4.7 Article

Relationship between the Ubiquitin-Proteasome System and Autophagy in Colorectal Cancer Tissue

Journal

BIOMEDICINES
Volume 11, Issue 11, Pages -

Publisher

MDPI
DOI: 10.3390/biomedicines11113011

Keywords

ubiquitin-proteasome system; autophagy; colorectal cancer tissue

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This study analyzed the changes in the transcriptional activity of autophagy-related genes and the ubiquitination process in colorectal cancer tissue. The results showed dysregulation of ubiquitination and autophagy processes, especially in the early stages of cancer, which may contribute to tumor progression and poor prognosis.
Background: Dysregulation of the autophagy process via ubiquitin is associated with the occurrence of a number of diseases, including cancer. The present study analyzed the changes in the transcriptional activity of autophagy-related genes and the ubiquitination process (UPS) in colorectal cancer tissue. (2) Methods: The process of measuring the transcriptional activity of autophagy-related genes was analyzed by comparing colorectal cancer samples from four clinical stages I-IV (CS I-IV) of adenocarcinoma to the control (C). The transcriptional activity of genes associated with the UPS pathway was determined via the microarray technique (HG-U133A, Affymetrix). (3) Results: Of the selected genes, only PTEN-induced kinase 1 (PINK1) indicated statistical significance for all groups of colon cancer tissue transcriptome compared to the control. The transcriptional activity of the protein tyrosine phosphatase non-receptor type 22 (PTPN22) gene increased in all stages of the cancer, but the p-value was only less than 0.05 in CSIV vs. C. Forkhead box O1 (FOXO 1) and ubiquitin B (UBB) are statistically overexpressed in CSI. (4) Conclusions: The pathological expression changes in the studied proteins observed especially in the early stages of colorectal cancer suggest that the dysregulation of ubiquitination and autophagy processes occur during early neoplastic transformation. Stopping or slowing down the processes of removal of damaged proteins and their accumulation may contribute to tumor progression and poor prognosis.

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