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Papers In Press, published online ahead of print January 30, 2001
Pulmonary Biology, Children's Hospital Medical Center, Cincinnati, OH 45229-3039
Corresponding Author: tim.weaver{at}chmcc.org
Proteolytic processing of surfactant protein C (SP-C) proprotein in multivesicular bodies of alveolar type II cells results in a 35-residue mature peptide, consisting of a transmembrane domain and a 10-residue extramembrane domain. SP-C mature peptide is stored in lamellar bodies (a lysosomal-like organelle) and secreted with surfactant phopholipids into the alveolar space. This study was designed to identify the peptide domain of SP-C required for sorting and secretion of this integral membrane peptide. Deletion analyses in transiently transfected PC12 cells and isolated mouse type II cells suggested the extramembrane domain of mature SP-C was cytosolic and sufficient for sorting to the regulated secretory pathway. Intratracheal injection of adenovirus encoding SP-C mature peptide resulted in secretion into the alveolar space of wildtype mice but not SP-C (-/-) mice. SP-C secretion in null mice was restored by addition of the N-terminal propeptide. The cytosolic domain, consisting of the N-terminal propeptide and extramembrane domain of mature SP-C peptide, supported secretion of the transmembrane domain of PDGFR. Collectively, these studies indicate that the N-terminal propeptide of SP-C is required for intracellular sorting and secretion of SP-C.
J. Biol. Chem, 10.1074/jbc.M011770200
Submitted on December 28, 2000
Revised on January 25, 2001
Accepted on January 30, 2001
Secretion of surfactant protein C (SP-C), an integral membrane protein requires the N-terminal propeptide
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