scholarly journals Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C): Structure and surface activity

2006 ◽  
Vol 1758 (4) ◽  
pp. 509-518 ◽  
Author(s):  
Dunja Lukovic ◽  
Inés Plasencia ◽  
Francisco J. Taberner ◽  
Jesús Salgado ◽  
Juan J. Calvete ◽  
...  
Keyword(s):  
Surface Activity ◽  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Surfactant Protein C ◽  
Pulmonary Surfactant Protein

scholarly journals Amyloid fibril formation by pulmonary surfactant protein C

FEBS Letters ◽  
1999 ◽  
Vol 464 (3) ◽  
pp. 138-142 ◽  
Author(s):  
Magnus Gustafsson ◽  
Johan Thyberg ◽  
Jan Näslund ◽  
Erik Eliasson ◽  
Jan Johansson
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Amyloid Fibril ◽  
Surfactant Protein ◽  
Fibril Formation ◽  
Surfactant Protein C ◽  
Amyloid Fibril Formation ◽  
Pulmonary Surfactant Protein

scholarly journals A method for S- and O-palmitoylation of peptides: synthesis of pulmonary surfactant protein-C models

1999 ◽  
Vol 343 (3) ◽  
pp. 557-562 ◽  
Author(s):  
Esmail YOUSEFI-SALAKDEH ◽  
Jan JOHANSSON ◽  
Roger STRÖMBERG
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Cd Spectroscopy ◽  
Reversed Phase ◽  
Prolonged Treatment ◽  
Surfactant Protein C ◽  
Palmitoyl Chloride ◽  
Α Helix ◽  
Pulmonary Surfactant Protein

A method for O- and S-palmitoylation of non-protected peptides has been developed. The peptides are treated with excess of palmitoyl chloride in 100% trifluoroacetic acid for 10 min at room temperature. The acidic conditions prevent acylation of amino groups, which is only significant after prolonged treatment (hours to days). The tripeptides Gly-Cys-Phe and Gly-Ser-Phe were converted into the respective S- and O-palmitoylated compounds, and the hydrophobic pulmonary surfactant protein-C model peptides, LRIPCCPVNLKRLLVVV [SP-C(1-17)] and FGIPSSPVLKRLLILLLLLLLILLLILGALLMGL [SP-C(Leu)] were converted into their respective S,S- and O,O-dipalmitoylated peptides. The reactions were virtually quantitative, and the palmitoylated peptides were isolated in about 75-80% yield after reversed-phase HPLC purification. CD spectroscopy showed that S,S-dipalmitoylation of SP-C(1-17) affects the peptide secondary structure (substantial increase in the α-helix content) in dodecylphosphocholine micelles.

The role of pulmonary surfactant protein C during the breathing cycle

1998 ◽  
Vol 327-329 ◽  
pp. 632-635 ◽  
Author(s):  
H.-J. Galla ◽  
N. Bourdos ◽  
A. von Nahmen ◽  
M. Amrein ◽  
M. Sieber
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Breathing Cycle ◽  
Surfactant Protein C ◽  
Pulmonary Surfactant Protein

Localization of Misprocessed Pulmonary Surfactant Protein C in Tubular Myelin Enriched Fractions By Cryo Immunogold Labeling

2000 ◽  
Vol 6 (S2) ◽  
pp. 868-869
Author(s):  
C.-L. Na ◽  
E. A. Evans ◽  
H. T. Akinbi ◽  
T. E. Weaver
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Intracellular Localization ◽  
Surfactant Protein ◽  
Biologically Active ◽  
Alveolar Type ◽  
Double Knockout ◽  
Surfactant Protein C ◽  
Associated Proteins ◽  
Pulmonary Surfactant Protein

Pulmonary surfactant is secreted by alveolar type II cells and reduces the surface tension at the air-liquid interface of alveoli. After pulmonary surfactant is secreted into the alveolar space, it transforms into tubular myelin, a highly ordered 3-dimensional lattice-like structure. Pulmonary surfactant protein C (SP-C), one of four pulmonary surfactant associated proteins, is synthesized as a proprotein which is processed to biologically active 35 amino acid mature peptide by proteolytic cleavage of N- and C-terminal peptides from the SP-C propeptide (Weaver, 1998). Processing of SP-C is linked to the expression of pulmonary surfactant protein B (SP-B): In SP-B deficient mice, SP-C is misprocessed and present in the bronchoalveolar lavage (BAL; Vorbroker et. al., 1995a). Although the intracellular localization of SP-C is well established (Vorbroker et. al., 1995b), there is no ultrastructure study available regarding the localization of misprocessed SP-C in the airway. In this study, we used transgenic mice expressing a truncated human SP-B propeptide (hSP-BΔC+/+) bred into the murine granulocyte macrophage colony stimulating factor (GMCSF) and SP-B double knockout background (hSP-BΔC+/+: GMCSF-/-: mSP-B-/-) as a model to localize the misprocessed SP-C by cryoimmunogold labeling.

scholarly journals Pulmonary Surfactant Protein C Reduces the Size of Liquid Ordered Domains in a Ternary Membrane Model System

2009 ◽  
Vol 96 (3) ◽  
pp. 608a-609a ◽  
Author(s):  
Florian Baumgart ◽  
Lu�s Loura ◽  
Manuel Prieto ◽  
Jes�s P�rez Gil
Keyword(s):  
Pulmonary Surfactant ◽  
Protein C ◽  
Surfactant Protein ◽  
Model System ◽  
Membrane Model ◽  
Surfactant Protein C ◽  
Liquid Ordered ◽  
Pulmonary Surfactant Protein
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