Journal of Applied Physiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Appl Physiol 48: 812-820, 1980;
8750-7587/80 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 King, R. J.
Right arrow Articles by Martin, H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by King, R. J.
Right arrow Articles by Martin, H.

Journal of Applied Physiology, Vol 48, Issue 5 812-820, Copyright © 1980 by American Physiological Society


ARTICLES

Intracellular metabolism of the apoproteins of pulmonary surfactant in rat lung

R. J. King and H. Martin

We studied the metabolic turnover of the major apoproteins of pulmonary surfactant from rat lung and compared it with similar studies on the metabolism of dipalmitoyl phosphatidylcholine (DPPC). At varying times after the injection of tritiated leucine or tritiated palmitate we isolated the alveolar cells and alveolar fluid and measured the incorporation of the radioactive leucine into the 35,000-dalton (apoprotein A) and 10,000-dalton (apoprotein B) apoproteins of surfactant and of the radioactive palmitate into DPPC. Maximum labeling of apoprotein A in type II cells occurred within 1 h after injection of the precursor and declined in the next 19 h. The labeling of intracellular DPPC followed the same time course. The labeling of apoprotein B in type II cells was low, and the change of its labeling with time was not consistent with its being secreted by these cells. Both proteins were labeled in alveolar fluid and in alveolar macrophages. The results indicate that apoprotein A is synthesized by type II cells and is probably secreted as part of the surfactant complex. Apoprotein B is not secreted by type II cells with the same time course as apoprotein A or the lipids of surfactant, but our results do not define its origin or physiological purpose.


This article has been cited by other articles:


Home page
Am. J. Respir. Cell Mol. Bio.Home page
K. Osanai, R. J. Mason, and D. R. Voelker
Trafficking of Newly Synthesized Surfactant Protein A in Isolated Rat Alveolar Type II Cells
Am. J. Respir. Cell Mol. Biol., December 1, 1998; 19(6): 929 - 935.
[Abstract] [Full Text]




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