Abstract
A cholecystokinin (CCK)-inactivating peptidase was purified and identified as a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10), a cytosolic subtilisin-like peptidase of previously unknown functions. The peptidase was found in neurons responding to cholecystokinin, as well as in non-neuronal cells. Butabindide, a potent and specific inhibitor, was designed and shown to protect endogenous cholecystokinin from inactivation and to display pro-satiating effects mediated by the CCKA receptor.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Dockray, G. J. Gastrointestinal Endocrinology: Receptors and Post-receptors Mechanisms (ed. Thompson, J.) 321–332 (Academic, New York, 1990).
Vanderhaegen, J. J., Signeau, J. C. & Gepts, W. Nature 257, 604–605 (1975).
Dockray, G. J. Nature 264, 568–570 (1976).
Vanderhaegen, J. J. & Crawley, J. N. Ann. N.Y. Acad. Sci. 448, 1–697 (1984).
Hughes, J., Dockray, G. J. & Woodruff, G. (eds) The Neuropeptide Cholecystokinin (CCK) (Ellis Horwood, Chichester, 1989).
Hökfelt, T. et al. Nature 285, 476–479 (1980).
Woodruff, G. & Hughes, J. A. Rev. Pharmac. 31, 469–501 (1991).
Smith, G. P. & Gibbs, J. Ann. N.Y. Acad. Sci. 713, 236–241 (1994).
Malfroy, B., Swerts, J. P., Guyon, A., Roques, B. P. & Schwartz, J.-C. Nature 276, 523–526 (1978).
Llorens-Cortes, C. et al. Biochem. biophys. Res. Commun. 96, 1710–1716 (1980).
Roques, B. P. et al. Nature 288, 286–288 (1980).
Patey, G. et al. Science 212, 1153–1155 (1981).
Baumer, Ph. et al. Gut 33, 753–758 (1992).
Deschodt-Lanckman, M. et al. Peptides 4, 71–78 (1983).
Deschodt-Lanckman, M. et al. Peptides 5, 649–651 (1984).
Matsas, A., Turner, A. J. & Kenny, A. J. FEBS Lett. 175, 124–128 (1984).
McDermott, J. R. et al. Neurochem. Int. 5, 641–647 (1983).
Steardo, L. et al. J. Neurochem. 45, 784–790 (1985).
Durieux, C. et al. Neuropeptides 7, 1–9 (1986).
Zuzel, K. A., Rose, C. & Schwartz, J.-C. J. Neurochem. 15, 149–158 (1985).
Wilson, C., Gibson, A. M. & McDermott, J. R. Neurochem. Res. 18, 743–749 (1993).
Rose, C., Camus, A. & Schwartz, J.-C. Proc. natn. Acad. Sci. U.S.A. 85, 8326–8330 (1988).
Rose, C., Camus, A. & Schwartz, J.-C. Neurosci. 29, 583–594 (1989).
Camus, A., Rose, C. & Schwartz, J.-C. Neurosci. 29, 595–602 (1989).
Llorens-Cortes, C., Gros, C. & Schwartz, J.-C. Proc. natn. Acad. Sci. U.S.A. 83, 6226–6230 (1986).
Tomkinson, B. & Jonsson, A. K. Biochemistry 30, 168–174 (1991).
Bålöw, R. M., Ragnarsson, V. & Zetterqvist, Ö. J. biol. Chem. 258, 11622–11628 (1983).
Bålöw, R. M. et al. J. biol. Chem. 261, 2409–2417 (1986).
Tomkinson, B. Biochem. J. 304, 517–523 (1994).
Low, M. G. FASEB J. 3, 1600–1607 (1989).
Ferguson, M. A. J. A. Rev. Biochem. 57, 285–320 (1988).
Low, M. G., Stiernberg, J., Waneck, G. L., Flavel, R. A. & Kincade, P. W. J. immunol. Meth. 113, 101–111 (1988).
Malfroy, B. et al. Biochem. biophys. Res. Commun. 114, 59–66 (1987).
Massoulié, J., Pezzementi, L., Bon, S., Krejci, F. & Vallette, F. M. Prog. Neurobiol. 41, 31–91 (1993).
Schwartz, J.-C., Malfroy, B. & De la Baume, S. Life Sci. 29, 1715–1740 (1981).
Vanderhaegen, J. J. in Handbk Chem. Neuroanat. Vol. 4, Part 1 (eds Bjorklund, A. & Hökfelt, T.) 406–435 (Elsevier, Amsterdam, 1985).
Hughes, J. et al. Proc. natn. Acad. Sci. U.S.A. 87, 6728–6732 (1990).
Persson, H. et al. Proc. natn. Acad. Sci. U.S.A. 86, 6166–6170 (1989).
Powers, J. C. & Harper, W. Proteinase Inhibitors (eds Barrett, A. J. & Salvesen, G.) 55–152 (Elsevier, Amsterdam, 1986).
Schechter, I. & Berger, A. Biochem. biophys. Res. Commun. 27, 157–162 (1967).
Cheng, C. & Prussoff, W. H. Biochem. Pharmac. 22, 3099–3108 (1973).
Tarr, G. E. Methods of Protein Microcharacterization (ed. Shively, J. E) 155–194 (Humana, Clifton, NJ, 1986).
Laemmli, U. K. Nature 227, 680–685 (1970).
Danielsen, E. M., Sjöström, H., Noren, O. & Dabelsteen, E. Biochem. biophys. Acta 494, 332–342 (1977).
Whittaker, V. P. Ann. N.Y. Acad. Sci. 137, 982–998 (1966).
Giros, B. et al. J. Pharmac. exp. Ther. 243, 666–673 (1987).
Ellman, G. L., Courtney, K. D., Andres, V. Jr & Featherstone, R. Biochem. Pharmac. 7, 88–95 (1961).
Sokoloff, P., Giros, B., Martres, M. P., Bouthenet, M. L. & Schwartz, J.-C. Nature 347, 146–151 (1990).
Lotti, V. J. et al. J. Pharmac. exp. Ther. 241, 103–109 (1987).
Chariot, J., Nagain, C., Hugonet, F., Tsocas, A. & Rozé, C. Am. J. Physiol. 259, G198–G204 (1990).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Rose, C., Vargas, F., Facchinetti, P. et al. Characterization and inhibition of a cholecystokinin-inactivating serine peptidase. Nature 380, 403–409 (1996). https://doi.org/10.1038/380403a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/380403a0
This article is cited by
-
Gut bacterial metabolites modulate endoplasmic reticulum stress
Genome Biology (2021)
-
Cloning, Purification, and Characterization of Tripeptidyl Peptidase from Streptomyces herbaricolor TY-21
Applied Biochemistry and Biotechnology (2018)
-
The protein-interaction network with functional roles in tumorigenesis, neurodegeneration, and aging
Molecular and Cellular Biochemistry (2016)
-
Novel protein–protein interactions of TPPII, p53, and SIRT7
Molecular and Cellular Biochemistry (2015)
-
Inhibiting the breakdown of endogenous opioids and cannabinoids to alleviate pain
Nature Reviews Drug Discovery (2012)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.