C-terminal proteolysis of the avian 1,25-dihydroxyvitamin D3 receptor

Elizabeth A. Allegretto, J. Wesley Pike, Mark R. Haussler

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Exposure of the 60 kDa chick intestinal 1,25-dihydroxyvitamin D3 (1,25(OH)2D3) receptor to carboxypeptidase A resulted in a time dependent decrease in receptor hormone-binding; after 2 h, there was no detectable macro-molecular-bound 1,25(OH)2[3H]D3. Upon DNA-cellulose chromatography of this preparation, a 56 kDa protein adsorbed to the column and eluted as a function of para-chloromercuribenzene sulfonate (a sulfhydryl blocking reagent). The 56 kDa fragment was detected by anti-receptor monoclonal antibodies via immunoblot technology. The 1,25(OH)2[3H]D3 eluted in the fall through fractions of the column. Thus, cleavage of up to 40 amino acids from the carboxy-terminus of the 1,25(OH)2D3 receptor results in a protein which no longer binds to hormone, but retains its capacity to interact with DNA-cellulose and monoclonal antibody. These results represent novel biochemical evidence that allows us to orient the 1,25(OH)2D3 binding domain near the C-terminus of the receptor.

Original languageEnglish (US)
Pages (from-to)479-485
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Aug 31 1987

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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