Sorbitol-induced apoptosis of human leukemia is mediated by caspase activation and cytochrome c release

Gabriella Marfè, Emanuela Morgante, Carla Di Stefano, Livia Di Renzo, Luisa De Martino, Giuseppe Iovane, Matteo Antonio Russo, Paola Sinibaldi-Salimei

Research output: Contribution to journalArticlepeer-review

Abstract

It has been reported that sorbitol induces apoptosis in several cancer cell lines. However, the molecular mechanism underlying the sorbitol-induced apoptotic process is not yet clearly understood. In the present study, the intracellular signaling pathways of sorbitol-induced apoptosis in human K562 cells were investigated using both morphological analysis and DNA fragmentation technique. In this study, we demonstrated that sorbitol-induced apoptosis in human K562 cells is a concentration- and time-dependent manner. This sorbitol-induced apoptosis in human K562 cells was also accompanied by the up-regulation of Bax, and down-regulation of p-Bcl-2, but no effect on the levels of Bcl-XL. Moreover, the sorbitol treatment resulted in a significant reduction of mitochondria membrane potential, increase in the release of mitochondrial cytochrome c (cyt c), and activation of caspase 3. Furthermore, treatment with caspase 3 inhibitor (z-DEVD-fmk) was capable of preventing the sorbitol-induced caspase 3 activity and cell death. These results clearly demonstrate that the induction of apoptosis by sorbitol involves multiple cellular/molecular pathways and strongly suggest that pro- and anti-apoptotic Bcl-2 family proteins, mitochondrial membrane potential, mitochondrial cyt c, and caspase 3, they all participate in sorbitol-induced apoptotic process in human K562 cells.

Original languageEnglish
Pages (from-to)371-377
Number of pages7
JournalArchives of Toxicology
Volume82
Issue number6
DOIs
Publication statusPublished - Jun 2008

Keywords

  • Apoptosis
  • Bcl-2
  • Bcl-xL
  • Caspases
  • Sorbitol

ASJC Scopus subject areas

  • Health, Toxicology and Mutagenesis
  • Toxicology

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