Salusins are multifunctional bioactive peptides discovered by bioinformatics analyses of a full-length cDNA library. Salusin alpha and salusin beta are related peptides of 28 and 20 amino acids that were recently characterized. These peptides are considered to be biosynthesized from preprosalusin, an alternative-splicing product of the torsion dystonia-related gene (TOR2A), after frameshift reading and digestion at dibasic amino acids. Salusin alpha has recently been shown to be involved in atherosclerosis; it potently suppresses acyl-CoA:cholesterol acyltransferase-1 which stores cholesterol ester converted from free cholesterol in macrophages, thereby reducing human macrophage foam cell formation.