Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation

Guo, Kun; Gan, Lin; Zhang, Shu; Cui, Feng Jie; Wang, Cun; Li, Yan; Kang, Nan; Gao, Mei; Liu, Kun Yin

doi:10.3892/or.2012.1844

Cited by 32 publications

(20 citation statements)

References 29 publications

(30 reference statements)

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“…Alteration of O -GlcNAc level by OGA overexpression in HeLa cells led to decreased pSer-82 level and increased pSer-71 level in vimentin (66). Guo et al also showed that nuclear translocation of HSP27 observed in liver cancer cells is regulated by both O -GlcNAc and phosphate groups (67). Another study from Srikanth et al displayed the synergistic effects of O -GlcNAcylation and phosphorylation on keratin 8 and 18 (68).…”

Section: O-glcnac Modification and Phosphorylation In Cancermentioning

confidence: 99%

Aberrant O-GlcNAcylated Proteins: New Perspectives in Breast and Colorectal Cancer

et al. 2014

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Increasing glucose consumption is thought to provide an evolutionary advantage to cancer cells. Alteration of glucose metabolism in cancer influences various important metabolic pathways including the hexosamine biosynthesis pathway (HBP), a relatively minor branch of glycolysis. Uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), an end product of HBP, is a sugar substrate used for classical glycosylation and O-GlcNAcylation, a post-translational protein modification implicated in a wide range of effects on cellular functions. Emerging evidence reveals that certain cellular proteins are abnormally O-GlcNAc modified in many kinds of cancers, indicating O-GlcNAcylation is associated with malignancy. Since O-GlcNAc rapidly on and off modifies in a similar time scale as in phosphorylation and these modifications may occur on proteins at either on the same or adjacent sites, it suggests that both modifications can work to regulate the cellular signaling pathways. This review describes the metabolic shifts related to the HBP, which are commonly found in most cancers. It also describes O-GlcNAc modified proteins identified in primary breast and colorectal cancer, as well as in the related cancer cell lines. Moreover, we also discuss the potential use of aberrant O-GlcNAcylated proteins as novel biomarkers of cancer.

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Section: O-glcnac Modification and Phosphorylation In Cancermentioning

confidence: 99%

Aberrant O-GlcNAcylated Proteins: New Perspectives in Breast and Colorectal Cancer

et al. 2014

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“…Recently, phosphorylated HSPB1 has been proved to suppress apoptosis, enhance invasion and survival in cancer cells [29]. Additionally, recent studies indicated that phosphorylation of HSPB1 could modify the subcellular localization of HSPB1 in HCC cells [30]. And abolish the phosphorylation of HSPB1 through mutating the phosphorylation site from serine residues to alanine residues blocks the phosphorylation of HSPB1 and attenuates the translocation of HSPB1 to nuclei in HCC cells, and suggested that the subcellular localization of HSPB1 may play essential biological roles in liver cancer [30].…”

Section: Resultsmentioning

confidence: 99%

Distinct prognostic roles of HSPB1 expression in non-small cell lung cancer

Huang¹,

Li²,

Sun³

et al. 2018

neo

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Lung cancer is the leading cause of cancer morbidity and mortality around world. Heat shock protein beta-1 (HSPB1) expression is aberrantly increased in non-small cell lung cancer (NSCLC) patients. However, the roles of HSPB1 expression in the prognosis of NSCLC are still elusive. In this study, we investigated the prognostic roles of HSPB1 in NSCLC by using "The Kaplan-Meier plotter" (KM plotter) database. Our data indicated that HSPB1 mRNA low expression was correlated to better overall survival (OS) for all NSCLC patients, hazard ratio (HR) 1.41 (1.24-1.61), p=1.1e-7, and better OS in lung adenocarcinoma (LUAD) patients, HR 1.81 (1.42-2.32), p=1.5e-06, but not in lung squamous cell carcinoma (LUSC) patients, HR 1.21 (0.94-1.55), p=0.14. In addition, mRNA low expression of HSPB1 is also significantly associated with better OS of NSCLC patients in different smoking status, in different chemotherapy status, in clinical stage I & II, as well as patients with successful surgery treatment. Our results indicated that HSPB1 expression may have distinct prognostic values in NSCLC patients, and may provide an effective clinical strategy to accurately predict the prognosis of NSCLC patients.

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“…As reported by other authors the equilibrium between large and small oligomers might be shifted by phosphorylation, depending on the physiological requirements of the cell. Interestingly, the ability to form small oligomers upon phosphorylation was shown to mediate the entry of HspB1 in the nucleus [48,49,50,51]. Based on these findings HSPB1 phospho-Ser-15 might perform other important functions in HT1-dependent tumorigenesis by entering into the nucleus as small oligomer.…”

Section: Resultsmentioning

confidence: 99%

Heat Shock Response Associated with Hepatocarcinogenesis in a Murine Model of Hereditary Tyrosinemia Type I

Angileri

Morrow

Roy

et al. 2014

Cancers

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Hereditary Tyrosinemia type 1 (HT1) is a metabolic liver disease caused by genetic defects of fumarylacetoacetate hydrolase (FAH), an enzyme necessary to complete the breakdown of tyrosine. The severe hepatic dysfunction caused by the lack of this enzyme is prevented by the therapeutic use of NTBC (2-[2-nitro-4-(trifluoromethyl)benzoyl]cyclohexane-1,3-dione). However despite the treatment, chronic hepatopathy and development of hepatocellular carcinoma (HCC) are still observed in some HT1 patients. Growing evidence show the important role of heat shock proteins (HSPs) in many cellular processes and their involvement in pathological diseases including cancer. Their survival-promoting effect by modulation of the apoptotic machinery is often correlated with poor prognosis and resistance to therapy in a number of cancers. Here, we sought to gain insight into the pathophysiological mechanisms associated with liver dysfunction and tumor development in a murine model of HT1. Differential gene expression patterns in livers of mice under HT1 stress, induced by drug retrieval, have shown deregulation of stress and cell death resistance genes. Among them, genes coding for HSPB and HSPA members, and for anti-apoptotic BCL-2 related mitochondrial proteins were associated with the hepatocarcinogenetic process. Our data highlight the variation of stress pathways related to HT1 hepatocarcinogenesis suggesting the role of HSPs in rendering tyrosinemia-affected liver susceptible to the development of HCC.

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Translocation of HSP27 into liver cancer cell nucleus may be associated with phosphorylation and O-GlcNAc glycosylation

Cited by 32 publications

References 29 publications

Aberrant O-GlcNAcylated Proteins: New Perspectives in Breast and Colorectal Cancer

Aberrant O-GlcNAcylated Proteins: New Perspectives in Breast and Colorectal Cancer

Distinct prognostic roles of HSPB1 expression in non-small cell lung cancer

Heat Shock Response Associated with Hepatocarcinogenesis in a Murine Model of Hereditary Tyrosinemia Type I

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