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Brain-Type Glycogen Phosphorylase (PYGB) in the Pathologies of Diseases: A Systematic Review.
Yang, Caiting; Wang, Haojun; Shao, Miaomiao; Chu, Fengyu; He, Yuyu; Chen, Xiaoli; Fan, Jiahui; Chen, Jingwen; Cai, Qianqian; Wu, Changxin.
Afiliación
  • Yang C; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • Wang H; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • Shao M; School of Medicine & Holistic Integrative Medicine, Nanjing University of Chinese Medicine, Nanjing 210023, China.
  • Chu F; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • He Y; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • Chen X; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • Fan J; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • Chen J; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
  • Cai Q; Shanghai Key Laboratory of Molecular Imaging, Shanghai University of Medicine and Health Sciences, Shanghai 201318, China.
  • Wu C; Institutes of Biomedical Sciences, Shanxi University, Taiyuan 030006, China.
Cells ; 13(3)2024 Feb 05.
Article en En | MEDLINE | ID: mdl-38334681
ABSTRACT
Glycogen metabolism is a form of crucial metabolic reprogramming in cells. PYGB, the brain-type glycogen phosphorylase (GP), serves as the rate-limiting enzyme of glycogen catabolism. Evidence is mounting for the association of PYGB with diverse human diseases. This review covers the advancements in PYGB research across a range of diseases, including cancer, cardiovascular diseases, metabolic diseases, nervous system diseases, and other diseases, providing a succinct overview of how PYGB functions as a critical factor in both physiological and pathological processes. We present the latest progress in PYGB in the diagnosis and treatment of various diseases and discuss the current limitations and future prospects of this novel and promising target.
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Texto completo: 1 Base de datos: MEDLINE Asunto principal: Glucógeno Fosforilasa / Glucógeno Tipo de estudio: Systematic_reviews Límite: Humans Idioma: En Revista: Cells Año: 2024 Tipo del documento: Article País de afiliación: China

Texto completo: 1 Base de datos: MEDLINE Asunto principal: Glucógeno Fosforilasa / Glucógeno Tipo de estudio: Systematic_reviews Límite: Humans Idioma: En Revista: Cells Año: 2024 Tipo del documento: Article País de afiliación: China