Emd, also known as Emerin, is a skeletal protein. Abnormal nuclear structure caused by its dysregulation is common in tumour cells. It has been found to play a role in glucose metabolism, where it promotes glycolysis and inhibits aerobic oxidation in lung adenocarcinoma by interacting with PDHA [1].

In lung adenocarcinoma, Emd was highly expressed, and its high expression promoted malignant phenotypes. The ISGylation at lysine 37 of Emd inhibited lysine 36 ubiquitination, upregulating Emd stability. Emd bound with PDHA, stimulating serine 293 and 300 phosphorylation, inhibiting PDHA expression, and facilitating glycolysis of glucose that should enter the aerobic oxidation pathway. In clinical specimens, Emd was negatively associated with PDHA, while positively associated with Emd ISGylation, tumour stage, and diameter [1].

In conclusion, Emd is a significant protein in the context of lung adenocarcinoma, with its role in glucose metabolism—specifically inhibiting aerobic oxidation—being a key finding. Understanding Emd's function in this disease through such research can potentially provide new strategies for lung adenocarcinoma treatment.

References:

1. Zhang, Congcong, Cui, Jiangtao, Cao, Leiqun, Xia, Jinjing, Zhang, Xiao. 2022. ISGylation of EMD promotes its interaction with PDHA to inhibit aerobic oxidation in lung adenocarcinoma. In Journal of cellular and molecular medicine, 26, 5078-5094. doi:10.1111/jcmm.17536. https://pubmed.ncbi.nlm.nih.gov/36071546/