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


     

Am J Physiol Cell Physiol 256: C18-C27, 1989;
0363-6143/89 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Everson, W. V.
Right arrow Articles by Jefferson, L. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Everson, W. V.
Right arrow Articles by Jefferson, L. S.

AJP - Cell Physiology, Vol 256, Issue 1 C18-C27, Copyright © 1989 by American Physiological Society

ARTICLES

Effect of amino acid deprivation on initiation of protein synthesis in rat hepatocytes

W. V. Everson, K. E. Flaim, D. M. Susco, S. R. Kimball and L. S. Jefferson
Department of Physiology, College of Medicine, Pennsylvania State University, Hershey 17033.

Conditions were defined for maintaining optimal protein synthetic activity in suspensions of freshly isolated rat hepatocytes. Under these conditions, isolated hepatocytes exhibited rates of protein synthesis and levels of polysomal aggregation equivalent to those observed in vivo and in perfused liver. Deprivation of total amino acids or single, essential amino acids resulted in a rapid decrease in the rate of protein synthesis, which was readily reversed by readdition of the deficient amino acid(s). The decrease was accompanied by a disaggregation of polysomes and an inhibition of 43S initiation complex formation, which was indicative of a limitation in the rate of initiation of protein synthesis. Extracts prepared from perfused liver deprived of amino acids were inhibitory to initiation of protein synthesis in reticulocyte lysate. The inhibition in reticulocyte lysate was accompanied by an increase in phosphorylation of the alpha-subunit of eukaryotic initiation factor 2 (eIF-2), suggesting activation of an eIF-2 alpha kinase or inhibition of a phosphatase in amino acid-deprived hepatocytes. This suggestion was confirmed by prelabeling hepatocytes with 32Pi before amino acid deprivation. Incorporation of 32Pi into eIF-2 alpha was two- to threefold higher in lysine-deprived cells than in hepatocytes incubated in fully supplemented medium. Overall, the results indicated that an increase in eIF-2 alpha phosphorylation was responsible for the defect in initiation of protein synthesis caused by amino acid deprivation.


This article has been cited by other articles:


Home page
 J ANIM SCIHome page
K. C. Divakala, L. I. Chiba, R. B. Kamalakar, S. P. Rodning, E. G. Welles, K. A. Cummins, J. Swann, F. Cespedes, and R. L. Payne
Amino acid supplementation of hydrolyzed feather meal diets for finisher pigs
J Anim Sci, April 1, 2009; 87(4): 1270 - 1281.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
P. M. J. O'Connor, S. R. Kimball, A. Suryawan, J. A. Bush, H. V. Nguyen, L. S. Jefferson, and T. A. Davis
Regulation of neonatal liver protein synthesis by insulin and amino acids in pigs
Am J Physiol Endocrinol Metab, June 1, 2004; 286(6): E994 - E1003.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
P. M. J. O'Connor, S. R. Kimball, A. Suryawan, J. A. Bush, H. V. Nguyen, L. S. Jefferson, and T. A. Davis
Regulation of translation initiation by insulin and amino acids in skeletal muscle of neonatal pigs
Am J Physiol Endocrinol Metab, July 1, 2003; 285(1): E40 - E53.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
T. G. Anthony, A. K. Reiter, J. C. Anthony, S. R. Kimball, and L. S. Jefferson
Deficiency of dietary EAA preferentially inhibits mRNA translation of ribosomal proteins in liver of meal-fed rats
Am J Physiol Endocrinol Metab, September 1, 2001; 281(3): E430 - E439.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
T. A. Davis, H. V. Nguyen, A. Suryawan, J. A. Bush, L. S. Jefferson, and S. R. Kimball
Developmental changes in the feeding-induced stimulation of translation initiation in muscle of neonatal pigs
Am J Physiol Endocrinol Metab, December 1, 2000; 279(6): E1226 - E1234.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Endocrinol. Metab.Home page
C. H. Lang, D. Wu, R. A. Frost, L. S. Jefferson, T. C. Vary, and S. R. Kimball
Chronic alcohol feeding impairs hepatic translation initiation by modulating eIF2 and eIF4E
Am J Physiol Endocrinol Metab, November 1, 1999; 277(5): E805 - E814.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
H. L. Fox, P. T. Pham, S. R. Kimball, L. S. Jefferson, and C. J. Lynch
Amino acid effects on translational repressor 4E-BP1 are mediated primarily by L-leucine in isolated adipocytes
Am J Physiol Cell Physiol, November 1, 1998; 275(5): C1232 - C1238.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Cianflone, Z. Zhang, H. Vu, R. Kohen-Avramoglu, D. Kalant, and A. D. Sniderman
The Effect of Individual Amino Acids on ApoB100 and Lp(a) Secretion by HepG2 Cells
J. Biol. Chem., November 15, 1996; 271(46): 29136 - 29145.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. K. Tyzack, X. Wang, G. J. Belsham, and C. G. Proud
ABC50 Interacts with Eukaryotic Initiation Factor 2 and Associates with the Ribosome in an ATP-dependent Manner
J. Biol. Chem., October 27, 2000; 275(44): 34131 - 34139.
[Abstract] [Full Text] [PDF]


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