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
Eccrine sweat gland duct, the "acrosyringium"; a dermal duct, consisting of a straight and coiled portion; and a secretory tubule, coiled deep in the dermis or hypodermis. The eccrine gland opens out through the sweat pore. The coiled portion is formed by two concentric layer of columnar or cuboidal epithelial cells. The epithelial cells are interposed by the myoepithelial cells. Myoepithelial cells support the secretory epithelial cells. The duct of eccrine gland is formed by two layers of cuboidal epithelial cells. Eccrine glands are active in thermoregulation by providing cooling from water evaporation of sweat secreted by the glands on the body surface