HSP70 Inhibition Alters Extracellular Vesicles Activity In Vitro
DOI:
https://doi.org/10.56532/mjsat.v6i3.645Keywords:
exosome, cancer, heat shock proteinAbstract
Heat shock protein 70 (HSP70) is a stress-induced molecular chaperone that is frequently overexpressed in many cancers, including colorectal cancer (CRC). In addition to its intracellular functions, HSP70 has been detected in extracellular vesicles (EVs) as well. EVs are nanovesicles that are released into the extracellular space and are known to promote cancer cell proliferation and migration. However, the role of HSP70 in influencing EV function remains unclear. This study examined the effects of HSP70 inhibition on EVs derived from the HT-29 colorectal cancer cell line. The HSP70 inhibitor VER-155008 was used to suppress HSP70 activity. Flow cytometric analysis confirmed that the isolated EVs expressed the characteristic surface markers CD63, CD81, and CD9. Wound healing assays showed a marked reduction in cell migration following VER-155008-EV treatment at both 24 and 48 hours. These findings suggest that inhibition of HSP70 alters the properties of EVs and may influence their ability to support tumor cell migration. This study provides insight into the potential role of HSP70 in modulating EV function in CRC.
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