Abstract
Small Heat shock proteins (sHsp) are a group of chaperone proteins. Under conditions of stress, the expression of sHsp is increased. Therefore, they are implicated in the pathogenesis of various autoimmune-mediated disorders and cancer. The purpose of this study was to analyze sHsp expression in exosomes from patients with gynecologic cancers and correlate these results with markers of cytotoxic immune response. The study group included patients with ovarian cancer, endometrial cancer, and patients with endometriosis. The levels of sHsps and cytotoxic markers were analyzed in serum, peritoneal fluid and exosomes using ELISA method. We found the highest levels of sHsp in exosomes from patients with ovarian cancer, but they were also elevated in patients with endometrial cancer and endometriosis. Moreover, we identified the presence of small Hsps in serum and peritoneal fluid in all study groups, but again the highest level was in patients with ovarian cancer. Small Hsps expression levels were positively correlated with markers of cytotoxic immune response.
Highlights
Small heat shock proteins are a diverse group of chaperone proteins with a molecular mass of 15–30 kDa that are conserved in prokaryotes and eukaryotes[1]
We found a significant difference between endometrial and ovarian cancer in the activity of Na+/K+- ATPase (8738 ± 4266 vs. 4842 ± 3651, p = 0.029)
The results suggest increased levels of Small Heat shock proteins (sHsp) in exosomes, most spectacularly in patients with ovarian cancer, and in patients with endometrial cancer or endometriosis
Summary
Small heat shock proteins (sHSP) are a diverse group of chaperone proteins with a molecular mass of 15–30 kDa that are conserved in prokaryotes and eukaryotes[1]. The presence of evolutionary conserved alpha-crystallin domain distinguishes all sHsp and alpha-crystallins[2]. Small Hsps are involved in a number of essential cellular functions. Most importantly, they bind to misfolded proteins to prevent irreversible aggregation and aid in refolding to a competent state[4,5]. The best characterized proteins, including Hsp[27], alphacrystallin, alpha-B crystallin, Hsp[22] and Hsp16.2, have a strong anti-aggregation chaperone activity[6]. A role for sHsp, mainly Hsp[27] and alpha-B crystallin in the presentation of oxidized proteins to the proteasome degradation machinery has been suggested[12]. Several studies described the role of sHsps as extracellular signals[23]
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