Glyceraldehyde‐3‐phosphate dehydrogenase promotes liver tumorigenesis by modulating phosphoglycerate dehydrogenase

Liu, Shanshan; Sun, Yu; Jiang, Ming; Li, Yangkai; Tian, Ye; Xue, Weili; Ding, Ninghe; Sun, Yue; Cheng, Cheng; Li, Jianshuang; Miao, Xiaoping; Liu, Xinran; Zheng, Ling; Huang, Kun

doi:10.1002/hep.29202

Cited by 72 publications

(47 citation statements)

References 48 publications

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“…Total RNA was isolated from cells using Trizol (Invitrogen). Two micrograms of RNA was used to synthesize the first single-strand cDNA using RevertAid™ First Strand cDNA Synthesis Kit (Fermentas, Vilnius, Lithuania) as previously reported 43 , 44 . Relative quantification of PRC1 in cells was determined using a Bio-Rad CFX96™ Real-Time PCR Detection System with Power SYBR ® Green PCR Master Mix (Applied Biosystems, Carlsbad, CA).…”

Section: Methodsmentioning

confidence: 99%

Reducing protein regulator of cytokinesis 1 as a prospective therapy for hepatocellular carcinoma

Liu

Meng

et al. 2018

Cell Death Dis

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Proteins that bind to microtubule are important for cell cycle, and some of these proteins show oncogenic characteristics with mechanisms not fully understood. Herein we demonstrate overexpression of protein regulator of cytokinesis 1 (PRC1), a microtubule-associated regulator of mitosis, in human hepatocellular carcinoma (HCC). Moreover, upregulated PRC1 is associated with lower survival rates of HCC patients. Mechanistically, reducing PRC1 blocks mitotic exit of HCC cells at telophase in a spindle assembly checkpoint independent manner, and acts synergistically with microtubule-associated agents (MTAs) to suppress p53-wt or p53-null HCC cells in a p53- or p14ARF-dependent manner; while overexpressing PRC1 increases the resistance of HCC to taxol. A combined treatment of taxol/shPRC1 results in 90% suppression of tumor growth in subcutaneous HCC xenograft models. In orthotopic xenograft mice, reducing PRC1 significantly alleviates HCC development and hepatic injury. Together, our results suggest a dual-mitotic suppression approach against HCC by combining MTAs with cytokinesis inhibition, which blocks mitosis at both metaphase and telophase.

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Section: Methodsmentioning

confidence: 99%

Reducing protein regulator of cytokinesis 1 as a prospective therapy for hepatocellular carcinoma

Liu

Meng

et al. 2018

Cell Death Dis

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“…NAD + -dependent enzyme 3-phosphoglycerate dehydrogenase (PHGDH) is the first and only rate-limiting enzyme in the serine and glycine de novo biosynthetic pathway [10]. It catalyzes glycolytic intermediate 3-phosphoglycerate (3-PG) transformed into 3-phosphohydroxypyruvate (3-PHP) [11,12]. Subsequent enzymatic reactions in the pathway convert 3-PHP to serine via transamination (PSAT1) and phosphate ester hydrolysis (PSPH).…”

Section: Introductionmentioning

confidence: 99%

The Role of D-3-Phosphoglycerate Dehydrogenase in Cancer

Zhao¹,

Fu²,

Du³

et al. 2020

Int. J. Biol. Sci.

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Serine, a non-essential amino acid, can be imported from the extracellular environment by transporters and de novo synthesized from glycolytic 3-phosphoglycerate (3-PG) in the serine biosynthetic pathway (SSP). It has been reported that active serine synthesis might be needed for the synthesis of proteins, lipids, and nucleotides and the balance of folate metabolism and redox homeostasis, which are necessary for cancer cell proliferation. Human D-3-phosphoglycerate dehydrogenase (PHGDH), the first and only rate-limiting enzyme in the de novo serine biosynthetic pathway, catalyzes the oxidation of 3-PG derived from glycolysis to 3-phosphohydroxypyruvate (3-PHP). PHGDH is highly expressed in tumors as a result of amplification, transcription, or its degradation and stability alteration, which dysregulates the serine biosynthesis pathway via metabolic enzyme activity to nourish tumors. And some recent researches reported that PHGDH promoted some tumors growth via non-metabolic way by upregulating target cancer-promoting genes. In this article, we reviewed the type, structure, expression and inhibitors of PHGDH, as well as the role it plays in cancer and tumor resistance to chemotherapy.

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“…Immunostaining was performed to further verify the difference on inflammatory reaction between BC and CMBC. F4/80 was a maker of macrophage and was always used for the identification of degree of inflammation . After the panmacrophage marker F4/80 staining, the surface of BC was positive stained, which indicated the macrophage infiltration and inflammation ( Figure 6 ).…”

Section: Resultsmentioning

confidence: 99%

“…MTT assay was performed according to a previously reported method . Briefly, HCE cells were plated at a density of 5000 cells per well, with BC/CMBC, in 96‐well culture plates.…”

Section: Methodsmentioning

confidence: 99%

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Improved Cell Viability and Biocompatibility of Bacterial Cellulose through in Situ Carboxymethylation

Zhou

Sun

Bao

et al. 2019

Macromolecular Bioscience

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Bacterial cellulose (BC) is a natural product with multiple properties, which has been utilized in tissue engineering. However, cell adhesion and proliferation are reported to be weaker on native BC, providing less support compared to other types of biomaterials, like collagen. To increase the biocompatibility and the medical performance of BC, in situ modification is used to add carboxymethyl group to BC. By partially changing the structure and physical properties of BC, carboxymethylation significantly increases cell affinity and viability, especially on the initial cell adhesion. Furthermore, in the in vivo implantation, the tissue reaction shows that carboxymethylation significantly increases the biocompatibility of BC, exhibiting better tissue condition and a lower inflammatory reaction which are proved through HE staining and immunohistochemistry. The data prove that in situ carboxymethylation is a simple and direct way of improving the performance of BC in medical applications.

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Glyceraldehyde‐3‐phosphate dehydrogenase promotes liver tumorigenesis by modulating phosphoglycerate dehydrogenase

Abstract: GAPDH increases histone methylation levels by up-regulating PHGDH, promoting diversion from glycolysis to serine biosynthesis, and consequently accelerating HCC development. (Hepatology 2017;66:631-645).

Cited by 72 publications

References 48 publications

Reducing protein regulator of cytokinesis 1 as a prospective therapy for hepatocellular carcinoma

Reducing protein regulator of cytokinesis 1 as a prospective therapy for hepatocellular carcinoma

The Role of D-3-Phosphoglycerate Dehydrogenase in Cancer

Improved Cell Viability and Biocompatibility of Bacterial Cellulose through in Situ Carboxymethylation

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