Advertisement

Purification of the Cholecystokinin Receptor

  • Laurence J. Miller
Part of the Receptor Purification book series (RP, volume 1)

Abstract

Cholecystokinin (CCK) is a gastrointestinal and neural peptide hormone with physiological activities at multiple target tissues (Mutt, 1980). These include the classical targets of the gallbladder muscularis smooth muscle and the pancreatic acinar cell (for which this hormone was named “cholecystokinin-pancreozymin”) (Ivy and Oldberg, 1928; Jorpes and Mutt, 1966), as well as smooth muscle and some nerves at multiple levels of the digestive tract, including esophagus, stomach, intestine, and colon (Mutt, 1980). In addition, several potential activities have been described for this hormone at the levels of the brain and spinal cord (Dockray, 1982; Yaksh et al., 1982). Thus, there are multiple receptor subtypes from which to choose for CCK receptor purification.

Keywords

Pancreatic Acinar Cell Purification Scheme Smooth Muscle Tumor Guanine Nucleotide Binding Protein Affinity Label 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Baldwin, G. S., Chandler, R., Scanlon, D. B., and Weinstock, J. (1986) J. Biol. Chem. 261 12252–12257.PubMedGoogle Scholar
  2. Bayley, H. (1983) Lab Tech. Biochem. Molec. Biol. 12 1–163.CrossRefGoogle Scholar
  3. Bitar, K. N. and Makhlouf, G. M. (1982) Am. J. Physiol. 242 G400–G407.PubMedGoogle Scholar
  4. Bone, E. A. and Rosenzweig, S. A. (1988) Peptides 9 373–381.PubMedCrossRefGoogle Scholar
  5. Chang, R. S. L. and Lotti, V. J. (1986) Proc. Natl. Acad. Sci. USA 83 4923–4926.PubMedCrossRefGoogle Scholar
  6. Dockray, G. J. (1982) Br. Med. Bull. 38 253–258.PubMedGoogle Scholar
  7. Dourish, C. T. and Hill, D. R. (1987) Trends Pharmacol. Sci. 8 207–209.CrossRefGoogle Scholar
  8. Duong, L. T. and Vlasuk, G. P. (1988) FASEB J. 2 A1796.Google Scholar
  9. Eysselein, V. E., Reeve, J. R., Jr., Shively, J. E., Miller, C., and Walsh, J. H. (1984) Proc. Natl. Acad. Sci. USA 81 G565–G568.CrossRefGoogle Scholar
  10. Gaisano, H. Y., Klueppelberg, U. G., Pinon, D., Pfenning, M. A., Powers, S. P., and Miller, L. J. (1989) J. Clin. Invest. 83,321–325.PubMedCrossRefGoogle Scholar
  11. Hames, B. D. (1984) in Gel Electrophoresis of Proteins a Practical Approach (Hames, B. D. and Rickwood, D., eds.), IRL Press, Washington, DC.Google Scholar
  12. Hill, D. R., Shaw, T. M., and Woodruff, G. N. (1987) Neurosci. Lett. 79 286–289.PubMedCrossRefGoogle Scholar
  13. Hill, D. R., Shaw, T. M., and Woodruff, G. N. (1988) Neurosci. Lett. 89,133–139.PubMedCrossRefGoogle Scholar
  14. Hjelmeland, L. M. and Chrambach, A. (1984) in Membranes, Detergents, and Receptor Solubilization , vol. 1 (Venter, J.C. and Harrison, L. C., eds.), Alan R. Liss, Inc., New York, pp. 35–46.Google Scholar
  15. Innis, R. B. and Snyder, S. H. (1980) Proc. Natl. Acad. Sci. USA 77,6917–6921.PubMedCrossRefGoogle Scholar
  16. Ivy, A.C. and Oldberg, E.(1980) Am, J. Physiol. 86,599–613.Google Scholar
  17. Jorpes, E. and Mutt, V. (1966) Acta Physiol. Scand. 66,196–202.PubMedCrossRefGoogle Scholar
  18. Klueppelberg, U. G., Gaisano, H., Powers, S., and Miller, L. J. (1988a) Gastroenterology 94, A408.Google Scholar
  19. Lambert, M., Svoboda, M., Furnelle, J., and Christophe, J. (1985) Eur. J. Biochem. 147, 611–617.PubMedCrossRefGoogle Scholar
  20. Madison, L. D., Rosenzweig, S. A., and Jamieson, J. D. (1984) J. Biol. Chem. 259, 14818–14823.PubMedGoogle Scholar
  21. Maton, P. N., Jensen, R. T., and Gardner, J. D. (1986) Horm. Metabol. Res. 18 2–9.CrossRefGoogle Scholar
  22. Matsumoto, M., Park, J., and Yamada, T. (1987) Am. J. Physiol. 252, G143–C147.PubMedGoogle Scholar
  23. Merritt, J. E., Taylor, C. W., Rubin, R. P., and Putney, Jr., J. W. (1986) Biochem. J. 236, 337–343.PubMedGoogle Scholar
  24. Miller, L. J. (1984) Am. J. Physiol. 247, G402–G410.PubMedGoogle Scholar
  25. Miller, L. J., Rosenzweig, S. A., and Jamieson, J. D. (1981) J. Biol. Chem. 256,12417–12423.PubMedGoogle Scholar
  26. Moran, T. H., Robinson, P., Goldrich, M. S., and McHugh, P. (1986) Brain Res. 362,175–179.PubMedCrossRefGoogle Scholar
  27. Mu, F.-T., Baldwin, G., Weinstock, J., Stockman, D., and Toh, B. H. (1987) Proc. Natl. Acad. Sci. USA 84 2698–2702.PubMedCrossRefGoogle Scholar
  28. Mutt, V. (1980) in Gastrointestinal Hormones (Glass, G. B. J., ed.), Raven Press, New York, pp. 169–221.Google Scholar
  29. Ondetti, M. A., Rubin, B., Engel, S. L., Pluscec, J., and Sheehan, J. T. (1970) Am. J. Dig. Dis. 15,149–156.PubMedCrossRefGoogle Scholar
  30. Pearson, R. K. and Miller, L. J. (1987) J. Bio. Chem. 262 (2), 869–876.Google Scholar
  31. Pearson, R. K., Hadac, E. M., and Miller, L. J. (1986) Gastroenterology 90 1985–1991.PubMedGoogle Scholar
  32. Pearson, R. K., Miller, J. J., Powers, S. P., and Hadac, E. M. (1987a) Pancreas 2 (1), 79–84.CrossRefGoogle Scholar
  33. Pearson, R. K., Powers, S. P., Hadac, E. M., Gaisano, H., and Miller, L. J. (1987b) Biochem. Biophys. Res. Commun. 147, 346–353.CrossRefGoogle Scholar
  34. Pearson, R. K., Miller, L. J., Hadac, E. M., and Powers, S. P. (1987c) J. Biol. Chem. 262,13850–13856.Google Scholar
  35. Pilch, P. F. and Czech, M. P. (1984) in Membranes, Detergents,and Receptor Solubilization, vol. I (Venter, J. C. and Harrison, L. C., eds.), Alan R. Liss, Inc., New York, pp. 161–175.Google Scholar
  36. Powers, S. P., Fourmy, D., Gaisano, H., and Miller, L. J. (1988) J. Biol. Chem. 263, 5295–5300.PubMedGoogle Scholar
  37. Rosenzweig, S. A., Miller, L. J., and Jamieson, J. D. (1982) Fed. Proc. 41 1183.Google Scholar
  38. Rosenzweig, S. A., Miller, L. J., and Jamieson, J. D. (1983) J. Cell. Biol. 96,1288–1297.PubMedCrossRefGoogle Scholar
  39. Sakamoto, C., Goldfine, I. D., and Williams, J. A. (1983) J. Biol. Chem. 258,12707–12711.PubMedGoogle Scholar
  40. Sakamoto, C., Williams, J. A., and Goldfine, I. D. (1984) Biochem. Biophys. Res. Commun. 124, 497–502.PubMedCrossRefGoogle Scholar
  41. Schjoldager, B., Powers, S. P., and Miller, L. J. (1988) Am. J. Physiol. 255, G579–G586.PubMedGoogle Scholar
  42. Segrest, J. P., Jackson, R. L., Andrews, E. P., and Marchesi, V. T. (1971) Biochem. Biophys. Res. Commun. 44 390–395.PubMedCrossRefGoogle Scholar
  43. Shaw, M. J., Hadac, E. M., and Miller, L. J. (1987) J. Biol. Chem. 262,14313–14318.PubMedGoogle Scholar
  44. Soll, A. H., Amirian, D. A., Thomas, L. P., Reedy, T. J., and Elashoff, J. D. (1984) J. Clin. Invest. 73,1434–1447. PubMedCrossRefGoogle Scholar
  45. Steigerwalt, R. W., Goldfine, I. D., and Williams, J. A. (1984) Am. J. Physiol. 247, G709–714.PubMedGoogle Scholar
  46. Svoboda, M., Lambert, M., Furnelle, J., and Christophe, J. (1982) Regul. Pept. 4,163–172.PubMedCrossRefGoogle Scholar
  47. Szecowka, J., Goldfine, I. D., and Williams, J. A. (1985) Regul. Pept. 10 71–83.PubMedCrossRefGoogle Scholar
  48. Villanueva, M. L., Collins, S. M., Jensen, R. T., and Gardner, J. D. (1982) Am. J. Physiol. 242, G416–G422.PubMedGoogle Scholar
  49. Von Schrenck, T., Moran, T. H., Heinz-Erian, P., Gardner, J. P., and Jensen, R. T. (1988) Am. J. Physiol. 255, G512–G521.Google Scholar
  50. Wank, S. A., Gardner, J. P., and Jensen, R. T. (1988) Biomed. Res. Suppl. 1,186.Google Scholar
  51. Williams, J. A. and McChesney, D. J. (1987) Regul. Pept. 18 109–117.PubMedCrossRefGoogle Scholar
  52. Yaksh, T. L., Abay, E. O., and Go, V. L. W. (1982) Brain Res. 242, 279–290.PubMedCrossRefGoogle Scholar
  53. Zahidi, A., Fourmy, D., Darbon, J.-M., Pradayrol, L., Scemama, J.-L., and Ribet, A. (1986) Regul. Pept. 15, 25–36.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Laurence J. Miller

There are no affiliations available

Personalised recommendations