Primary structure differences of human surfactant-associated proteins isolated from normal and proteinosis lung
| Autor: | Ewald Hannappel, Klaus P. Schäfer, Tilman Voss, Kurt Prof Dr Klemm, Andrea Schäfer, Per F. Nielsen, Jörg Maaßen, Bernhard Landis, Michael Przybylski, Claudia S. Maier |
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| Rok vydání: | 1992 |
| Předmět: |
Pulmonary Surfactant-Associated Proteins
Protein Conformation Proteolipids Alveolar proteinosis Blotting Western Molecular Sequence Data Protein dimer Pulmonary Alveolar Proteinosis Thioester Mass Spectrometry chemistry.chemical_compound Pulmonary surfactant medicine Humans Amino Acid Sequence Molecular Biology Polyacrylamide gel electrophoresis Chromatography High Pressure Liquid Glycoproteins chemistry.chemical_classification Lung Pulmonary Surfactant-Associated Protein A Protein primary structure Pulmonary Surfactants Pathophysiology medicine.anatomical_structure Biochemistry chemistry Molecular Medicine |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1138:261-267 |
| ISSN: | 0925-4439 |
| Popis: | The primary structures of human pulmonary surfactant-associated proteins SP-A, SP-B and SP-C isolated from lung lavage of patients with alveolar proteinosis exhibit significant differences from lung surfactant proteins isolated from lungs of healthy individuals. In contrast to SP-A from normal lungs, proteinosis SP-A was shown by SDS gel electrophoresis to contain large amounts of unreducibly cross-linked beta chains. Specific primary structure modifications of SP-C and SP-B proteins were established by direct molecular weight and structural analysis, using [ 252 Cf]plasma desorption mass spectrometry (PD/MS) as the principal method. In comparison to normal lung surfactant SP-B, proteinosis SP.B showed a significantly increased molecular weight by approx. 500 Da for the unreduced protein dimer. SP-C proteins from normal lungs were identified to possess a bis-cysteinyl-5,6-(thioester)palmitoylated structure, and to contain a frayed N-terminus resulting in two sequences of 34 and 35 amino acid residues. In contrast, SP-C from proteinosis patients was modified by (i) partial or even complete removal of palmitate residues and (ii) additional N-terminal proteolytic degradation. These results indicate the presence of pathophysiological structure modifications, which are likely to occur in the alveolar space, and may lead to a reduced surfactant function. |
| Databáze: | OpenAIRE |
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