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
Envelope glycoprotein GP120 the neuronal cells, and it is also known to activate STAT1 and induce interleukins IL-6 and IL-8 secretion in neuronal cells. Envelope glycoprotein GP120 Envelope glycoprotein GP120 (or gp120) is a glycoprotein exposed on the surface of the HIV envelope. It was discovered by Professors Tun-Hou Lee and Myron "Max" Essex of the Harvard School of Public Health in 1988. The 120 in its name comes from its molecular weight of 120 kDa. Gp120 is essential for virus entry into cells as it plays a vital role in attachment to specific cell surface receptors. These receptors are DC-SIGN, Heparan Sulfate