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2000
Volume 20, Issue 2
  • ISSN: 1574-8871
  • E-ISSN: 1876-1038

Abstract

Background

The HSP90 marker is believed to play a constructive role in facilitating neoplastic transformation mainly interaction with multiple pro-survival proteins. Well-designed studies are needed to elucidate the role of HSP90 as a diagnostic marker and therapeutic target in testicular tumors.

Objective

The current study aimed to investigate the expression of HSP90 in various types of testicular cancer and highlight its expression in embryonal testicular cancer.

Material and Methods

Immunohistochemical staining for HSP90 in 84 male patients, with non-metastatic testicular cancer, who underwent orchiectomy from 2000 to 2023, was retrospectively performed at the Laboratory Department of General Hospital of Nikaia in Greece.

Results

A total of 84 males, with a mean age of 36.2 years, who have undergone high-cord radical orchiectomy, were included in this study. Out of the included males, 28.57% had embryonal carcinoma, 23.81% had seminoma, 19.05% had yolk sac tumor, 11.9% had mature teratoma, 9.52% had immature teratoma, and 7.14% had choriocarcinoma. HSP90b was positive in all embryonal carcinoma, seminoma, and choriocarcinoma cases, while it was positive in 75% of the yolk sac tumor, 75% of mature teratoma, and 75% of immature teratoma specimens. HSP90 was found negative in all choriocarcinoma, mature teratoma, and immature teratoma specimens, while it was positive in 25% of yolk sac tumor, 8.33% of embryonal carcinoma, and 10% of seminoma cases. Concerning the expression of HSP90b, a statistically significant relationship was found between excised tumor specimens and normal parenchyma specimens, especially in sac cases ( <0.001). Regarding HSP90a expression, a statistically significant relationship (OR=21.5, =0.021) was found between excised tumor specimens and normal parenchyma specimens, especially in embryonal carcinoma cases ( <0.001).

Conclusion

HSP90b is highly expressed in the majority of the types of testicular tumors, both in tumor and normal parenchyma specimens, while HSP90a staining is negative in resected specimens. Further well-designed studies are needed to elucidate the role of HSP90 as a diagnostic marker and therapeutic target in testicular tumors.

© 2025 Bentham Science Publishers
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2024-09-25
2025-07-29

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References

  1. CinoneM. AlbrizioM. GuaricciA.C. LacitignolaL. DesantisS. Testicular expression of heat SHOCK proteins 60, 70, and 90 in cryptorchid horses.Theriogenology2024217839110.1016/j.theriogenology.2024.01.019 38262223
     [Google Scholar]
  2. De MaioA. SantoroM.G. TanguayR.M. HightowerL.E. Ferruccio Ritossa’s scientific legacy 50 years after his discovery of the heat shock response: A new view of biology, a new society, and a new journal.Cell Stress Chaperones201217213914310.1007/s12192‑012‑0320‑z 22252402
     [Google Scholar]
  3. D’SouzaS.M. BrownI.R. Constitutive expression of heat shock proteins Hsp90, Hsc70, Hsp70 and Hsp60 in neural and non-neural tissues of the rat during postnatal development.Cell Stress Chaperones19983318819910.1379/1466‑1268(1998)003<0188:CEOHSP>2.3.CO;2 9764759
     [Google Scholar]
  4. HorwichA.L. Molecular chaperones in cellular protein folding: the birth of a field.Cell2014157228528810.1016/j.cell.2014.03.029 24725397
     [Google Scholar]
  5. CsermelyP. SchnaiderT. SotiC. ProhászkaZ. NardaiG. The 90-kDa molecular chaperone family: Structure, function, and clinical applications. A comprehensive review.Pharmacol. Ther.199879212916810.1016/S0163‑7258(98)00013‑8 9749880
     [Google Scholar]
  6. MoserC. LangS.A. KainzS. Blocking heat shock protein-90 inhibits the invasive properties and hepatic growth of human colon cancer cells and improves the efficacy of oxaliplatin in p53 -deficient colon cancer tumors in vivo.Mol. Cancer Ther.20076112868287810.1158/1535‑7163.MCT‑07‑0410 18025273
     [Google Scholar]
  7. CaoJ. LiuZ. YuanJ. Subgrouping testicular germ cell tumors based on immunotherapy and chemotherapy associated lncRNAs.Heliyon2024102e2432010.1016/j.heliyon.2024.e24320 38298718
     [Google Scholar]
  8. ChieffiP. De MartinoM. EspositoF. Further insights into testicular germ cell tumor oncogenesis: Potential therapeutic targets.Expert Rev. Anticancer Ther.202020318919510.1080/14737140.2020.1736566 32164473
     [Google Scholar]
  9. GoldbergH. KlaassenZ. ChandrasekarT. FleshnerN. HamiltonR.J. JewettM.A.S. Germ cell testicular tumors—contemporary diagnosis, staging and management of localized and advanced disease.Urology201912581910.1016/j.urology.2018.12.025 30597167
     [Google Scholar]
  10. DudejaV. VickersS.M. SalujaA.K. The role of heat shock proteins in gastrointestinal diseases.Gut20095871000100910.1136/gut.2007.140194 19520890
     [Google Scholar]
  11. EhrenfriedJ.A. HerronB.E. TownsendC.M.Jr EversB.M. Heat shock proteins are differentially expressed in human gastrointestinal cancers.Surg. Oncol.19954419720310.1016/S0960‑7404(10)80036‑2 8528482
     [Google Scholar]
  12. ZouJ. GuoY. GuettoucheT. SmithD.F. VoellmyR. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1.Cell199894447148010.1016/S0092‑8674(00)81588‑3 9727490
     [Google Scholar]
  13. VoellmyR. On mechanisms that control heat shock transcription factor activity in metazoan cells.Cell Stress Chaperones20049212213310.1379/CSC‑14R.1 15497499
     [Google Scholar]
  14. KogaF. XuW. KarpovaT.S. McNallyJ.G. BaronR. NeckersL. Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent Akt and Erk activation.Proc. Natl. Acad. Sci. USA200610330113181132210.1073/pnas.0604705103 16844778
     [Google Scholar]
  15. KangB.H. PlesciaJ. DohiT. RosaJ. DoxseyS.J. AltieriD.C. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network.Cell2007131225727010.1016/j.cell.2007.08.028 17956728
     [Google Scholar]
  16. Al-kaabiM.M. BakirW.A. GaidanH.A. Immunohistochemical expression of interlukin10 (IL10) and heat shock protein-90 (HSP-90) in prostatic carcinoma.Indian J. Pathol. Microbiol.202063223023410.4103/IJPM.IJPM_460_19 32317521
     [Google Scholar]
  17. TangD. KhalequeM.A. JonesE.L. Expression of heat shock proteins and heat shock protein messenger ribonucleic acid in human prostate carcinoma in vitro and in tumors in vivo.Cell Stress Chaperones2005101465810.1379/CSC‑44R.1 15832947
     [Google Scholar]
  18. DevajaO. KingR.J. PapadopoulosA. RajuK.S. Heat-shock protein 27 (HSP27) and its role in female reproductive organs.Eur. J. Gynaecol. Oncol.19971811622 9061315
     [Google Scholar]
  19. KawakamiE. HiranoT. HoriT. TsutsuiT. Testicular superoxide dismutase activity, heat shock protein 70 concentration and blood plasma inhibin-alpha concentration of dogs with a Sertoli cell tumor in a unilateral cryptorchid testis.J. Vet. Med. Sci.200769121259126210.1292/jvms.69.1259 18176022
     [Google Scholar]
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Expression of Heat Shock Protein 90 in Testicular Cancer: A Retrospective Cohort Study
Rev. Recent Clin. Trials 20, 153 (2025); https://doi.org/10.2174/0115748871317252240919051309
/content/journals/rrct/10.2174/0115748871317252240919051309
/content/journals/rrct/10.2174/0115748871317252240919051309
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  • Article Type:     Research Article
Keyword(s): biomarker; choriocarcinoma; embryonal carcinoma; Heat shock proteins; HSP90; testicular cancer

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