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Characterization of Cell-Surface Receptors for Calcitonin in Hormone-Responsive Cancer Cells

  • J. M. Moseley
  • D. M. Findlay
  • J. J. Gorman
  • V. P. Michelangeli
  • T. J. Martin
Part of the Methodological Surveys in Biochemistry and Analysis book series (MSBA, volume 13)

Abstract

Calcitonin (CT) binding to human breast cancer cells is poorly reversible, and brief exposure causes sustained activation of adenyl cyclase. Receptor-bound CT appears to be internalized and degraded before release from the cells, akin to epidermal growth factor (EGF) behaviour. With an enzymic coupling reaction a photoaffinity-labelled salmon CT derivative has been prepared. After binding and UV treatment, an 85,000 mol. wt. component of the CT receptor has been identified electrophoretically. Experiments with lectins and other agents have indicated that the component is rich in N-acetylglucosamine, and it may represent a distinct sub-class of CT receptors, not necessarily connected to adenyl cyclase activation.

Keywords

Adenylate Cyclase Human Lung Cancer Cell Line Calcitonin Receptor PHOTOAFFINITY Labelling Late Cyclase 
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.

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Copyright information

© Plenum Press, New York 1984

Authors and Affiliations

  • J. M. Moseley
    • 1
  • D. M. Findlay
    • 1
  • J. J. Gorman
    • 2
  • V. P. Michelangeli
    • 1
  • T. J. Martin
    • 1
  1. 1.Department of Medicine, Repatriation General HospitalUniversity of MelbourneWest HeidelbergAustralia
  2. 2.Physiology and MedicineHoward Florey Institute of ExperimentalParkvilleAustralia

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