The Role of Heat Shock Proteins and Autophagy in Mechanisms Underlying Effects of Sulforaphane on Doxorubicin-Induced Toxicity in HEK293 Cells.
Level 5 - mechanism / opinion, no new human data
In vitro bench research (HEK293 cell culture)
PubMed 37294118 · doi:10.33549/physiolres.935107
What was done
Human embryonic kidney cells (HEK293) were treated with doxorubicin (DOX), sulforaphane (SFN), or their combination to assess the role of heat shock proteins (HSP60, HSP40), redox signaling (Nrf-2, superoxide dismutase activities), and autophagy markers (LC3A/B-II, Atg5, Atg12) in mediating SFN-induced cytoprotection against DOX toxicity.
What was found
The abstract reports directional findings without numerical values. SFN significantly reduced DOX cytotoxicity. In DOX-exposed cells, SFN co-treatment was associated with up-regulated Nrf-2 and HSP60 protein levels, whereas HSP40 increased with SFN alone but not during co-exposure. SFN also reversed DOX-induced suppression of superoxide dismutase (SOD) activities and reversed DOX-associated up-regulation of autophagy markers (LC3A/B-II, Atg5, and Atg12).
Why it matters
The study suggests HSP60 up-regulation, Nrf-2 activation, and autophagy modulation are involved in sulforaphane's ability to protect kidney cells from anthracycline-mediated oxidative damage.
Limits
This is an in vitro study conducted exclusively in a single immortalized human embryonic kidney cell line (HEK293), precluding direct translation to in vivo pharmacokinetics or clinical nephroprotection. The abstract does not report specific drug concentrations, exposure durations, sample sizes (replicates), or exact quantitative effect sizes.
Cited by
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