Results 11 to 20 of about 5,491 (207)

Lactylation and Central Nervous System Diseases

Brain Sciences
As the final product of glycolysis, lactate serves as an energy substrate, metabolite, and signaling molecule in various diseases and mediates lactylation, an epigenetic modification that occurs under both physiological and pathological conditions ...
Ye Chen, Dongqiong Xiao, Xihong Li
doaj   +3 more sources

Protein lactylation induced by neural excitation [PDF]

Cell Reports, 2021
Abstract Lactate is known to have diverse roles in the brain at the molecular and behavioral levels under both physiological and pathophysiological conditions, such as learning and memory and regulation of mood. Recently, a novel post-translational modification called lysine lactylation has been found in histone H3 of
Hideo Hagihara, Hirotaka Shoji, Hikari Otabi, Atsushi Toyoda, Kaoru Katoh, Masakazu Namihira, Tsuyoshi Miyakawa   +6 more
openaire   +3 more sources

Lysine lactylation in diseases: beyond histone lactylation

Cell Death & Disease
Abstract Lactylation, a recently identified post-translational modification, was initially characterized as lysine residue modification in histone subunits that regulates gene transcription via epigenetic mechanisms. Elevated intracellular lactate has been shown to drive histone lysine lactylation (Kla), establishing its association ...
Yiming Liu, Xuan Guo, Xinyang Hu, Sining Zhou, Qi Yang, Pingping Feng, Linghui Zeng   +6 more
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Über Lactyl‐p‐aminobenzoesäure [PDF]

Berichte der deutschen chemischen Gesellschaft, 1917
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Lactylation and antitumor immunity

Frontiers in Immunology
Lactylation, a recently discovered post-translational modification (PTM), plays a critical role in cancer biology. Warburg effect induces lactate accumulation, which serves as a metabolic end-product and intercellular signaling mediator within the tumor microenvironment (TME).
Yang, Biao, Li, Lingyu, Shi, Dongmei, Zhong, Tao, Xiong, Huabao   +4 more
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Lactylation and human disease

Expert Reviews in Molecular Medicine
Abstract Background Lactylation, a new epigenetic modification, is an important way in which lactate exerts physiological functions. There is a close relationship between increased lactylations caused by lactate and glycolysis, which can interact and play a role in disease through lactate as an intermediate mediator.
Linlin Wan, HuiJuan Zhang, Jialing Liu, Qian He, Jiumei Zhao, Chenglong Pan, Kepu Zheng, Yu Tang   +7 more
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PRMT1‐Mediated LDHA Methylation Drives STAT3 Lactylation to Orchestrate Intestinal Inflammation and Tumorigenesis

Advanced Science, EarlyView.
This study identifies an immunometabolic axis wherein SAM‐driven PRMT1 methylates LDHA, enhancing its activity. The resultant lactate induces STAT3 K709 lactylation, which stabilizes an active conformation to promote STAT3 phosphorylation and IL‐10 expression.
Hui Wang, Mengyu Zhang, Weipeng Gong, Jiaxuan Wu, Junping Zhang, Wenxiu Zhang, Yue Liu, Kui Wang, Canhua Huang, Jun Zhou, Sijin Wu, Yan Li, Tianliang Li   +12 more
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Lactate and lactylation in cancer

Signal Transduction and Targeted Therapy
Abstract Accumulated evidence has implicated the diverse and substantial influence of lactate on cellular differentiation and fate regulation in physiological and pathological settings, particularly in intricate conditions such as cancer. Specifically, lactate has been demonstrated to be pivotal in molding the tumor microenvironment (TME ...
Jie Chen, Ziyue Huang, Ya Chen, Hao Tian, Peiwei Chai, Yongning Shen, Yiran Yao, Shiqiong Xu, Shengfang Ge, Renbing Jia   +9 more
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Phosphorylation‐Facilitated CKB Lactylation At K11 By GCN5 Enhances Creatine Kinase Activity and Mitigates Neuronal Damage After Cerebral Ischemia‐Reperfusion

Advanced Science, EarlyView.
This study uncovers hierarchical coordination between K11 lactylation and S199 phosphorylation of CKB in cerebral ischemia‐reperfusion injury. Such dual modifications potentiate CKB enzymatic function, remodel energy metabolism, alleviate oxidative stress and neuronal damage, and represent a viable therapeutic target for stroke treatment.
Chao Duan, Ruolin Zhang, Shihui Ding, Ying Feng, Tao Shen, Ziwei Wang, Wendai Bao, Ke Shui, Jun Qin, Jun Chen, Min Zhang, Zijing Ren, Dongmei Zhao, Xingrong Guo, Zhibing Ai, Xin Yang, Peiyang Zhou, Zhiqiang Dong   +17 more
wiley   +1 more source

HNRNPU K181 Lactylation Drives Cervical Cancer Growth by Upregulating PHGDH and Reprogramming Serine Metabolism

Advanced Science, EarlyView.
Lactate in cervical cancer induces HNRNPU K181 lactylation, opposed by NAA50‐mediated acetylation and suppressed by Pazopanib. This lactylation enhances HNRNPU binding to PHGDH pre‐mRNA exon 1, maintaining exon 1‐containing transcripts and mRNA stability, thereby activating serine metabolism.
Chang Zhang, Qingfei Meng, Hui Jiao, Huixin Liu, Xiangchao Wang, Honglan Zhou, Yishu Wang   +6 more
wiley   +1 more source