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Mucosal interactions with enteropathogenic bacteria
Published in Phillip D. Smith, Richard S. Blumberg, Thomas T. MacDonald, Principles of Mucosal Immunology, 2020
Nadine Cerf-Bensussan, Pamela Schnupf, Valérie Gaboriau-Routhiau, Philippe J. Sansonetti
Among the host factors that facilitate AIEC colonization is the abnormal ileal expression of CEACAM6, which has been observed in patients with ileal Crohn's disease. In contrast to CEACAM1, which is constitutively expressed on the apical cell surface of intestinal epithelial cells, CEACAM6 is an induced molecule. AIEC adhere to the brush border of primary ileal enterocytes isolated from patients with Crohn's disease, but not those from individuals without IBD, due to the abnormal expression of CEACAM6. Most AIEC strains associated with Crohn's disease ileal mucosa express type I pili variants that increase the interaction between AIEC and ileal epithelial cells. Increased expression of CEACAM6 can result from interferon-γ (IFN-γ) or TNF-α stimulation and also from infection with AIEC bacteria, indicating that AIEC can promote their own colonization in patients with Crohn's disease. The presence of AIEC bacteria and their ability to induce the secretion of pro-inflammatory cytokines by infected macrophages could lead to an amplification loop of colonization and inflammation. This has been confirmed in vivo with the LF82 strain of AIEC, but not nonpathogenic E. coli K-12, wherein LF82 persists in the gut of mice that transgenically express human CEACAMs and induces severe colitis.
T cell-mediated elimination of cancer cells by blocking CEACAM6–CEACAM1 interaction
Published in OncoImmunology, 2022
Jessica Pinkert, Hans-Henning Boehm, Mark Trautwein, Wolf-Dietrich Doecke, Florian Wessel, Yingzi Ge, Eva Maria Gutierrez, Rafael Carretero, Christoph Freiberg, Uwe Gritzan, Merlin Luetke-Eversloh, Sven Golfier, Oliver Von Ahsen, Valentina Volpin, Antonio Sorrentino, Anchana Rathinasamy, Maria Xydia, Robert Lohmayer, Julian Sax, Ayse Nur-Menevse, Abir Hussein, Slava Stamova, Georg Beckmann, Julian Marius Glueck, Dorian Schoenfeld, Joerg Weiske, Dieter Zopf, Rienk Offringa, Bertolt Kreft, Philipp Beckhove, Joerg Willuda
Carcinoembryonic antigen-related cell adhesion molecule 6 (CEACAM6, CD66c, nonspecific cross-reacting antigen, NCA, or NCA-50/90) is a glycosylphosphatidylinositol (GPI)-linked cell surface protein that belongs to the CEACAM family of the immunoglobulin (Ig) supergene family.6,7 CEACAMs participate in the regulation of cell-cell adhesion, tissue formation, angiogenesis, apoptosis, tumor suppression, invasion, and metastasis formation but can also act as pathogen receptors.8–10 They undergo homo- and heterophilic interactions with other CEACAMs, and CEACAM6 has been found to bind CEACAM5 and CEACAM8.6,7,11 Since neither CEACAM5 nor CEACAM8 possesses intracellular signaling domains or is expressed on T cells, other CEACAM ligands may mediate the T cell suppression observed with CEACAM6. Among them, CEACAM1 is found on activated T cells and one of the few CEACAM receptors containing intracellular immunoreceptor tyrosine-based inhibitory motive (ITIM) domains for T cell signaling.11 Indeed, CEACAM1-CEACAM1 homophilic interactions between T cells and CEACAM1-expressing cancer cells can play a role in antitumor T cell suppression, and binding of CEACAM1 by pathogens can lead to T cell inhibition.9,10
Generation and in vivo characterization of a novel high-affinity human antibody targeting carcinoembryonic antigen
Published in mAbs, 2023
Louis Plüss, Frederik Peissert, Abdullah Elsayed, Giulia Rotta, Jonas Römer, Sheila Dakhel Plaza, Alessandra Villa, Emanuele Puca, Roberto De Luca, Annette Oxenius, Dario Neri
Other CEA-related cell adhesion molecules (CEACAMs) have highly conserved N-terminal domains to CEA, especially CEACAM1, and CEACAM6. The specificity of the F4 antibody to CEA was confirmed by flow cytometry on transiently antigen-expressing CHO cells, as no binding was detected on CEACAM1- and CEACAM6-expressing cells [Supplementary Figure S6].
Characterization of sphere cells derived from a patient-derived xenograft model of lung adenocarcinoma treated with ionizing radiation
Published in International Journal of Radiation Biology, 2020
Jinhyang Choi, Eun Jung Ko, Eun Jin Ju, Seok Soon Park, Jin Park, Seol Hwa Shin, Se Jin Jang, Jung Shin Lee, Si Yeol Song, Seong-Yun Jeong, Eun Kyung Choi
Interestingly, many markers identified by cDNA microarray are known to be related to immune reactions. Overexpression of SERPINB4, an intracellular serine protease inhibitor, is known to inhibit granzyme M-induced and NK cell-mediated cell death. Granzyme-mediated cell death is the major pathway for cytotoxic lymphocytes to kill virus-infected and tumor cells (de Koning et al. 2011). Another name for CCL2, chemokine (C-C motif) ligand 2, is monocyte chemoattractant protein 1 (MCP1). CCL2-CCR2 signaling has been shown to recruit myeloid cells such as tumor-associated macrophages to trigger an angiogenic switch, and to induce myeloid-derived suppressor cells (MDSCs) to suppress and evade immune-mediated killing (Lim et al. 2016). Ubiquitin D (UBD) is well known as the ubiquitin-like modifier FAT10, a protein of the immune system. FAT10 expression is highly upregulated by pro-inflammatory cytokines, IFN-γ and TNF-α in all cell types and tissues, and it was also found to be upregulated in many cancer types such as glioma, colorectal, liver, or gastric cancer (Aichem and Groettrup 2016). SLPI, secretory leukocyte peptidase inhibitor, has been shown to possess anti-inflammatory and antiprotease functions including downregulation of TNF-α expression by lipopolysaccharide (LPS) in macrophages and inhibition of nuclear factor nuclear factor-kappaB (NF-κB) activation in a rat model of acute lung injury (Taggart et al. 2005). Overexpression of CEACAM6, carcinoembryonic antigen-related cell adhesion molecule 6, which is a member of the CEA family of cell adhesion proteins within the immunoglobulin superfamily, is correlated with malignancy in colorectal cancer (CRC), pancreatic ductal adenocarcinoma (PDA), and hepatobiliary, gastric, breast, non-small cell lung, and head/neck cancers (Johnson and Mahadevan 2015). LPS-binding protein, LBP, is an acute-phase protein synthesized predominantly in the liver that binds to LPS of gram-negative bacteria to elicit immune responses by presenting the LPS to the cell surface pattern recognition receptors, CD14 and TLR4 (Lamping et al. 1996; Kogut et al. 2005). There have been no reports stating that LBP is directly related to cancer. However, it was reported that LBP was significantly and positively correlated with the mean radiation dose to the lung in NSCLC (Chalubinska-Fendler et al. 2016). The type 2 cystatin proteins (CST2, cystatin SA) are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. Cystatin SN (CST1) has been identified as a marker of colorectal cancers (Yoneda et al. 2009). High expression of the salivary cystatins CST1, CST2, and CST4 can promote bone metastasis in cancer cell lines (Blanco et al. 2012).