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Review
. 2024 Apr 24;25(9):4634.
doi: 10.3390/ijms25094634.

Claudins in Cancer: A Current and Future Therapeutic Target

Caroline Hana  1 , Nyein Nyein Thaw Dar  1 , Michael Galo Venegas  1 , Michel Vulfovich  1
Affiliations
Review

Claudins in Cancer: A Current and Future Therapeutic Target

Caroline Hana et al. Int J Mol Sci. .

Abstract

Claudins are a family of 27 proteins that have an important role in the formation of tight junctions. They also have an important function in ion exchange, cell mobility, and the epithelial-to-mesenchymal transition, the latter being very important in cancer invasion and metastasis. Therapeutic targeting of claudins has been investigated to improve cancer outcomes. Recent evidence shows improved outcomes when combining monoclonal antibodies against claudin 18.2 with chemotherapy for patients with gastroesophageal junction cancer. Currently, chimeric antigen receptor T-cells targeting claudin 18 are under investigation. In this review, we will discuss the major functions of claudins, their distribution in the normal as well as cancerous tissues, and their effect in cancer metastasis, with a special focus on the therapeutic targeting of claudins to improve cancer outcomes.

Keywords: CAR-T cell therapy; carcinoma; claudin; monoclonal antibodies; targeted therapy.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Simplified diagram of the common structure of claudins with 4 transmembrane domains (I through IV) spanning the thickness of the phospholipid bilayer, with 2 extracellular domains, a larger 1st domain and a smaller 2nd domain. ECL: extracellular loop; ICL: intracellular loop.
See this image and copyright information in PMC

References

    1. Niessen C.M. Tight junctions/adherens junctions: Basic structure and function. J. Investig. Dermatol. 2007;127:2525–2532. doi: 10.1038/sj.jid.5700865. - DOI - PubMed
    1. Staehelin L.A. Further observations on the fine structure of freeze-cleaved tight junctions. J. Cell Sci. 1973;13:763–786. doi: 10.1242/jcs.13.3.763. - DOI - PubMed
    1. Schneeberger E.E., Lynch R.D. The tight junction: A multifunctional complex. Am. J. Physiol. Cell Physiol. 2004;286:C1213–C1228. doi: 10.1152/ajpcell.00558.2003. - DOI - PubMed
    1. Ikenouchi J., Furuse M., Furuse K., Sasaki H., Tsukita S., Tsukita S. Tricellulin constitutes a novel barrier at tricellular contacts of epithelial cells. J. Cell Biol. 2005;171:939–945. doi: 10.1083/jcb.200510043. - DOI - PMC - PubMed
    1. Furuse M., Hirase T., Itoh M., Nagafuchi A., Yonemura S., Tsukita S., Tsukita S. Occludin: A novel integral membrane protein localizing at tight junctions. Pt 2J. Cell Biol. 1993;123:1777–1788. doi: 10.1083/jcb.123.6.1777. - DOI - PMC - PubMed