MSR1 was first described in 1979 by Brown and Goldstein, who demonstrated that it mediated the uptake and degradation of acetylated low-density lipoprotein (acetyl-LDL) but not non-modified low-density lipoprotein (LDL) . This receptor is involved in the phagocytosis of a wide range of ligands, including modified lipoproteins, bacterial pathogens, and apoptotic cells .
The role of MSR1 in health and disease is often dichotomous, being either host-protective or detrimental to the pathogenesis of disease . For instance, MSR1 is important for M2 macrophage polarization, which is associated with anti-inflammatory responses and tissue repair . However, altered expression of MSR1 can contribute to the pathogenesis of various diseases. For example, elevated levels of MSR1 have been observed in patients with fulminant hepatitis, where it promotes neutrophil-mediated complement activation .
The recombinant expression of human MSR1 in sf9 cells (a cell line derived from the fall armyworm, Spodoptera frugiperda) is a common method used to produce this protein for research purposes . The sf9 cell line is widely used in the baculovirus expression system, which allows for high-level expression of recombinant proteins with post-translational modifications similar to those in mammalian cells .
Recombinant MSR1 produced in sf9 cells is used in various research applications, including studies on receptor-ligand interactions, the role of MSR1 in disease pathogenesis, and the development of therapeutic strategies targeting MSR1 . By understanding the molecular mechanisms influencing MSR1 expression and function, researchers can gain insights into its role in health and disease and explore potential therapeutic interventions .