Processing of pulmonary surfactant protein B by napsin and cathepsin H
作者： Takayuki Ueno , Stig Linder , Cheng-Lun Na , Ward R. Rice , Jan Johansson
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摘要: Surfactant protein B (SP-B) is an essential constituent of pulmonary surfactant. SP-B synthesized in alveolar type II cells as a preproprotein and processed to the mature peptide by cleavage NH2- COOH-terminal peptides. An aspartyl protease has been suggested cleave NH2-terminal propeptide resulting 25-kDa intermediate. Napsin, expressed cells, was detected fetal lung homogenates early day 16 gestation, 1 before onset expression processing. Napsin localized multivesicular bodies, site proprotein processing cells. Incubation from with crude membrane extract napsin-transfected resulted enhanced levels Purified napsin cleaved recombinant SP-B/EGFP fusion within between Leu178 Pro179, 22 amino acids upstream NH2 terminus SP-B. Cathepsin H, cysteine also implicated pro-SP-B processing, 13 did not peptide, whereas cathepsin H boundary at several other sites peptide. Knockdown small interfering RNA decreased SP-C These results suggest that napsin, least one enzyme are involved maturation biologically active
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