirp signal-regulatory protein

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