HSP47 is associated with the prognosis of laryngeal squamous cell carcinoma by inhibiting cell viability and invasion and promoting apoptosis

Abstract

Abstract. Heat shock protein 47 (HSP47) is a 47 kDa collagen binding protein that has a close relationship with the development and progression of tumours. However, little is known concerning the expression profile of HSP47 in laryngeal squamous cell carcinoma (LSCC) patients and there is still insufficient data concerning the underlying mechanisms. The aim of the present study was to explore the expression of HSP47 in LSCC and provide an overview of its association with tumourigenicity and clinical prognosis. The expression of HSP47 in LSCC and adjacent non-cancerous laryngeal tissues was assessed via western blotting and immunohistochemical studies. The prognostic significance of HSP47 expression was analysed using a Kaplan-Meier survival curve. To investigate the influence of HSP47 on the viability, invasion and apoptosis of a LSCC cell line, we performed an in vitro analysis with plasmid vectors and small interfering RNA (siRNA). Our results showed that HSP47 protein expression in the LSCC tissues was markedly decreased compared to that noted in the adjacent non-cancerous tissues, and low expression of HSP47 was correlated with poor prognosis in LSCC patients. Upregulation of HSP47 via plasmid vectors inhibited the proliferation, reduced the invasive ability, increased the sensitivity to cisplatin chemotherapy, promoted apoptosis, and induced the G1 phase arrest of LSCC cells in vitro. The expression of apoptosis-regulating proteins was also altered when HSP47 was upregulated, involving increased expression of cleaved caspase-7/-8/-9, PARP, and Bax and decreased expression of Bcl-2. Our present data suggest that HSP47 is an important prognostic factor and an attractive therapeutic target in LSCC due to its influence on the biological behaviour of LSCC cells.

Presence of heat shock protein 47-positive fibroblasts in cancer stroma is associated with increased risk of postoperative recurrence in patients with lung cancer

“…Increased HSP47 expression in cancer cells promotes cancer progression in part by enhancing deposition of the ECM proteins [9], and several types of cancers are correlated with HSP47 expression in cancer cells [8][9][10]. The present study demonstrated that HSP47-positive broblasts in the stroma, but not HSP47positive cancer cells, were associated with recurrence of lung cancer after surgery.…”

“…[3][4][5][6][7] HSP47 has also been reported to be associated with several types of cancers, including cervical, breast, pancreatic, gastric, and colon cancer. [8][9][10][11] It is encoded by the SERPINH1 gene located on chromosome 11q13.5, and this region is one of the most frequently ampli ed in human cancer. [12] Several types of cancers are associated with abnormal protein folding, and HSP47 has been described as an important chaperone in the control and maintenance of cellular protein homeostasis.…”

Presence of heat shock protein 47-positive fibroblasts in cancer stroma is associated with increased risk of postoperative recurrence in patients with lung cancer

“…Increased HSP47 expression in cancer cells promotes cancer progression in part by enhancing deposition of the ECM proteins, [9] and several types of cancers are correlated with HSP47 expression in cancer cells. [8][9][10] The present study demonstrated that HSP47-positive fibroblasts in the stroma, but not HSP47-positive cancer cells, were associated with recurrence of lung cancer after surgery.…”

“…[3][4][5][6][7] HSP47 has also been reported to be associated with several types of cancers, including cervical, breast, pancreatic, gastric, and colon cancer. [8][9][10][11] It is encoded by the SERPINH1 gene located on chromosome 11q13.5, and this region is one of the most frequently amplified in human cancer. [12] Several types of cancers are associated with abnormal protein folding, and HSP47 has been described as an important chaperone in the control and maintenance of cellular protein homeostasis.…”

Tra2β silencing suppresses cell proliferation in laryngeal squamous cell carcinoma via inhibiting PI3K/AKT signaling

“…In the past decades, a number of molecules, such as TSR2, HSP47, snail, and so on were demonstrated to serve important roles in cellular processes including proliferation, differentiation, metastasis, and tumorigenesis in the prognosis of LSCC. [29][30][31][32][33] Tra2β, one of the human alternative splicing factors, is associated with cancer cell survival and therapeutic sensitivity, 34,35 but the regulatory role and regulatory mechanism of Tra2β in LSCC have remained elusive. In the present study, qRT-PCR and immunohistochemistry assays indicated that Tra2β was significantly upregulated in LSCC tissues compared with adjacent nontumorous tissues.…”