Up-regulation of human PNPase mRNA by beta-interferon has no effect on protein level in melanoma cell lines

Acta Biochim Pol. 2006;53(1):179-88. Epub 2006 Feb 26.

Abstract

Human mitochondrial polynucleotide phosphorylase (hPNPase) is an exoribonuclease localized in mitochondria. The exact physiological function of this enzyme is unknown. Recent studies have revealed the existence of a relationship between induction of hPNPase mRNA and both cellular senescence and growth arrest of melanoma cells following beta-interferon treatment. The aim of this study was to verify whether the augmented hPNPase mRNA level results in increase of the protein level. In several cell lines established from five metastatic melanoma patients we did not find any such correlation. However, an elevated level of hPNPase protein was observed in interferon-induced HeLa and Jurkat cells. This increase was correlated with a slight shortening of poly(A) tails of mitochondrial ND3 transcript.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cell Line, Tumor
  • Exoribonucleases / metabolism
  • Gene Expression Regulation, Neoplastic*
  • HeLa Cells
  • Humans
  • Interferon-beta / metabolism*
  • Jurkat Cells
  • Melanoma / metabolism*
  • Mitochondria / enzymology*
  • Molecular Sequence Data
  • Polyribonucleotide Nucleotidyltransferase / biosynthesis*
  • RNA, Messenger / metabolism*
  • Up-Regulation*

Substances

  • RNA, Messenger
  • Interferon-beta
  • Polyribonucleotide Nucleotidyltransferase
  • Exoribonucleases