Constitutive degradation of PML/RARalpha through the proteasome pathway mediates retinoic acid resistance

Blood. 1999 Mar 1;93(5):1477-81.

Abstract

PML/RARalpha is the leukemogenetic protein of acute promyelocytic leukemia (APL). Treatment with retinoic acid (RA) induces degradation of PML/RARalpha, differentiation of leukaemic blasts, and disease remission. However, RA resistance arises during RA treatment of APL patients. To investigate the phenomenon of RA resistance in APL, we generated RA-resistant sublines from APL-derived NB4 cells. The NB4.007/6 RA-resistant subline does not express the PML/RARalpha protein, although its mRNA is detectable at levels comparable to those of the parental cell line. In vitro degradation assays showed that the half-life of PML/RARalpha is less than 30 minutes in NB4.007/6 and longer than 3 hours in NB4. Treatment of NB4.007/6 cells with the proteasome inhibitors LLnL and lactacystin partially restored PML/RARalpha protein expression and resulted in a partial release of the RA-resistant phenotype. Similarly, forced expression of PML/RARalpha, but not RARalpha, into the NB4/007.6 cells restored sensitivity to RA treatment to levels comparable to those of the NB4 cells. These results indicate that constitutive degradation of PML/RARalpha protein may lead to RA resistance and that PML/RARalpha expression is crucial to convey RA sensitivity to APL cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antineoplastic Agents / pharmacology*
  • Cysteine Endopeptidases / metabolism*
  • Drug Resistance, Neoplasm*
  • Humans
  • Leukemia, Promyelocytic, Acute / metabolism*
  • Multienzyme Complexes / metabolism*
  • Neoplasm Proteins / metabolism*
  • Oncogene Proteins, Fusion / metabolism*
  • Proteasome Endopeptidase Complex
  • Tretinoin / pharmacology*

Substances

  • Antineoplastic Agents
  • Multienzyme Complexes
  • Neoplasm Proteins
  • Oncogene Proteins, Fusion
  • promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein
  • Tretinoin
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex