Serpin family A member 12 (SERPINA12)

Serpin family A member 12 (SERPINA12), commonly called vaspin, is a secreted serine protease inhibitor predominantly produced in visceral adipose tissue. It functions as an adipokine and specifically inhibits the serine protease kallikrein 7, protecting insulin from degradation and thereby modulating insulin sensitivity and glucose homeostasis. Vaspin also interacts with the cell surface chaperone protein GRP78 (heat shock protein family A member 5), initiating intracellular signaling via AKT, AMPK, and MAPK pathways. SERPINA12 has established roles in lipid metabolism, inflammation, and may influence angiogenesis and cell proliferation. Dysregulation of SERPINA12/vaspin is associated with obesity, insulin resistance, type 2 diabetes, and several endocrine pathologies. Serum vaspin/ SERPINA12 concentrations are under investigation as biomarkers for metabolic diseases[1][2][3].

Other names

Serpin A12VaspinOL-64Visceral adipose tissue-derived serine protease inhibitorVisceral adipose-specific serpinserpin peptidase inhibitor clade A member 12

Inhibition of target serine proteases (especially kallikrein 7) to protect insulin from degradation and modulate metabolic homeostasis; Intracellular signaling modulation via binding to GRP78/Heat shock protein family A member 5 on the cell surface, activating kinase pathways.