Major urinary protein 1 (MUP1)

Major urinary protein 1 (MUP1) is a member of the lipocalin superfamily, characterized by a conserved beta-barrel structure with a central hydrophobic pocket [1, 2]. Primarily synthesized in the liver and secreted into the blood and urine, MUP1 traditionally functions as a transporter and stabilizer for volatile pheromones, playing a key role in chemical communication and social behavior in rodents [1, 5]. Beyond its role in pheromone signaling, MUP1 has emerged as a significant metabolic regulator that modulates glucose and lipid homeostasis [3]. It has been shown to suppress hepatic gluconeogenesis and enhance energy expenditure in skeletal muscle by promoting mitochondrial biogenesis and oxidative function [1, 3]. In animal models of obesity and type 2 diabetes, MUP1 levels are markedly reduced, and the administration of recombinant MUP1 has demonstrated therapeutic potential in ameliorating hyperglycemia and insulin resistance [3, 4]. While MUP genes are highly expanded in rodents and absent in humans, functional analogs like PAEP (glycodelin) are studied for similar roles, and MUP1 itself is a target for developing treatments for metabolic disorders and potentially neuropsychiatric conditions like autism [6].

Other names

MUP-1Major urinary protein IMup7Up-1Ltn-1Mup-aMup10Lvtn-1Mus m 1Alpha-2u-globulin

MUP1 acts as a humoral metabolic regulator that increases mitochondrial biogenesis and oxidative phosphorylation in skeletal muscle, thereby increasing energy expenditure. It also suppresses hepatic gluconeogenesis and improves systemic insulin sensitivity by enhancing insulin signaling pathways.