S-nitrosoproteomics profiling elucidates the regulatory mechanism of S-nitrosylation on beef quality.
Meat Sci
; 216: 109580, 2024 Oct.
Article
in En
| MEDLINE
| ID: mdl-38941777
ABSTRACT
This study aimed to quantitively profile the S-nitrosylation in beef semimembranosus (SM) with different treatments (nitric oxide donor or nitric oxide synthase inhibitor) by applying iodoTMT-based nitrosoproteomics. Results showed that 2096 S-nitrosylated cysteine sites in 368 proteins were detected in beef SM. Besides, differential SNO-modified proteins were screened, some of which were involved in crucial biochemical pathways, including calcium-releasing-related proteins, energy metabolic enzymes, myofibrils, and cytoskeletal proteins. GO analysis indicated that differential proteins were localized in a wide range of cellular compartments, such as cytoplasm, organelle, and mitochondrion, providing a prerequisite for S-nitrosylation exerting broad roles in post-mortem muscles. Furthermore, KEGG analysis validated that these proteins participated in the regulation of diverse post-mortem metabolic processes, especially glycolysis. To conclude, changes of S-nitrosylation levels in post-mortem muscles could impact the structure and function of crucial muscle proteins, which lead to different levels of muscle metabolism and ultimately affect beef quality.
Key words
Full text:
1
Database:
MEDLINE
Main subject:
Muscle, Skeletal
/
Proteomics
/
Red Meat
/
Muscle Proteins
Limits:
Animals
Language:
En
Journal:
Meat Sci
Journal subject:
CIENCIAS DA NUTRICAO
Year:
2024
Type:
Article