Function of Surfactant Proteins B and C

Weaver, Timothy E.; Conkright, Juliana Johnson

doi:10.1146/annurev.physiol.63.1.555

Cited by 347 publications

(243 citation statements)

References 131 publications

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“…The hydrophobic surfactant proteins B (SP-B) and C (SP-C) are key components and when disturbed or lacking lead to dysfunctional surfactant (7)(8)(9). SP-B is encoded by a single gene (SFTPB) and is translated and processed in alveolar type II cells to a mature monomeric protein of about 8 kDa which is secreted and active as a homodimer of 16 kDa in the alveolar space (10).…”

mentioning

confidence: 99%

Surfactant proteins in pediatric interstitial lung disease

et al. 2015

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mentioning

confidence: 99%

Surfactant proteins in pediatric interstitial lung disease

et al. 2015

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“…An unexpected role for SP-C in pulmonary homeostasis was provided by recent studies (8,9) demonstrating that a mutation in the sp-C gene was associated with idiopathic interstitial pneumonitis (IIP) 1 in humans. Pulmonary disease in these patients was inherited as an autosomal dominant trait.…”

mentioning

confidence: 99%

Pneumonitis and Emphysema in sp-C Gene Targeted Mice

Glasser¹,

Detmer²,

Ikegami³

et al. 2003

Journal of Biological Chemistry

202

161

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“…These positively charged segments likely provide important surfaces for interaction of the protein with lung surfactant phospholipids, especially phospholipids with anionic headgroups (2). The functional importance of anionic lipids is underlined by the observation that an anionic phospholipid, such as phosphatidylglycerol (PG), is a critical component of artificial lung surfactant (31).…”

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confidence: 99%

NMR Structures of the C-Terminal Segment of Surfactant Protein B in Detergent Micelles and Hexafluoro-2-propanol

et al. 2004

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Although the membrane-associated surfactant protein B (SP-B) is an essential component of lung surfactant, which is itself essential for life, the molecular basis for its activity is not understood. SP-B's biophysical functions can be partially mimicked by subfragments of the protein, including the C-terminus. We have used NMR to determine the structure of a C-terminal fragment of human SP-B that includes residues 63-78. Structure determination was performed both in the fluorinated alcohol hexafluoro-2-propanol (HFIP) and in sodium dodecyl sulfate (SDS) micelles. In both solvents, residues 68-78 take on an amphipathic helical structure, in agreement with predictions made by comparison to homologous saposin family proteins. In HFIP, the five N-terminal residues of the peptide are largely unstructured, while in SDS micelles, these residues take on a well-defined compact conformation. Differences in helical residue side chain positioning between the two solvents were also found, with better agreement between the structures for the hydrophobic face than the hydrophilic face. A paramagnetic probe was used to investigate the position of the peptide within the SDS micelles and indicated that the peptide is located at the water interface with the hydrophobic face of the helix oriented inward, the hydrophilic face of the helix oriented outward, and the N-terminal residues even farther from the micelle center than those on the hydrophilic face of the R-helix. Interactions of basic residues of SP-B with anionic lipid headgroups are known to have an impact on function, and these studies demonstrate structural ramifications of such interactions via the differences observed between the peptide structures determined in HFIP and SDS.

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Function of Surfactant Proteins B and C

Cited by 347 publications

References 131 publications

Surfactant proteins in pediatric interstitial lung disease

Surfactant proteins in pediatric interstitial lung disease

Pneumonitis and Emphysema in sp-C Gene Targeted Mice

NMR Structures of the C-Terminal Segment of Surfactant Protein B in Detergent Micelles and Hexafluoro-2-propanol

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