Knockdown of serpin peptidase inhibitor clade C member�1 inhibits the growth of nasopharyngeal carcinoma cells

Abstract

Nasopharyngeal carcinoma (NPC) is a type of cancer originating in the nasopharynx. There are no NPC-specific treatments available at present. Serpin peptidase inhibitor clade C member 1 (SERPINC1) serves roles in anticoagulation and anti-inflammation. The aim of the present study was to investigate the role of SERPINC1 in the proliferation and apoptosis of NPC cells. Tumor and adjacent healthy tissue samples were collected from patients with NPC. Additionally, the SERPINC1 gene was silenced in the HNE3 cell line using short interfering RNA targeted against SERPINC1 (SERPINC1-siRNA). Cell viability was determined via a Cell Counting Kit-8 assay; furthermore, proliferation and apoptosis were investigated via flow cytometry. Western blotting and reverse transcription-quantitative polymerase chain reaction analysis were performed to determine the expression levels of protein and mRNA. It was revealed that the expression levels of SERPINC1 mRNA and protein were increased in NPC tumor tissues compared with in adjacent healthy tissues. The expression of SERPINC1 mRNA and protein in HNE3 cells decreased following SERPINC1-siRNA transfection. Furthermore, knockdown of SERPINC1 promoted apoptosis and inhibited proliferation. It was also demonstrated that silencing SERPINC1 upregulated the expression of B-cell lymphoma-2 (Bcl-2)-associated X protein and p53 mRNA and protein, and downregulated that of Bcl-2, survivin and cyclin D1. Downregulation of SERPINC1 reduced the phosphorylation of phosphatidylinositol 3-kinase (PI3K), protein kinase B (Akt) and mammalian target of rapamycin (mTOR). Thus, SERPINC1 knockdown may promote the apoptosis of HNE3 cells and inhibit proliferation via the suppression of the PI3K/Akt/mTOR signaling pathway.

Noninvasive Analysis Using Data‐Independent Acquisition Mass Spectrometry: New Epidermal Proteins That Reveal Sex Differences in the Aging Process

“…8 Oxidative Medicine and Cellular Longevity proteins were consistent with other aging-related proteomics findings. Xu et al found that low expression of SERPINC1 may suppress the PI3K/AKT/mTOR signaling pathway [37] and the suppression of the PI3K/AKT/mTOR signaling pathway can delay aging [38]. We also obtained some results that differ from previous findings, such as the results regarding the expression of GPC1 protein; in previous studies, GPC1 has been found to be significantly downregulated with aging [39], while it was upregulated with aging in our study.…”

Discovery of core gene families associated with liver metastasis in colorectal cancer and regulatory roles in tumor cell immune infiltration

“…As for the top 5 down-regulated key DEGs, SERPINC1 (Serpin Family C Member 1), PELI1 (Pellino E3 Ubiquitin Protein Ligase 1), GSTA5 (glutathione S-transferase alpha 5), GPR171 (G Protein-Coupled Receptor 171), GPR68 (G Protein-Coupled Receptor 68) were observed in GSE75050 and TMEM229A (Transmembrane Protein 229A), CALML5 (Calmodulin Like 5), MMP12 (Matrix Metallopeptidase 12), MSH4 (mutS homolog 4) TREM1 (Triggering Receptor Expressed On Myeloid Cells 1) were detected in GSE131418. SERPINC1 exert anti-coagulatory and anti-inflammatory effects, it also facilitates proliferative and apoptotic processes in nasopharyngeal carcinoma [62] . PELI1 modulates biological activities through modifying protein at post-translational level or ubiquitination process, its high expression coincided with advanced B-cell lymphoma cases [63] .…”

Screening and identification of key genes and pathways in metastatic uveal melanoma based on gene expression using bioinformatic analysis

“…SERPINA1 and SERPINC1 are members of the serpin family, SERPINA1 was found to improve nonsmall cell lung cancer cell migration, colony formation, and resistance to apoptosis, [ 47 ] while knockdown of SERPINC1 was reported to inhibit neural progenitor cell proliferation via suppression of the PI3K/Akt/mTOR signaling pathway. [ 48 ] ITIH2, also known as serum-derived HA-associated protein (SHAP), forms complexes with hyaluronan (HA) to regulate the localization, synthesis, and degradation of HA in serum. Elevated serum levels of the SHAP-HA complex indicate poor prognosis in endometrial and ovarian cancers.…”