Abstract
CD26, or dipeptidyl peptidase IV, is a widely distributed cell surface glycoprotein of approximately 110 kD molecular weight. It is constitutively expressed on a variety of different cell types, particularly on epithelial cells of the intestine, prostate and kidney-proximal tubules1–3. On T cells the expression of CD26 is regulated more stringently. The molecule is absent from the majority of human resting peripheral blood T lymphocytes and is expressed weakly on a fraction of T cells in the blood. Expression increases within two days of T cell activation and increases further after culture in vitro 1. 2. It has been shown to be a suitable marker for T cells activated in vivo 4 and memory T cells have been shown to reside in the CD26+ T cell fraction5. CD26 has several unique properties that distinguish this molecule from related surface proteases:
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i.
the expression of CD26 is tightly regulated in different tissues
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ii.
it is associated with the differentiation and activation status of different cells
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iii.
CD26 is highly conserved among different species6.
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Fleischer, B., Steeg, C., Hühn, J., von Bonin, A. (1997). Molecular Associations Required for Signalling VIA Dipeptidyl Peptidase IV (CD26). In: Ansorge, S., Langner, J. (eds) Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology, vol 421. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9613-1_16
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DOI: https://doi.org/10.1007/978-1-4757-9613-1_16
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