There are four surfactant-specific proteins, designated surfactant protein A (SP-A), SP-B, SP-C and SP-D respectively. SP-A and SP-D are hydrophilic surfactant proteins and are members of the collectin family. SP-B and SP-C are hydrophobic surfactant proteins and may be the most appropriate indicators for the evolutionary origin of surfactant. SP-B is synthesized by the alveolar type II epithelial cells as a 40-42 kD precursor that is subsequently proteolytically processed to 7.8-8 kD. SP-B enhances the spreading and stability of surfactant phospholipids in the alveolus. SP-B is essential for air-breathing in mammals and is therefore largely conserved. SP-B can interact with both phospholipid head groups and fatty chains and is particularly active in enhancing surface active behavior in endogenous and exogenous lung surfactants. Even low SP-B contents had measurable effects in increasing the adsorption, dynamic surface tension lowering, and/or film respreading of DPPC, mixed synthetic lipids, and column-purified lung surfactant phospholipids. Deficiency of SP-B and other surfactant components is associated with respiratory distress syndrome (RDS) in premature infants and adults with respiratory distress syndrome (ARDS).
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.