This study investigated the effects of lactate levels in broiler breast on protein lactylation modification, meat quality, and their correlation. High lactate injections led to increased lactate levels in both serum and breast muscle, and significantly reduced the values of pH, pH and pH. Additionally, the lactylation levels in breast muscle were increased both post-slaughter and post-mortem. Protein lactylation in breast muscle occurred through enzymatic and non-enzymatic pathways at these stages, with the underlying mechanisms varying according to lactate levels and the muscle aging process. Correlation analysis revealed that post-slaughter lactylation contributed to breast muscle morphometry, whereas post-mortem lactylation was associated with meat quality and texture profile. These findings could demonstrate the presence and dynamic patterns of protein lactylation in broiler breast muscles, offering new insights into the role of lactate accumulation in meat quality variation.
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http://dx.doi.org/10.1016/j.foodchem.2025.143613 | DOI Listing |
Mol Cell
March 2025
Department of Experimental and Clinical Biomedical Sciences "Mario Serio, " University of Florence, Viale Morgagni 50, 50134 Florence, Italy. Electronic address:
The recently discovered lysine lactylation represents a critical post-translational modification with widespread implications in epigenetics and cancer biology. Initially identified on histones, lysine lactylation has been also described on non-histone proteins, playing a pivotal role in transcriptional activation, protein function, and cellular processes. Two major sources of the lactyl moiety have been currently distinguished: L-lactyl-CoA (precursor of the L-lactyl moiety) and S-D-lactylglutathione (precursor of the D-lactyl moiety), which enable enzymatic and non-enzymatic mechanisms of lysine lactylation, respectively.
View Article and Find Full Text PDFInt Immunopharmacol
March 2025
Department of Obstetrics and Gynecology, Key Laboratory of Birth Defects and Related Diseases of Women and Children, Ministry of Education, West China Second University Hospital, Sichuan University, Chengdu 610041, People's Republic of China. Electronic address:
T cells play an important role in adaptive immune responses, providing antigen specificity for pathogen and tumor recognition. Recent studies have elucidated the complex interplay between T cell metabolism and broad epigenetic modifications in response to tumors, occurring at transcriptional, post-transcriptional, and post-translational levels. At the transcriptional level, gene expression is regulated through mechanisms such as DNA methylation, chromatin remodeling, and transcription factor activity.
View Article and Find Full Text PDFJ Appl Toxicol
March 2025
Joint Research Center for Occupational Medicine and Health of IHM and School of Public Health, Anhui University of Science and Technology, Hefei, Anhui, China.
As a group I carcinogen, environmental exposures to formaldehyde (FA) have been associated with various types of malignancies. However, exact mechanisms of FA-triggered carcinogenesis are still not clear. Lactylation is recently identified as a post-translational modification driven by overproduced lactic acid (LA) that regulates protein activities in different cellular processes.
View Article and Find Full Text PDFSci Rep
March 2025
Department of Pathology, Henan Provincial People's Hospital, People's Hospital of Zhengzhou University, People's Hospital of Henan University, Zhengzhou, 450003, Henan, China.
Background Posttranslational modifications of histone lysine (K) have integral connections with cell metabolism, and participate in the carcinogenesis of various cancers. This study focuses on evaluating the expression of histone H4 lys 5 lactylation (H4K5lac) and its clinical role in breast cancer (BC). Methods During this research, immunohistochemistry (IHC) and immunoblotting, utilizing a specific primary anti-L-lactyl-histone H4 (Lys 5) rabbit monoclonal antibody, were employed to assess H4K5lac expression in BC tissue chips.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
March 2025
Ben May Department for Cancer Research, The University of Chicago, Chicago, IL 60637.
The recently identified histone modification lysine lactylation can be stimulated by L-lactate and glycolysis. Although the chemical group added upon lysine lactylation was originally proposed to be the L-enantiomer of lactate (K), two isomeric modifications, lysine D-lactylation (K) and N-ε-(carboxyethyl) lysine (K), also exist in cells, with their precursors being metabolites of glycolysis. The dynamic regulation and differences among these three modifications in response to hypoxia remain poorly understood.
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