Mortalin is a distinct bio-marker and prognostic factor in serous ovarian carcinoma

Xu, Meifeng; Jin, Tiefeng; Chen, Liyan; Zhang, Xianglan; Zhu, Guang; Wang, Qianrong; Lin, Zhenhua

doi:10.1016/j.gene.2019.02.033

Cited by 31 publications

(31 citation statements)

References 44 publications

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“…Mortalin suppression inhibited CRC cell proliferation and EMT via deregulating the levels of β‐catenin, Survivin, c‐Myc, and Cyclin‐D1. These results were consistent with our previous study . In brief, certain molecular mechanisms by which mortalin participates in carcinogenesis are not completely understood.…”

Section: Discussionsupporting

confidence: 93%

“…Immunostaining for mortalin was determined by a double semiquantitative scoring system. 20 Tan granules appearance was regarded as positive staining. Briefly, the staining intensity of the cells was scored.…”

Section: Analysis Of the Ihc Resultsmentioning

confidence: 99%

“…These results were consistent with our previous study. 20 In brief, certain molecular mechanisms by which mortalin participates in carcinogenesis are not completely understood. Mortalin activates the Wnt/β-catenin pathway and, consequently, modulates EMT progression directly or indirectly.…”

Section: Discussionmentioning

confidence: 99%

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Mortalin contributes to colorectal cancer by promoting proliferation and epithelial–mesenchymal transition

Zhang

Cui

et al. 2019

IUBMB Life

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This study focused on the expression of mortalin in colorectal cancer (CRC). Mortalin activated the Wnt/β‐catenin pathway to accelerate cell proliferation and the epithelial–mesenchymal transition (EMT) program. Data from online databases displayed that the expression of mortalin was high in CRC, which was further validated using clinical specimens. Meanwhile, high mortalin expression was positively associated with a poor overall survival rate. Suppression of mortalin inhibited CRC cell proliferation as evaluated by the 3‐(4,5‐dimethyl‐2‐thiazolyl)‐2,5‐diphenyl‐2‐H‐tetrazolium bromide (MTT), colony formation, and immunofluorescence staining assays. In addition, depletion of mortalin inhibited CRC cell EMT progression and deactivated the Wnt/β‐catenin pathway. Altogether, mortalin is highly expressed in CRC and may indicate a poor prognosis. Mortalin accelerated CRC progression by stimulating cell proliferation and the EMT program. This study may provide a potential clinical therapeutic target for CRC.

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Section: Discussionsupporting

confidence: 93%

Section: Analysis Of the Ihc Resultsmentioning

confidence: 99%

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Mortalin contributes to colorectal cancer by promoting proliferation and epithelial–mesenchymal transition

Zhang

Cui

et al. 2019

IUBMB Life

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“…Similarly, the elevated expression of GRP75 in intrahepatic cholangiocarcinoma cells was associated with EMT induction, which was accompanied by a decrease of the E-cadherin level while increasing the expression of vimentin and Snail; the suppression of GRP75 expression resulted in reverse effects, namely the accumulation of E-cadherin and downregulation of vimentin and Snail expression [253]. The EMT induction associated with GRP75-dependent activation of the Wnt/β-catenin signaling pathway was described for ovarian carcinoma [254] and colorectal cancer [255]. All these references [251][252][253][254][255] provide evidence that GRP75 does promote EMT in cancer cells, thus driving them to a stem (invasive and metastatic) phenotype.…”

Section: Grp75mentioning

confidence: 84%

“…The EMT induction associated with GRP75-dependent activation of the Wnt/β-catenin signaling pathway was described for ovarian carcinoma [254] and colorectal cancer [255]. All these references [251][252][253][254][255] provide evidence that GRP75 does promote EMT in cancer cells, thus driving them to a stem (invasive and metastatic) phenotype.…”

Section: Grp75mentioning

confidence: 97%

Molecular Chaperones in Cancer Stem Cells: Determinants of Stemness and Potential Targets for Antitumor Therapy

Kabakov

Yakimova

Matchuk

2020

Cells

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Cancer stem cells (CSCs) are a great challenge in the fight against cancer because these self-renewing tumorigenic cell fractions are thought to be responsible for metastasis dissemination and cases of tumor recurrence. In comparison with non-stem cancer cells, CSCs are known to be more resistant to chemotherapy, radiotherapy, and immunotherapy. Elucidation of mechanisms and factors that promote the emergence and existence of CSCs and their high resistance to cytotoxic treatments would help to develop effective CSC-targeting therapeutics. The present review is dedicated to the implication of molecular chaperones (protein regulators of polypeptide chain folding) in both the formation/maintenance of the CSC phenotype and cytoprotective machinery allowing CSCs to survive after drug or radiation exposure and evade immune attack. The major cellular chaperones, namely heat shock proteins (HSP90, HSP70, HSP40, HSP27), glucose-regulated proteins (GRP94, GRP78, GRP75), tumor necrosis factor receptor-associated protein 1 (TRAP1), peptidyl-prolyl isomerases, protein disulfide isomerases, calreticulin, and also a transcription heat shock factor 1 (HSF1) initiating HSP gene expression are here considered as determinants of the cancer cell stemness and potential targets for a therapeutic attack on CSCs. Various approaches and agents are discussed that may be used for inhibiting the chaperone-dependent development/manifestations of cancer cell stemness.

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ENSMUST00000147869 regulates proliferation and fibrosis of mesangial cells in diabetic nephropathy by interacting with Hspa9

et al. 2022

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Our previous study showed that ENSMUST00000147869 was abnormally low expressed in the early stage of diabetic nephropathy (DN). ENSMUST000 00147869 could inhibit the fibrosis and proliferation of mouse mesangial cells (MMCs), but the mechanism is still unclear. This study aims to explore the specific mechanism underline ENSMUST00000147869 regulates the proliferation and fibrosis of MMCs in DN. Nucleocytoplasmic fractionation was applied to define the location of ENSMUST00000147869 in MMCs. RNA-protein pulldown, RNA immunoprecipitation and mass spectrometry were used to identify upregulated Hspa9 directly interacting with ENSMUST00000147869. SiRNA and lentivirus packaging were used to clarify the role of Hspa9 downregulated by ENSMUST00000147869 in promoting proliferation and fibrosis in MMCs. CHX and MG132 were used to clarify the regulatory role of ENSMU ST00000147869 to Hspa9. Immunoprecipitation confirmed the binding of Hspa9 and HMGB1. HSPA9 was a direct binding protein of ENSMU ST00000147869, and ENSMUST00000147869 could inhibit proliferation and fibrosis of MMCs by down-regulating HSPA9 through ubiquitination process. HMGB1 was the downstream binding protein of Hspa9, and ENSMUS T00000147869 could inhibit the interaction between Hspa9 and HMGB1. Our data showed that ENSMUST00000147869 regulates Hspa9 through the ubiquitin proteasome pathway and inhibits the binding of Hspa9 and HMGB1.The ENSMUST00000147869/Hspa9/HMGB1 axis may act as a diagnostic molecular marker and an effective therapeutic target for DN.

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Mortalin is a distinct bio-marker and prognostic factor in serous ovarian carcinoma

Cited by 31 publications

References 44 publications

Mortalin contributes to colorectal cancer by promoting proliferation and epithelial–mesenchymal transition

Mortalin contributes to colorectal cancer by promoting proliferation and epithelial–mesenchymal transition

Molecular Chaperones in Cancer Stem Cells: Determinants of Stemness and Potential Targets for Antitumor Therapy

ENSMUST00000147869 regulates proliferation and fibrosis of mesangial cells in diabetic nephropathy by interacting with Hspa9

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