Chemiluminescence Immunoassay Method of Urinary Liver Fatty-acid-binding Protein as a Promising Candidate for Kidney Disease

Niu, Lisong; Li, Lanya; Li, Jinshan; Chen, Zhitian; Lin, Jiayuan; Zhang, Bo; Fu, Xiaoling

doi:10.1007/s10895-022-03120-z

Cited by 1 publication

(1 citation statement)

References 27 publications

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“…Studies have shown that FABP1 is closely related to the occurrence and development of diabetes [ 22 ]. It is also considered an early marker of diabetic nephropathy to predict the outcome of the disease due to its sensitive indicator of kidney injury [ 1 , 2 , 37 ]. Recently, H-FABP (FABP3) has emerged as another potentially promising biomarker for myocardial injury because it increases as early as 0–3 h from the onset of acute myocardial infarction [ 56 , 58 ].…”

Section: Discussionmentioning

confidence: 99%

Menin orchestrates hepatic glucose and fatty acid uptake via deploying the cellular translocation of SIRT1 and PPARγ

Liu,

Li,

Sun

et al. 2023

Cell Biosci

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Background Menin is a scaffold protein encoded by the Men1 gene, which interacts with various transcriptional proteins to activate or repress cellular processes and is a key mediator in multiple organs. Both liver-specific and hepatocyte-specific Menin deficiency promotes high-fat diet-induced liver steatosis in mice, as well as insulin resistance and type 2 diabetic phenotype. The potential link between Menin and hepatic metabolism homeostasis may provide new insights into the mechanism of fatty liver disease. Results Disturbance of hepatic Menin expression impacts metabolic pathways associated with non-alcoholic fatty liver disease (NAFLD), including the FoxO signaling pathway, which is similar to that observed in both oleic acid-induced fatty hepatocytes model and biopsied fatty liver tissues, but with elevated hepatic Menin expression and inhibited FABP1. Higher levels of Menin facilitate glucose uptake while restraining fatty acid uptake. Menin targets the expression of FABP3/4/5 and also CD36 or GK, PCK by binding to their promoter regions, while recruiting and deploying the cellular localization of PPARγ and SIRT1 in the nucleus and cytoplasm. Accordingly, Menin binds to PPARγ and/or FoxO1 in hepatocytes, and orchestrates hepatic glucose and fatty acid uptake by recruiting SIRT1. Conclusion Menin plays an orchestration role as a transcriptional activator and/or repressor to target downstream gene expression levels involved in hepatic energy uptake by interacting with the cellular energy sensor SIRT1, PPARγ, and/or FoxO1 and deploying their translocations between the cytoplasm and nucleus, thereby maintaining metabolic homeostasis. These findings provide more evidence suggesting Menin could be targeted for the treatment of hepatic steatosis, NAFLD or metabolic dysfunction-associated fatty liver disease (MAFLD), and even other hepatic diseases. Graphical Abstract

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