Multimedialna platforma wiedzy medycznej Internetowa Księgarnia Medyczna Kalendarium Konferencji
Ginekologia Polska
MENU
Shortcuts Submit an article Author Guidelines Ahead Of Print Reviewers 2023

open access

Vol 92, No 12 (2021)
Research paper
Published online: 2021-05-21
View PDF Download PDF file
Get Citation

Heat shock protein 27 (HSP27) in patients with ovarian cancer

Piotr Bodzek1, Aleksandra Damasiewicz-Bodzek1, Iwona Janosz1, Lukasz Witek1, Anita Olejek1
DOI: 10.5603/GP.a2021.0061
·
Pubmed: 34105741
·
Ginekol Pol 2021;92(12):837-843.
Affiliations
  1. Department of Gynaecology, Obstetrics and Oncological Gynaecology, Faculty of Medical Sciences in Zabrze Medical University of Silesia, Bytom, Poland

open access

Vol 92, No 12 (2021)
ORIGINAL PAPERS Gynecology
Published online: 2021-05-21

Abstract

Objectives: Ovarian cancer remains a very common cause of death among women worldwide. The cause is to be found in too late of a diagnostic process and therapeutic difficulties The presence of heat shock proteins in the serum of ovarian cancer patients is still a new area of study. It is necessary to continue studies on the possibilities for using these markers to predict a patient’s response to a specific therapy and to monitor treatment progress.
Material and methods: The study included 52 women with ovarian cancer, hospitalised at the Department of Obstetrics, Gynaecology and Oncological Gynaecology, Medical University of Silesia. The control group consisted of 25 healthy women. The levels of HSP27 in the studied sera were determined by an immunoenzymatic method (ELISA).
Results: The mean concentration of HSP27 in the group of patients with ovarian cancer was significantly higher than in the control group of healthy women. We have shown that mean HSP27 levels in ovarian cancer patients increase with tumour progression and further depend on the clinical stage of the disease (FIGO). Positivity values analysis revealed in all clinical stages of ovarian cancer, excluding stage 1, it was significantly higher than in the control group, and at the 4th stage, it is significantly higher than at the 1st, 2nd, and 3rd stages. However, both for the untreated patients and those patients after chemotherapy, the mean HSP27 levels were significantly higher than in the control group.
Conclusions: Our studies indicate a significant contribution of HSP27 to the pathogenesis of ovarian cancer. It seems that serum HSP27 can be a marker for this cancer’s development, and a marker for the clinical stage.

Abstract

Objectives: Ovarian cancer remains a very common cause of death among women worldwide. The cause is to be found in too late of a diagnostic process and therapeutic difficulties The presence of heat shock proteins in the serum of ovarian cancer patients is still a new area of study. It is necessary to continue studies on the possibilities for using these markers to predict a patient’s response to a specific therapy and to monitor treatment progress.
Material and methods: The study included 52 women with ovarian cancer, hospitalised at the Department of Obstetrics, Gynaecology and Oncological Gynaecology, Medical University of Silesia. The control group consisted of 25 healthy women. The levels of HSP27 in the studied sera were determined by an immunoenzymatic method (ELISA).
Results: The mean concentration of HSP27 in the group of patients with ovarian cancer was significantly higher than in the control group of healthy women. We have shown that mean HSP27 levels in ovarian cancer patients increase with tumour progression and further depend on the clinical stage of the disease (FIGO). Positivity values analysis revealed in all clinical stages of ovarian cancer, excluding stage 1, it was significantly higher than in the control group, and at the 4th stage, it is significantly higher than at the 1st, 2nd, and 3rd stages. However, both for the untreated patients and those patients after chemotherapy, the mean HSP27 levels were significantly higher than in the control group.
Conclusions: Our studies indicate a significant contribution of HSP27 to the pathogenesis of ovarian cancer. It seems that serum HSP27 can be a marker for this cancer’s development, and a marker for the clinical stage.

Full Text:

View PDF Download PDF file
Get Citation

Keywords

ovarian cancer; heat shock protein; HSP27

About this article
Title

Heat shock protein 27 (HSP27) in patients with ovarian cancer

Journal

Ginekologia Polska

Issue

Vol 92, No 12 (2021)

Article type

Research paper

Pages

837-843

Published online

2021-05-21

Page views

6904

Article views/downloads

819

DOI

10.5603/GP.a2021.0061

Pubmed

34105741

Bibliographic record

Ginekol Pol 2021;92(12):837-843.

Keywords

ovarian cancer
heat shock protein
HSP27

Authors

Piotr Bodzek
Aleksandra Damasiewicz-Bodzek
Iwona Janosz
Lukasz Witek
Anita Olejek

References (56)
  1. Sienko J, Gaj P, Czajkowski K, et al. Peroxiredoxin-5 is a negative survival predictor in ovarian cancer. Ginekol Pol. 2019; 90(1): 1–6.
    CrossRefPubMed
  2. Zhao X, He M. Comprehensive pathway-related genes signature for prognosis and recurrence of ovarian cancer. PeerJ. 2020; 8: e10437.
    CrossRefPubMed
  3. Mielczarek-Palacz A, Sikora J, Kondera-Anasz Z, et al. The immune complex p53 protein/anti-p53 autoantibodies in the pathogenesis of ovarian serous carcinoma. Ginekol Pol. 2020; 91(9): 519–253.
    CrossRefPubMed
  4. Hoter A, Naim HY. Heat shock proteins and ovarian cancer: important roles and therapeutic opportunities. Cancers (Basel). 2019; 11(9): 1389.
    CrossRefPubMed
  5. Wu J, Liu T, Rios Z, et al. Heat shock proteins and cancer. Trends Pharmacol Sci. 2017; 38(3): 226–256.
    CrossRefPubMed
  6. Liu Z, Liu Y, Long Y, et al. Role of HSP27 in the multidrug sensitivity and resistance of colon cancer cells. Oncol Lett. 2020; 19(3): 2021–2027.
    CrossRefPubMed
  7. Wantoch von Rekowski K, König P, Henze S, et al. Insight into cisplatin-resistance signaling of W1 ovarian cancer cells emerges mTOR and HSP27 as targets for sensitization strategies. Int J Mol Sci. 2020; 21(23): 9240.
    CrossRefPubMed
  8. Sreedhar AS, Csermely P. Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy: a comprehensive review. Pharmacol Ther. 2004; 101(3): 227–257.
    CrossRefPubMed
  9. Nappi L, Aguda AH, Nakouzi NAl, et al. Ivermectin inhibits HSP27 and potentiates efficacy of oncogene targeting in tumor models. J Clin Invest. 2020; 130(2): 699–714.
    CrossRefPubMed
  10. Costa-Beber LC, Hirsch GE, Heck TG, et al. Chaperone duality: the role of extracellular and intracellular HSP70 as a biomarker of endothelial dysfunction in the development of atherosclerosis. Arch Physiol Biochem. 2020 [Epub ahead of print]: 1–8.
    CrossRefPubMed
  11. Taha EA, Ono K, Eguchi T. Roles of extracellular HSPs as biomarkers in immune surveillance and immune evasion. Int J Mol Sci. 2019; 20(18): 4588.
    CrossRefPubMed
  12. Zhang Z, Jing J, Ye Y, et al. Characterization of the dual functional effects of heat shock proteins (HSPs) in cancer hallmarks to aid development of HSP inhibitors. Genome Med. 2020; 12(1): 101.
    CrossRefPubMed
  13. Chatterjee S, Burns TF. Targeting heat shock proteins in cancer: a promising therapeutic approach. Int J Mol Sci. 2017; 18(9).
    CrossRefPubMed
  14. Dias TR, Samanta L, Agarwal A, et al. Proteomic signatures reveal differences in stress response, antioxidant defense and proteasomal activity in fertile men with high seminal ROS levels. Int J Mol Sci. 2019; 20(1): 203.
    CrossRefPubMed
  15. Patinen T, Adinolfi S, Cortés CC, et al. Regulation of stress signaling pathways by protein lipoxidation. Redox Biol. 2019; 23: 101114.
    CrossRefPubMed
  16. Saini J, Sharma PK. Clinical, prognostic and therapeutic significance of heat shock proteins in cancer. Curr Drug Targets. 2018; 19(13): 1478–1490.
    CrossRefPubMed
  17. Njoku K, Chiasserini D, Whetton AD, et al. Proteomic biomarkers for the detection of endometrial cancer. Cancers (Basel). 2019; 11(10): 1572.
    CrossRefPubMed
  18. Jin Y, Kim SC, Kim HJ, et al. Use of protein-based biomarkers of exfoliated cervical cells for primary screening of cervical cancer. Arch Pharm Res. 2018; 41(4): 438–449.
    CrossRefPubMed
  19. Heinrich JC, Donakonda S, Haupt VJ, et al. New HSP27 inhibitors efficiently suppress drug resistance development in cancer cells. Oncotarget. 2016; 7(42): 68156–68169.
    CrossRefPubMed
  20. Korneeva I, Bongiovanni AM, Girotra M, et al. Serum antibodies to the 27-kd heat shock protein in women with gynecologic cancers. Am J Obstet Gynecol. 2000; 183(1): 18–21.
    CrossRefPubMed
  21. Parcellier A, Schmitt E, Brunet M, et al. Small heat shock proteins HSP27 and alphaB-crystallin: cytoprotective and oncogenic functions. Antioxid Redox Signal. 2005; 7(3–4): 404–413.
    CrossRefPubMed
  22. Zhao M, Shen F, Yin YX, et al. Increased expression of heat shock protein 27 correlates with peritoneal metastasis in epithelial ovarian cancer. Reprod Sci. 2012; 19(7): 748–753.
    CrossRefPubMed
  23. Olejek A, Damasiewicz-Bodzek A, Bodzek P, et al. Concentrations of antibodies against heat shock protein 27 in the sera of women with ovarian carcinoma. Int J Gynecol Cancer. 2009; 19(9): 1516–1520.
    CrossRefPubMed
  24. Korneeva I, Bongiovanni AM, Girotra M, et al. IgA antibodies to the 27-kDa heat-shock protein in the genital tracts of women with gynecologic cancers. Int J Cancer. 2000; 87(6): 824–828, doi: 10.1002/1097-0215(20000915)87:6<824::aid-ijc11>3.0.co;2-k.
    PubMed
  25. Grotegut P, Hoerdemann PJ, Reinehr S, et al. Heat shock protein 27 injection leads to caspase activation in the visual pathway and retinal T-cell response. Int J Mol Sci. 2021; 22(2): 513.
    CrossRefPubMed
  26. Korneeva I, Caputo TA, Witkin SS. Cell-free 27 kDa heat shock protein (hsp27) and hsp27-cytochrome c complexes in the cervix of women with ovarian or endometrial cancer. Int J Cancer. 2002; 102(5): 483–486.
    CrossRefPubMed
  27. Wang S, Zhang X, Wang H, et al. Heat shock protein 27 enhances SUMOylation of heat shock protein B8 to accelerate the progression of breast cancer. Am J Pathol. 2020; 190(12): 2464–2477.
    CrossRefPubMed
  28. Zhang S, Zhang Xq, Huang Sl, et al. The effects of HSP27 on gemcitabine-resistant pancreatic cancer cell line through snail. Pancreas. 2015; 44(7): 1121–1129.
    CrossRefPubMed
  29. Didelot C, Lanneau D, Brunet M, et al. Anti-cancer therapeutic approaches based on intracellular and extracellular heat shock proteins. Curr Med Chem. 2007; 14(27): 2839–2847.
    CrossRefPubMed
  30. Arispe N, Doh M, Simakova O, et al. Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability. FASEB J. 2004; 18(14): 1636–1645.
    CrossRefPubMed
  31. Mambula SS, Calderwood SK. Heat induced release of Hsp70 from prostate carcinoma cells involves both active secretion and passive release from necrotic cells. Int J Hyperthermia. 2006; 22(7): 575–585.
    CrossRefPubMed
  32. Sidera K, Patsavoudi E. Extracellular HSP90: an emerging target for cancer therapy. Current Signal Transduction Therapy. 2009; 4(1): 51–58.
    CrossRef
  33. Tsutsumi S, Neckers L. Extracellular heat shock protein 90: a role for a molecular chaperone in cell motility and cancer metastasis. Cancer Sci. 2007; 98(10): 1536–1539.
    CrossRefPubMed
  34. Li W, Sahu D, Tsen F. Secreted heat shock protein-90 (Hsp90) in wound healing and cancer. Biochim Biophys Acta. 2012; 1823(3): 730–741.
    CrossRefPubMed
  35. de Azevedo-Santos AP, Rocha MC, Guimarães SJ, et al. Could increased expression of Hsp27, an "anti-inflammatory" chaperone, contribute to the monocyte-derived dendritic cell bias towards tolerance induction in breast cancer patients? Mediators Inflamm. 2019; 2019: 8346930.
    CrossRefPubMed
  36. Vulczak A, Catalão CH, Freitas LA, et al. HSP-target of therapeutic agents in sepsis treatment. Int J Mol Sci. 2019; 20(17): 4255.
    CrossRefPubMed
  37. Geisler JP, Tammela JE, Manahan KJ, et al. HSP27 in patients with ovarian carcinoma: still an independent prognostic indicator at 60 months follow-up. Eur J Gynaecol Oncol. 2004; 25(2): 165–168.
    PubMed
  38. Li KC, Heo K, Ambade N, et al. Reduced expression of HSP27 following HAD-B treatment is associated with Her2 downregulation in NIH:OVCAR-3 human ovarian cancer cells. Mol Med Rep. 2015; 12(3): 3787–3794.
    CrossRefPubMed
  39. Elpek GO, Karaveli S, Simşek T, et al. Expression of heat-shock proteins hsp27, hsp70 and hsp90 in malignant epithelial tumour of the ovaries. APMIS. 2003; 111(4): 523–530.
    CrossRefPubMed
  40. Ioachin E. Immunohistochemical tumour markers in endometrial carcinoma. Eur J Gynaecol Oncol. 2005; 26(4): 363–371.
    PubMed
  41. Ajalyakeen H, Almohareb M, Al-Assaf M. Overexpression of heat shock protein 27 (HSP-27) is associated with bad prognosis in oral squamous cell carcinoma. Dent Med Probl. 2020; 57(3): 227–231.
    CrossRefPubMed
  42. Yuan Q, Cai HQ, Zhong Yi, et al. Overexpression of IGFBP2 mRNA predicts poor survival in patients with glioblastoma. Biosci Rep. 2019; 39(6): BSR20190045.
    CrossRefPubMed
  43. Soldes OS, Kuick RD, Thompson IA, et al. Differential expression of Hsp27 in normal oesophagus, Barrett's metaplasia and oesophageal adenocarcinomas. Br J Cancer. 1999; 79(3–4): 595–603.
    CrossRefPubMed
  44. Lambot MA, Peny MO, Fayt I, et al. Overexpression of 27-kDa heat shock protein relates to poor histological differentiation in human oesophageal squamous cell carcinoma. Histopathology. 2000; 36(4): 326–330.
    CrossRefPubMed
  45. Ciocca DR, Calderwood SK. Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications. Cell Stress Chaperones. 2005; 10(2): 86–103.
    CrossRefPubMed
  46. Arts HJ, Hollema H, Lemstra W, et al. Heat-shock-protein-27 (hsp27) expression in ovarian carcinoma: relation in response to chemotherapy and prognosis. Int J Cancer. 1999; 84(3): 234–238, doi: 10.1002/(sici)1097-0215(19990621)84:3<234::aid-ijc6>3.0.co;2-9.
    PubMed
  47. Yamamoto K, Okamoto A, Isonishi S, et al. Heat shock protein 27 was up-regulated in cisplatin resistant human ovarian tumor cell line and associated with the cisplatin resistance. Cancer Lett. 2001; 168(2): 173–181.
    CrossRefPubMed
  48. Tanaka Y, Fujiwara K, Tanaka H, et al. Paclitaxel inhibits expression of heat shock protein 27 in ovarian and uterine cancer cells. Int J Gynecol Cancer. 2004; 14(4): 616–620.
    CrossRefPubMed
  49. Moutaoufik MT, Tanguay RM. Analysis of insect nuclear small heat shock proteins and interacting proteins. Cell Stress Chaperones. 2021; 26(1): 265–274.
    CrossRefPubMed
  50. Beere HM. Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways. J Clin Invest. 2005; 115(10): 2633–2639.
    CrossRefPubMed
  51. Qi Z, Shen L, Zhou H, et al. Phosphorylation of heat shock protein 27 antagonizes TNF-α induced HeLa cell apoptosis via regulating TAK1 ubiquitination and activation of p38 and ERK signaling. Cell Signal. 2014; 26(7): 1616–1625.
    CrossRefPubMed
  52. Gawad A, Ptak-Belowska A, Brzozowski T, et al. Monocytes and vascular endothelial cells apoptosis. Role of p-HSP27. J Physiol Pharmacol. 2009; 60(4): 55–61.
    PubMed
  53. Piura B, Rabinovich A, Yavelsky V, et al. Heat shock proteins and malignancies of the female genital tract. Harefuah. 2002; 141(11): 969–972.
    PubMed
  54. Könsgen D, Klinkmann G, Kaul A, et al. Soluble heat-shock protein 27 in blood serum is a non-invasive prognostic biomarker for ovarian cancer. Eur J Obstet Gynecol Reprod Biol. 2020; 255: 154–159.
    CrossRefPubMed
  55. Annunziata CM, Kleinberg L, Davidson B, et al. BAG-4/SODD and associated antiapoptotic proteins are linked to aggressiveness of epithelial ovarian cancer. Clin Cancer Res. 2007; 13(22 Pt 1): 6585–6592.
    CrossRefPubMed
  56. De AK, Roach SE. Detection of the soluble heat shock protein 27 (hsp27) in human serum by an ELISA. J Immunoassay Immunochem. 2004; 25(2): 159–170.
    CrossRefPubMed

Regulations

Important: This website uses cookies. More >>

The cookies allow us to identify your computer and find out details about your last visit. They remembering whether you've visited the site before, so that you remain logged in - or to help us work out how many new website visitors we get each month. Most internet browsers accept cookies automatically, but you can change the settings of your browser to erase cookies or prevent automatic acceptance if you prefer.

By VM Media Group sp. z o.o., ul. Świętokrzyska 73, 80–180 Gdańsk
tel.:+48 58 320 94 94, faks:+48 58 320 94 60, e-mail:  viamedica@viamedica.pl