Semaphorin-3A regulates liver sinusoidal endothelial cell porosity and promotes hepatic steatosis

Nat Cardiovasc Res. 2024 Jun;3(6):734-753. doi: 10.1038/s44161-024-00487-z. Epub 2024 Jun 14.

Abstract

Prevalence of metabolic dysfunction-associated steatotic liver disease (MASLD), formerly known as non-alcoholic fatty liver disease, increases worldwide and associates with type 2 diabetes and other cardiometabolic diseases. Here we demonstrate that Sema3a is elevated in liver sinusoidal endothelial cells of animal models for obesity, type 2 diabetes and MASLD. In primary human liver sinusoidal endothelial cells, saturated fatty acids induce expression of SEMA3A, and loss of a single allele is sufficient to reduce hepatic fat content in diet-induced obese mice. We show that semaphorin-3A regulates the number of fenestrae through a signaling cascade that involves neuropilin-1 and phosphorylation of cofilin-1 by LIM domain kinase 1. Finally, inducible vascular deletion of Sema3a in adult diet-induced obese mice reduces hepatic fat content and elevates very low-density lipoprotein secretion. Thus, we identified a molecular pathway linking hyperlipidemia to microvascular defenestration and early development of MASLD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cells, Cultured
  • Cofilin 1 / genetics
  • Cofilin 1 / metabolism
  • Diabetes Mellitus, Type 2 / genetics
  • Diabetes Mellitus, Type 2 / metabolism
  • Diabetes Mellitus, Type 2 / pathology
  • Diet, High-Fat / adverse effects
  • Disease Models, Animal
  • Endothelial Cells* / metabolism
  • Endothelial Cells* / pathology
  • Humans
  • Liver* / metabolism
  • Liver* / pathology
  • Male
  • Mice
  • Mice, Inbred C57BL*
  • Mice, Knockout
  • Neuropilin-1 / genetics
  • Neuropilin-1 / metabolism
  • Non-alcoholic Fatty Liver Disease* / genetics
  • Non-alcoholic Fatty Liver Disease* / metabolism
  • Non-alcoholic Fatty Liver Disease* / pathology
  • Obesity / genetics
  • Obesity / metabolism
  • Obesity / pathology
  • Phosphorylation
  • Semaphorin-3A* / genetics
  • Semaphorin-3A* / metabolism
  • Signal Transduction*

Substances

  • Semaphorin-3A
  • Neuropilin-1
  • Cofilin 1