AJP - Lung Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Lung Cell Mol Physiol 261: L118-L125, 1991;
1040-0605/91 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow A corrigendum has been published
Right arrow A corrigendum has been published
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stults, J. T.
Right arrow Articles by Benson, B. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stults, J. T.
Right arrow Articles by Benson, B. J.

AJP - Lung Cellular and Molecular Physiology, Vol 261, Issue 2 118-L125, Copyright © 1991 by American Physiological Society

ARTICLES

Lung surfactant protein SP-C from human, bovine, and canine sources contains palmityl cysteine thioester linkages

J. T. Stults, P. R. Griffin, D. D. Lesikar, A. Naidu, B. Moffat and B. J. Benson
Department of Protein Chemistry, Genentech, South San Francisco 94080.

Lung surfactant is a complex mixture of lipids and proteins that coats the alveoli to reduce surface tension and prevent airspace collapse. One of the principal protein constituents, surfactant protein C (SP-C), has been characterized following isolation from human, canine, and bovine sources. In each species, this highly hydrophobic protein is composed of 33-35 amino acids, the differences being due to NH2-terminal heterogeneity. A COOH-terminal leucine is conserved throughout. The cysteines in each species were found by fast atom bombardment mass spectrometry to be present as thioesters of palmitic acid. Acylation of recombinant SP-C with palmityl coenzyme A, followed by characterization before and after release of the acyl group with 1,4-dithiothreitol, provided corroborating evidence for the native structure.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Lung Cell. Mol. Physiol.Home page
S. M. Pietschmann and U. Pison
cDNA cloning of ovine pulmonary SP-A, SP-B, and SP-C: isolation of two different sequences for SP-B
Am J Physiol Lung Cell Mol Physiol, April 1, 2000; 278(4): L765 - L778.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. F. Beers, C. A. Lomax, and S. J. Russo
Synthetic Processing of Surfactant Protein C by Alevolar Epithelial Cells. THE COOH TERMINUS OF proSP-C IS REQUIRED FOR POST-TRANSLATIONAL TARGETING AND PROTEOLYSIS
J. Biol. Chem., June 12, 1998; 273(24): 15287 - 15293.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Z. Wang, O. Gurel, J. E. Baatz, and R. H. Notter
Acylation of Pulmonary Surfactant Protein-C Is Required for Its Optimal Surface Active Interactions with Phospholipids
J. Biol. Chem., August 9, 1996; 271(32): 19104 - 19109.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. J. Conkright, J. P. Bridges, C.-L. Na, W. F. Voorhout, B. Trapnell, S. W. Glasser, and T. E. Weaver
Secretion of Surfactant Protein C, an Integral Membrane Protein, Requires the N-terminal Propeptide
J. Biol. Chem., April 27, 2001; 276(18): 14658 - 14664.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online