New Regulatory roles for Human Serum Amyloid A.

Abstract

The current study illuminates the multifaceted role of Serum Amyloid A (SAA), an essential acute-phase protein implicated in diverse biological realms, encompassing inflammation, oncogenesis, and stress modulation. With a focus on delineating the intricate protein-protein interactions orchestrated by SAA, this investigation unravels its diverse functions within the human physiological landscape. Utilizing the HepG2 cell line, renowned for its proficiency in facilitating SAA overexpression, we meticulously generated protein extracts after inducing SAA hyperexpression. Integrating Co-Immunoprecipitation techniques with Liquid Chromatography-Tandem Mass Spectrometry (LC/MS/MS) enabled discernment and characterization of the protein complexes intricately associated with SAA. Our data elucidates a pronounced upregulation in SAA expression levels within induced samples compared to controls, substantiating its pivotal role among inflammatory cascades. Specifically, LC/MS/MS profiling delineated interactions with nine distinct proteins, encompassing pivotal players in actin dynamics, neuronal morphogenesis, lipid homeostasis, and immunomodulation. Furthermore, this investigation underscores the plausible ramifications of these molecular interactions in pathologies, including Alzheimer's disease, oncological manifestations, and rheumatoid arthritis. Through comprehensive analyses, this investigation sheds light on the intricate roles of SAA and provides a foundation for future therapeutic modalities targeting SAA pathologies.