Lipid-binding serum glycoprotein airway smooth muscle contractility by binding to and inhibiting the Ca2+ influx channel Orai1. BPI; BPIL1; BPIL2; BPIL3; CETP; LBP; LPLUNC1; LPLUNC3; LPLUNC4; PLTP; PLUNC; SPLUNC2; Lipid-binding serum glycoprotein In molecular biology, the lipid-binding serum glycoproteins family, also known as the BPI/LBP/Plunc family or LBP/BPI/CETP family represents a family which includes mammalian lipid-binding serum glycoproteins. Members of this family include: These proteins consist of N- and C-terminal domains, which share a similar two-layer alpha/beta structure, but show little sequence identity to each other. Bactericidal permeability-increasing protein (BPI) is a potent antimicrobial protein of 456 amino acids that binds to and
Secretory component Secretory component The secretory component is a component of immunoglobulin A (IgA). Secretory component is a proteolytic cleavage product of the polymeric immunoglobulin receptor which remains associated with dimeric IgA in sero-mucus secretions. Polymeric IgA binds to the polymeric immunoglobulin receptor on the basolateral surface of epithelial cells and is taken up into the cell via transcytosis. The receptor-IgA complex passes through the cellular compartments before being secreted on the luminal surface of the epithelial cells, still attached to the receptor. Proteolysis of the receptor occurs and the dimeric IgA molecule, along with the secretory component, are free to diffuse