Abstract
By using a CD26 negative human lymphoblastoid cell line (C8166), here we describe the characterization of a cell-surface protein which manifests CD26-like dipeptidyl peptidase IV (DPP IV) activity. This protein, referred to as DPP IV-β, shows a higher KM value for Gly-Pro-pNA than CD26 (0,31 mM compared to 0,11 mM, respectively). In addition, DPP IV-β was found not to bind 125I-labeled adenosine deaminase (a property of human CD26). Gel filtration experiments using extracts from C8166 and MOLT4 (a CD26 positive human T cell line) cells, revealed that the apparent molecular mass of DPP IV-β is 82 kDa, whereas that of CD26 is 110 kDa. In order to conveniently differentiate both activities, a new family of inhibitors, that selectively blocks peptidase activity associated to CD26, has been developed.
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© 1997 Springer Science+Business Media New York
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Blanco, J., Jacotot, E., Callebaut, C., Krust, B., Hovanessian, A.G. (1997). Further Characterization of DPP IV-β, a Novel Cell Surface Expressed Protein with Dipeptidyl Peptidase Activity. 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_25
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DOI: https://doi.org/10.1007/978-1-4757-9613-1_25
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-9615-5
Online ISBN: 978-1-4757-9613-1
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