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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
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The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
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  1. Home
  2. Research Domains
  3. Biomedical And Clinical Sciences
  4. Oncology And Carcinogenesis
  5. Predictive And Prognostic Markers
  6. Ubiquitin-specific Protease 14 Targets Pfkl-mediated Glycolysis To Promote The Proliferation And Migration Of Oral Squamous Cell Carcinoma.
  1. Home
  2. Research Domains
  3. Biomedical And Clinical Sciences
  4. Oncology And Carcinogenesis
  5. Predictive And Prognostic Markers
  6. Ubiquitin-specific Protease 14 Targets Pfkl-mediated Glycolysis To Promote The Proliferation And Migration Of Oral Squamous Cell Carcinoma.

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Ubiquitin-specific protease 14 targets PFKL-mediated glycolysis to promote the proliferation and migration of oral squamous cell carcinoma.

Xingming Zhang1, Lou Geng1, Yi Tang1

  • 1Department of Clinical Laboratory, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, 200011, China.

Journal of Translational Medicine
|February 22, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

Aberrant upregulation of ubiquitin-specific protease 14 (USP14) promotes oral cancer progression by stabilizing key glycolytic enzyme PFKL. This USP14-PFKL axis drives tumor growth and metastasis, offering new therapeutic targets.

Keywords:
DeubiquitinationGlycolysisOSCCPFKL

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Area of Science:

  • Oncology
  • Biochemistry
  • Molecular Biology

Background:

  • Aberrant ubiquitin-specific protease 14 (USP14) expression is linked to various cancers, including oral squamous cell carcinoma (OSCC).
  • Overexpression of USP14 correlates with adverse clinicopathological features and poor prognosis in OSCC patients.
  • USP14 is hypothesized to function as a tumor-promoting factor in OSCC progression.

Purpose of the Study:

  • To investigate the role of USP14 in the progression of oral squamous cell carcinoma (OSCC).
  • To elucidate the molecular mechanism by which USP14 contributes to OSCC tumorigenesis and metastasis.
  • To identify USP14 as a potential therapeutic target for OSCC.

Main Methods:

  • Investigated USP14 expression in OSCC tissues and correlated it with clinicopathological features and patient prognosis.
USP14
  • Identified USP14 as a deubiquitinating enzyme for phosphofructokinase-1 liver type (PFKL).
  • Examined the interaction between USP14 and PFKL, and its impact on glycolysis, proliferation, migration, and tumorigenesis in OSCC cells.
  • Main Results:

    • USP14 is aberrantly upregulated in OSCC and associated with poor prognosis.
    • USP14 directly deubiquitinates and stabilizes PFKL, a rate-limiting glycolytic enzyme.
    • USP14-mediated enhancement of PFKL activity promotes OSCC cell proliferation, migration, and tumorigenesis.
    • USP14 acts as a critical regulator of glycolysis in OSCC, influencing tumor growth and metastasis.

    Conclusions:

    • USP14 plays a significant tumor-promoting role in oral squamous cell carcinoma.
    • USP14 enhances glycolysis by stabilizing PFKL, thereby driving OSCC progression.
    • Targeting USP14 presents a promising therapeutic strategy for OSCC treatment.