Search results for "Pulmonary Surfactant-Associated Protein B"
showing 2 items of 2 documents
Palmitoylation of Pulmonary Surfactant Protein SP-C Is Critical for Its Functional Cooperation with SP-B to Sustain Compression/Expansion Dynamics in…
2010
AbstractRecent data suggest that a functional cooperation between surfactant proteins SP-B and SP-C may be required to sustain a proper compression-expansion dynamics in the presence of physiological proportions of cholesterol. SP-C is a dually palmitoylated polypeptide of 4.2 kDa, but the role of acylation in SP-C activity is not completely understood. In this work we have compared the behavior of native palmitoylated SP-C and recombinant nonpalmitoylated versions of SP-C produced in bacteria to get a detailed insight into the importance of the palmitic chains to optimize interfacial performance of cholesterol-containing surfactant films. We found that palmitoylation of SP-C is not essenti…
The Surfactant Peptide KL4 Sequence Is Inserted with a Transmembrane Orientation into the Endoplasmic Reticulum Membrane
2008
AbstractSurfactant protein B (SP-B) is an essential component of pulmonary surfactant. Synthetic surfactant peptide KL4, a peptide based on a C-terminal amphipathic helical region of human SP-B, efficiently mimics some functional properties of SP-B and is included in therapeutic surfactant preparations used in trials to treat respiratory distress syndrome. The membrane orientation of this peptide is controversial. We used an in vitro transcription-translation system to study the insertion of hydrophobic sequences into microsomal membranes, and showed that the KL4 sequence integrates efficiently with a transmembrane orientation despite the presence of intermittent lysines throughout the sequ…