Research Paper Volume 15, Issue 21 pp 12633—12650
KIFC1 promotes proliferation and pseudo-bipolar division of ESCC through the transportation of Aurora B kinase
- 1 Center of Healthy Aging, Changzhi Medical College, Changzhi 047500, China
- 2 Department of Pathology, Affiliated HePing Hospital of Changzhi Medical College, Changzhi 047500, China
- 3 Department of Pathology, The First Clinical College of Changzhi Medical College, Changzhi 047500, China
- 4 Department of Biology, Changzhi Medical College, Changzhi 047500, China
Received: July 4, 2023 Accepted: October 15, 2023 Published: November 8, 2023
https://doi.org/10.18632/aging.205203How to Cite
Copyright: © 2023 Du et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (CC BY 4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Abstract
Esophageal squamous cell carcinoma (ESCC) accounts for over 90% of total in China, and the five-year survival rate for patients is less than 30%. Accordingly, the identification of novel, effective early diagnosis markers and therapeutic targets for ESCC is of paramount importance. KIFC1 has been identified as highly expressed in several types of cancer, although its prognostic value is inconsistent, and no research has been conducted specifically on its effect on ESCC. To investigate the expression and function of KIFC1 in ESCC, we conducted immunohistochemical staining on 30 pairs of para-carcinoma tissue and cancerous tissues, revealing a significant increase in KIFC1 expression in ESCC tissues. Using siRNA to knock down KIFC1 significantly reduced the proliferation of EC109 ESCC cells both in vitro and in vivo. Bioinformatics analysis revealed a highly significant positive correlation between KIFC1 overexpression and signaling pathways associated with tumor proliferation pathways. In EC109 cells, overexpression of KIFC1 significantly increased the rate of centrosome amplification and the likelihood of pseudo-bipolar division. Furthermore, the expression of KIFC1 and the rate of centrosome amplification in ESCC tissues were also positively correlated. In order to explore the underline molecular mechanisms, we identified, through proteomics, that KIFC1 binds to the protein Aurora B. The knockdown of KIFC1 significantly reduced the distribution of Aurora B on the metaphase plate and substantially inhibited the phosphorylation of its classical substrate, Histone H3. In conclusion, these findings indicate the potential utility of KIFC1 as both a tumor marker and a promising target for therapeutic interventions.