Decreased Expression of PSMB9 Gene in Patients with Endometrial Carcinoma

Document Type : Original Article (s)

Authors

1 Assistant Professor, Department of Cell and Molecular Biology and Microbiology, School of Biological Science and Technology, University of Isfahan, Isfahan, Iran

2 MS Student, Department of Molecular Cell Biology and Microbiology, School of Biological Science and Technology, University of Isfahan, Isfahan, Iran

3 Professor, Department of Obstetrics and Gynecology, School of Medicine, Isfahan University of Medical Sciences, Isfahan, Iran

Abstract

Background: Endometrial carcinoma is the second most common neoplasm in women, and understanding the genes involved in its occurrence can help in understanding the disease behavior and, ultimately, in treating it.
Methods: There were 35 samples of frozen endometrial carcinoma tissues and 24 samples of normal endometrium adjacent to the tumors. Cell total RNA was extracted, followed by DNaseI enzyme treatment. Using random hexamers cDNA was synthesized. We measured PSMB9 gene expression by RT-qPCR using exon junction-specific primers. The statistical analysis was performed using REST2009 software.
Findings: The observation of two ribosomal RNA bands showed that RNA was not broken during extraction. The appropriate concentration of extracted RNA was in the appropriate range for cDNA. Examination of the melting curve showed that specific amplification of the PSMB9 gene was performed. The difference in PSMB9 mRNA expression between endometrial carcinoma tissue and adjacent normal tissue was 0.266 units. This was considered significant according to a P of 0.008.
Conclusion: There was a decrease in PSMB9 gene expression in endometrial carcinoma tissues compared with normal endometrial tissues adjacent to the tumor. The fact that PSMB9 expression has decreased may indicate that the gene has tumor suppressor functions.

Highlights

Seyed-Morteza Javadirad: Google Scholar

Elham shishebor: Google Scholar

Fariba Behnamfar: Google Scholar

 

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References

  1. Miller KD, Nogueira L, Devasia T, Mariotto AB, Yabroff KR, Jemal A, et al. Cancer treatment and survivorship statistics, 2022. CA Cancer J Clin 2022; 72(5): 409-36.
  2. Sung H, Ferlay J, Siegel RL, Laversanne M, Soerjomataram I, Jemal A, et al. Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries. CA Cancer J Clin 2021; 71(3): 209-49.
  3. Vizza E, Cutillo G, Bruno V, Sperduti I, Mancini E, Baiocco E, et al. Pattern of recurrence in patients with endometrial cancer: A retrospective study. Eur J Surg Oncol 2020; 46(9): 1697-702.
  4. Rostami S, Nahvijou A. Gynecologic Cancers Estimates in the I.R. Iran, 2012- 2040. Basic Clin Cancer Res 2022; 13(2): 111-8.
  5. Brehm A, Liu Y, Sheikh A, Marrero B, Omoyinmi E, Zhou Q, et al. Additive loss-of-function proteasome subunit mutations in CANDLE/PRAAS patients promote type I IFN production. J Clin Invest 2015; 125(11): 4196-211.
  6. Xu Y, Liu G, Zhou Y, Lu Z, Shi Z, Wang J. The genetic association between LMP2 and LMP7 polymorphisms and susceptibility of insulin dependent diabetes mellitus. Medicine (Baltimore) 2020; 99(13): e19482.
  7. Gergelits V, Parvanov E, Simecek P, Forejt J. Chromosome-wide characterization of meiotic noncrossovers (gene conversions) in mouse hybrids. Genetics 2021; 217(1): 1-14.
  8. Guillon H, de Massy B. An initiation site for meiotic crossing-over and gene conversion in the mouse. Nat Genet 2002; 32(2): 296-9.
  9. Van Kaert L, Ashton-Rickardt PG, Eichelberger M, Gaczynska M, Nagashima K, Rock KL, et al. Altered peptidase and viral-specific T cell response in LMP2 mutant mice. Immunity 1994; 1(7): 533-41.
  10. Del Rio Oliva M, Mellett M, Basler M. Immunoproteasome inhibition attenuates experimental psoriasis. Front Immunol 2022; 13: 1075615.
  11. Xie X, Bi H-L, Lai S, Zhang Y-L, Li N, Cao H-J, et al. The immunoproteasome catalytic β5i subunit regulates cardiac hypertrophy by targeting the autophagy protein ATG5 for degradation. Sci Adv
    2019; 5(5): eaau0495.
  12. Tripathi SC, Vedpathak D, Ostrin EJ. The Functional and Mechanistic Roles of Immunoproteasome Subunits in Cancer. Cells 2021; 10(12): 3587.
  13. Sultana GNN, Akter F, Israfil SMH, Ray UC, Jahan RA, Ali MS, et al. Quantitative analysis of serum cell-free DNA as a predictive and prognostic marker in breast cancer patients. Front Oncol 2023; 13: 1171412.
  14. Adamski MG, Gumann P, Baird AE. A method for quantitative analysis of standard and high-throughput qPCR expression data based on input sample quantity. PLoS One 2014; 9(8): e103917.
  15. Dutta D, Naiyer S, Mansuri S, Soni N, Singh V, Bhat KH, et al. COVID-19 Diagnosis: A Comprehensive Review of the RT-qPCR Method for Detection of SARS-CoV-2. Diagnostics 2022; 12(6): 1503.
  16. Javadirad SM, Mokhtari M, Esfandiarpour G, Kolahdouzan M. The pseudogene problem and RT-qPCR data normalization; SYMPK: a suitable reference gene for papillary thyroid carcinoma. Sci Rep 2020; 10(1): 18408.
  17. Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2−ΔΔCT method. Methods 2001; 25(4): 402-8.
  18. Hayashi T, Faustman DL. Development of spontaneous uterine tumors in low molecular mass polypeptide-2 knockout mice. Cancer Res 2002; 62(1): 24-7.
  19. Chen B, Zhu H, Yang B, Cao J. The dichotomous role of immunoproteasome in cancer: Friend or foe? Acta Pharm Sin B 2022; 13(5): 1976-89.
  20. Geoffroy K, Araripe Saraiva B, Viens M, Béland D, Bourgeois-Daigneault MC. Increased expression of the immunoproteasome subunits PSMB8 and PSMB9 by cancer cells correlate with better outcomes for triple-negative breast cancers. Sci Rep 2023; 13(1): 2129.
  21. Kalaora S, Lee JS, Barnea E, Levy R, Greenberg P, Alon M, et al. Immunoproteasome expression is associated with better prognosis and response to checkpoint therapies in melanoma. Nat Commun 2020; 11(1): 896.
  22. Van Allen EM, Miao D, Schilling B, Shukla SA, Blank C, Zimmer L, et al. Genomic correlates of response to CTLA-4 blockade in metastatic
    Science (80- ) 2015; 350(6257): 207-11.
  23. Leister H, Luu M, Staudenraus D, Lopez Krol A, Mollenkopf HJ, Sharma A, et al. Pro- and Antitumorigenic Capacity of Immunoproteasomes in Shaping the Tumor Microenvironment. Cancer Immunol Res 2021; 9(6): 682-92.
  24. Hayashi T, Horiuchi A, Sano K, Hiraoka N, Kasai M, Ichimura T, et al. Potential role of LMP2 as tumor-suppressor defines new targets for uterine leiomyosarcoma therapy. Sci Rep 2011; 1(1): 180.
  25. Hayashi T, Kobayashi Y, Kohsaka S, Sano K. The mutation in the ATP-binding region of JAK1, identified in human uterine leiomyosarcomas, results in defective interferon-γ inducibility of TAP1 and LMP2. Oncogene 2006; 25(29): 4016-26.
  26. Hayashi T, Horiuchi A, Sano K, Hiraoka N, Ichimura T, Sudo T, et al. Potential diagnostic biomarkers: differential expression of LMP2/β1i and cyclin B1 in human uterine leiomyosarcoma. Tumori 2014; 100(4): 99e-106e.
Journal of Isfahan Medical School
Volume 41, Issue 745
1st Week, February
January and February 2024
Pages 1045-1051

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History

  • Receive Date: 04 September 2023
  • Accept Date: 16 January 2024

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