» Articles » PMID: 28638266

Nuclear Expression of GS28 Protein: A Novel Biomarker That Predicts Prognosis in Colorectal Cancers

Overview
Journal Int J Med Sci
Specialty General Medicine
Date 2017 Jun 23
PMID 28638266
Citations 3
Authors
Affiliations
Soon will be listed here.
Abstract

GS28 (Golgi SNARE protein, 28 kDa), a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE) protein family, plays a critical role in mammalian endoplasmic reticulum (ER)-Golgi or intra-Golgi vesicle transport. To date, few researches on the GS28 protein in human cancer tissues have been reported. In this study, we assessed the prognostic value of GS28 in patients with colorectal cancer (CRC). We screened for GS28 expression using immunohistochemistry in 230 surgical CRC specimens. The CRCs were right-sided and left-sided in 28.3% (65/230) and 71.3% (164/230) of patients, respectively. GS28 staining results were available in 214 cases. Among these, there were 26 nuclear predominant cases and 188 non-nuclear predominant cases. Stromal GS28 expression was noted in 152 cases of CRC. GS28 nuclear predominant immunoreactivity was significantly associated with advanced tumour stage (p = 0.045) and marginally associated with perineural invasion (p = 0.064). Decreased GS28 expression in the stromal cells was significantly associated with lymph node metastasis (N stage; p = 0.036). GS28 expression was not associated with epidermal growth factor receptor (EGFR) immunohistochemical positivity or mutation status. Investigation of the prognostic value of GS28 with Kaplan-Meier analysis revealed a correlation with overall survival (p = 0.004). Cases with GS28 nuclear predominant expression had significantly poorer overall survival than those with a non-nuclear predominant pattern. Taken together, these results indicate that GS28 nuclear predominant expression could serve as a prognostic marker for CRC and may help in identifying aggressive forms of CRC.

Citing Articles

The role of Golgi complex proteins in cell division and consequences of their dysregulation.

Iannitti R, Mascanzoni F, Colanzi A, Spano D Front Cell Dev Biol. 2025; 12():1513472.

PMID: 39839669 PMC: 11747491. DOI: 10.3389/fcell.2024.1513472.


USO1 expression is dysregulated in non-small cell lung cancer.

Keogh A, Ryan L, Nur M, Baird A, Nicholson S, Cuffe S Transl Lung Cancer Res. 2022; 11(9):1877-1895.

PMID: 36248341 PMC: 9554690. DOI: 10.21037/tlcr-22-230.


The role of the Golgi apparatus in disease (Review).

Liu J, Huang Y, Li T, Jiang Z, Zeng L, Hu Z Int J Mol Med. 2021; 47(4).

PMID: 33537825 PMC: 7891830. DOI: 10.3892/ijmm.2021.4871.


Bioinformatics analysis of prognostic value and prospective pathway signal of miR-30a in ovarian cancer.

Lu W, Wu Y, Lu C, Zhu T, Ren Z, Yu Z J Ovarian Res. 2020; 13(1):120.

PMID: 33004058 PMC: 7532093. DOI: 10.1186/s13048-020-00722-8.

References
1.
Shike M, Winawer S, Greenwald P, Bloch A, Hill M, Swaroop S . Primary prevention of colorectal cancer. The WHO Collaborating Centre for the Prevention of Colorectal Cancer. Bull World Health Organ. 1990; 68(3):377-85. PMC: 2393072. View

2.
Ruan Q, Wang Q, Xie S, Fang Y, Darzynkiewicz Z, Guan K . Polo-like kinase 3 is Golgi localized and involved in regulating Golgi fragmentation during the cell cycle. Exp Cell Res. 2004; 294(1):51-9. DOI: 10.1016/j.yexcr.2003.10.022. View

3.
Tai G, Lu L, Wang T, Tang B, Goud B, Johannes L . Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport from the early/recycling endosome to the trans-Golgi network. Mol Biol Cell. 2004; 15(9):4011-22. PMC: 515336. DOI: 10.1091/mbc.e03-12-0876. View

4.
Gong H, Feng L . Computational analysis of the roles of ER-Golgi network in the cell cycle. BMC Syst Biol. 2014; 8 Suppl 4:S3. PMC: 4290691. DOI: 10.1186/1752-0509-8-S4-S3. View

5.
Mancini M, Machamer C, Roy S, Nicholson D, Thornberry N, Rosen A . Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis. J Cell Biol. 2000; 149(3):603-12. PMC: 2174848. DOI: 10.1083/jcb.149.3.603. View