Endoplasmic Reticulum Chaperones at the Tumor Cell Surface and in the Extracellular Space

Brychtová, Veronika; Vojtěšek, Bořivoj

doi:10.14735/amko20164s25

Cited by 3 publications

(1 citation statement)

References 61 publications

(76 reference statements)

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“…The role of extracellular Hsp90 has been previously shown to be important in migration and invasion of tumor cells [ 16 , 17 , 20 ]. Grp94 has also been shown to have a tumor-specific cell surface expression [ 15 , 36 ]. Inhibition of extracellular Hsp90 using cell-impermeable Hsp90 inhibitor FITC- Geldanamycin [ 21 ] has no apparent effect on the growth of the parasite in the axenic culture conditions ( S6 Fig ).…”

Section: Discussionmentioning

confidence: 99%

A secreted Heat shock protein 90 of Trichomonas vaginalis

et al. 2018

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Trichomonas vaginalis is a causative agent of Trichomoniasis, a leading non-viral sexually transmitted disease worldwide. In the current study, we show Heat shock protein 90 is essential for its growth. Upon genomic analysis of the parasite, it was found to possess seven ORFs which could potentially encode Hsp90 isoforms. We identified a cytosolic Hsp90 homolog, four homologs which can align to truncated cytosolic Hsp90 gene products along with two Grp94 homologs (ER isoform of Hsp90). However, both Grp94 orthologs lacked an ER retention motif. In cancer cells, it is very well established that Hsp90 is secreted and regulates key clients involved in metastases, migration, and invasion. Since Trichomonas Grp94 lacks ER retention motif, we examined the possibility of its secretion. By using cell biology and biochemical approaches we show that the Grp94 isoform of Hsp90 is secreted by the parasite by the classical ER-Golgi pathway. This is the first report of a genome encoded secreted Hsp90 in a clinically important parasitic protozoan.

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