Abstract
Dipeptidyl peptidase IV (DP IV, CD26) is a membrane bound serine protease which ubiquitously occurs in epithelial tissues of mammalian organisms, above all in kidney, liver and intestine1,2 but also on the surface of immune cells3. DP IV is involved not only in activation of B- and T-lymphocytes4,5 and NK-cells6 with peptidase activity but also in the regulation of growth process, DNA-synthesis and cytokine production7. Therefore it is important for the signal transduction during the immune response. DP IV catalyses the cleavage of N-terminal dipeptides from oligo- and polypeptides where the penultimate residue is proline or -with less efficiency- alanine8,9. To investigate the physiological role of DP IV in further detail, specific high sensitive substrates or inhibitors would be useful tools. Here we describe the synthesis and enzymatic characterisation of sensitive fluoro-genic rhodamine 110 (R110)-based substrates and fluoresceine- or biotin-labelled inhibitors and their use for the sensitive detection of DP IV on the surface of T-cell lines.
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Lorey, S., Faust, J., Hermanns, U., Bühling, F., Ansorge, S., Neubert, K. (1997). New Fluorogenic Dipeptidyl Peptidase IV/CD26 Substrates and Inhibitors. 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_20
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DOI: https://doi.org/10.1007/978-1-4757-9613-1_20
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