HSP105 expression in oral squamous cell carcinoma: Correlation with clinicopathological features and outcomes

Arvanitidou, Souzana; Martinelli-Kläy, Carla Patrícia; Samson, Jacky; Lobrinus, Johannes Alexander; Dulguerov, Nicolas; Lombardi, Tommaso

doi:10.1111/jop.13007

Cited by 3 publications

(4 citation statements)

References 21 publications

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“… 6 , 20 Another study suggested that increased expression of HSP105 in oral squamous cell carcinoma could be an unfavorable factor for malignancy. 7 These findings are consistent with our results. We believe that poorly differentiated CSCC cells exhibit a significantly faster rate of cell aggregation and proliferation with a higher proliferation index, which may be related to higher expression of HSP105, which may function to help cancer cells maintain functional integrity during tumor proliferation and prevent apoptosis.…”

Section: Discussionsupporting

confidence: 93%

“…Previous studies have revealed that HSP105 is overexpressed in CSCC and oral SCC. 7 , 8 The present work shows, for the first time to our knowledge, a lower expression of HSP105 in CSCC compared to the normal epidermis. These findings suggest that HSP105 may play different roles in different tumors and merit further investigation.…”

Section: Discussionsupporting

confidence: 55%

“… 6 Souzana et al studied the expression of HSP105 in oral SCCs, and their results suggested that the overexpression of HSP105 may be a prognostic factor for malignancy in oral SCC. 7 Muchemwa et al reported that tumors overexpressing HSP105 are ideal candidates for vaccination with HSP105-derived peptides or DNA. 8 However, an association between the level of HSP105 expression and CSCC has thus far been lacking.…”

Section: Introductionmentioning

confidence: 99%

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Expression of Heat Shock Protein 105 in Cutaneous Squamous Cell Carcinoma: Correlation with Clinicopathological Characteristics

Jia¹,

Li²,

Ye³

et al. 2021

CCID

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Background Heat shock proteins (HSPs), a group of heat stress proteins, are characterized by highly conserved properties. Malignant transformation is a cellular stress, and the expression of HSPs may be affected during this process. Heat shock protein 105 (HSP105) is a protective protein that has long been observed in many cancer types, but little attention has been given to cutaneous squamous cell carcinoma (CSCC). As such, the objectives of this study were to observe the expression of HSP105 on CSCC and evaluate its correlation with clinicopathological characteristics. Methods This retrospective study enrolled 60 patients with CSCC. The patients’ clinical data, including sex, age, tumor location, tumor type, and degree of pathological differentiation, were collected. The expression of HSP105 was measured by Western blot and immunohistochemical staining. Results HSP105 expression was decreased in CSCC (HSCORE=0.65 (0.30, 1.98)) compared with normal skin (HSCORE=2.20 (1.50, 2.80)) (P<0.001). These results were consistent with the Western blot analysis. HSP105 immunostaining of Bowen disease (HSCORE=1.28 (1.08, 2.40)) revealed higher expression than in verrucous carcinoma (HSCORE=0.30 (0.23, 0.85)), keratoacanthoma (HSCORE=0.53 (0.29, 0.93)) and acantholytic squamous cell carcinoma (HSCORE=0.53 (0.41, 0.68) (P<0.01)). Poorly differentiated CSCC showed significantly higher expression of HSP105. Conclusion Our study reveals for the first time that the expression of HSP105 is decreased in CSCC. We suggest that the molecular mechanisms underlying the differential expression of HSP deserve a more rigorous future study, the results of which might explain its role in carcinogenesis and its potential as a target for selective tumor therapy.

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Section: Discussionsupporting

confidence: 93%

Section: Discussionsupporting

confidence: 55%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Expression of Heat Shock Protein 105 in Cutaneous Squamous Cell Carcinoma: Correlation with Clinicopathological Characteristics

Jia¹,

Li²,

Ye³

et al. 2021

CCID

View full text Add to dashboard Cite

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“…Most malignant melanomas exhibit increased expression of iASPP (inhibitor of an apoptosis-stimulating protein of p53) [ 7 ], while HSP105 can bind to the tumor suppressor gene p53 to protect cells from apoptosis, which is essential for the survival and proliferation of cancer cells [ 8 – 10 ]. HSP105 was shown to be overexpressed in a variety of human cancer cells, and high expression of HSP105 in squamous cell carcinoma [ 11 ], lung adenocarcinoma [ 12 ] and oral squamous cell carcinoma [ 13 ] is always related to disease progression and poor prognosis. Although several studies have revealed that HSP105 expression in CMM and metastatic CMM is higher than that in nevi [ 14 ], the relationship between HSP105 and clinicopathological features of CMM has not been identified.…”

Section: Introductionmentioning

confidence: 99%

HSP105 expression in cutaneous malignant melanoma: Correlation with clinicopathological characteristics

Chen

Qian

et al. 2021

PLoS ONE

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Background Heat shock proteins can protect against stress-associated cellular challenges, but they can also protect some tumors from human immune system monitoring. Heat shock protein 105 (HSP105/110) is a high molecular weight protein whose expression has been reported in many cancers, but few studies on its role in cutaneous malignant melanoma have been published. In this study, we analyzed the relationship between HSP105 expression and the clinicopathological characteristics of CMM. Methods This retrospective study included 91 patients with CMM. The clinicopathological characteristics of CMM patients, including age, lesion duration, location, pathological classification, Clark’s level, Breslow thickness, metastasis and recurrence, were collected. Immunohistochemical staining and Western blot analysis for HSP105 were performed. Pigmented nevi (n = 20) served as a control. The staining intensity and percentage of stained cells were expressed as a histochemical score (HSCORE). Results HSP105 was overexpressed in melanoma compared with nevi. Differences in the HSCORE between nevi (HSCORE = 1.05(0.15,1.50)) and CMM (HSCORE = 2.68(1.80,3.60)) were remarkable (P<0.001). Exposed site lesions, recurrent and metastatic lesions, nodular melanoma and lentigo maligna melanoma were closely associated with higher HSP105 expression (P = 0.011, P = 0.001 and P = 0.001, respectively). Moreover, no significant difference was observed in Clark’s level, Breslow thickness, or lesion duration (P>0.05). Conclusion HSP105 is overexpressed in CMM. Higher HSP105 expression in lesions is associated with different clinicopathological variables. HSP105 may be a potential target for the diagnosis, treatment and prognostic prediction of CMM.

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Prognosis and predictive value of heat-shock proteins expression in oral cancer

Lü¹,

Yong-wu²,

Gan³

et al. 2021

Medicine

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Background: Heat-shock proteins (HSP) is a key chaperone protein which maintains intracellular proteostasis and is expressed on the surface of solid and hematological malignancies. Several studies have reported paradoxical evidence of the association between HSP expression and prognosis of oral cancer. To address the discrepancy, we carried out the meta-analysis to assess the role of HSP such as: HSP70, HSP90, HSP27, HSP60, and HSP105 in susceptibility, progression, and prognosis of oral cancer. Materials and methods: We retrieved the PubMed, Embase, Web of science, China National Knowledge Infrastructure (CNKI), and Wanfang databases to acquire the eligible studies which were associated with HSP70, HSP90, HSP27, HSP60, and HSP105 protein expression and oral cancer. We applied hazard ratio (HR) and its 95% confidence interval (95% CI) to assess the value of HSP protein expression in overall survival of oral cancer; odds ratio (OR) and its 95% CI were used to evaluate the association of risk and clinical features of oral cancer. Funnel plot, Begg test, and Egger line regression test were utilized to observe publication bias among studies. All statistical analysis was performed with Stata 14.0 software (Stata Corporation, College Station, TX). Results: A total of 26 studies were included in the present meta-analysis. On based of the results, HSP70 and HSP27 had no significant association with progression of oral cancer. However, the pooled HR and 95% CI revealed a significant well effects of HSP70 and HSP27 expression on survival of oral cancer. Moreover, the susceptibility of oral cancer was significantly associated with HSP70 and HSP60 overexpression. Conclusion: HSP70 and HSP27 protein overexpression might be valuable biomarkers for the prognosis of oral cancer. And HSP70 and HSP60 might have potential predictive effects on the risk of oral cancer.

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HSP105 expression in oral squamous cell carcinoma: Correlation with clinicopathological features and outcomes

Abstract: This article has been accepted for publication and undergone full peer review but has not been through the copyediting, typesetting, pagination and proofreading process, which may lead to differences between this version and the Version of Record. Please cite this article as

Cited by 3 publications

References 21 publications

Expression of Heat Shock Protein 105 in Cutaneous Squamous Cell Carcinoma: Correlation with Clinicopathological Characteristics

Expression of Heat Shock Protein 105 in Cutaneous Squamous Cell Carcinoma: Correlation with Clinicopathological Characteristics

HSP105 expression in cutaneous malignant melanoma: Correlation with clinicopathological characteristics

Prognosis and predictive value of heat-shock proteins expression in oral cancer

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