Rat liver protein synthesis after partial hepatectomy

1989 ◽  
Vol 17 (6) ◽  
pp. 1047-1047 ◽  
Author(s):  
V. R. PREEDY ◽  
L. PASKA ◽  
P. H. SUGDEN ◽  
P. S. SCHOFIELD ◽  
M. C. SUGDEN
1980 ◽  
Vol 186 (1) ◽  
pp. 35-45 ◽  
Author(s):  
A J Dickson ◽  
C I Pogson

Methods have been derived which permit the isolation of undergraded polyribosomes from isolated rat liver cells. Under the conditions used the polyribosome profile of hepatocytes immediately after isolation was essentially identical with that from intact liver. However, during incubation of cells in complex physiological media there was a progressive dissociation of polyribosomes. The addition of a variety of factors that produce reaggregation of polyribosomes in rat liver in vivo did not prevent dissociation during cell incubations. Although large polyribosomes were lost most rapidly, the albumin-synthesizing capacity of isolated cells was not selectively lost when compared with total protein synthesis. The significance of these results for the use of isolated hepatocytes in the study of liver protein synthesis is discussed.


1976 ◽  
Vol 158 (2) ◽  
pp. 485-488 ◽  
Author(s):  
H Pösö ◽  
J Jänne

Repeated injections of 1,3-diaminopropane into rats after partial hepatectomy caused a repression-type inhibiton of liver ornithine decarboxylase (EC 4.1.1.17) and totally prevented the marked increases in liver putrescine and spermidine concentrations that normally occur in response to partial hepatectomy. The inhibition of polyamine synthesis by diaminopropane was accompanied by a profound decrease (about 80%) in the synthesis of DNA in the regenerating rat liver without any changes in the synthesis of RNA and total liver protein.


1979 ◽  
Vol 178 (2) ◽  
pp. 373-379 ◽  
Author(s):  
M A McNurlan ◽  
A M Tomkins ◽  
P J Garlick

1. A method is described that allows for measurement of protein synthesis in liver and intestine in the rat. By injecting a massive amount of [14C]leucine (100 mumol/100 g body wt.) an attempt has been made to over come problems of precursor specific radioactivity and problems arising from the breakdown of labelled protein that are encountered when tracer amounts of amino acids are used. 2. Starvation for 2 days resulted in decline in the rate of total liver protein synthesis from 87%/day to 62%/day. 3. In jejunal mucosa the rate of protein synthesis was 136%/day. This declined to 105%/day after 2 days of starvation.


1978 ◽  
Vol 172 (1) ◽  
pp. 129-135 ◽  
Author(s):  
V M Pain ◽  
M J Clemens ◽  
P J Garlick

In rats fed on a protein-deficient diet, albumin synthesis as a percentage of total liver protein synthesis falls from the normal value of approx. 15% to about 8%. We have extracted total cytoplasmic RNA from individual rat livers and measured the concentration of active albumin mRNA by translation in a reticulocyte lysate system from which the endogenous mRNA had been removed [Pelham & Jackson (1976) Eur. J. Biochem. 67, 247-256]. In this messenger-dependent system it is possible to measure the synthesis of albumin as a proportion of the overall protein synthesis promoted by the addition of the hepatic RNA. The results show that the concentration of translatable albumin mRNA in samples of total cytoplasmic RNA from livers of protein-deficient rats is decreased markedly. These findings suggest that dietary protein supply affects selectively the synthesis and/or functional stability of albumin mRNA in rat liver.


1967 ◽  
Vol 242 (4) ◽  
pp. 700-704 ◽  
Author(s):  
C. Majumdar ◽  
Kinji Tsukada ◽  
Irving Lieberman

1973 ◽  
Vol 52 (2) ◽  
pp. 582-587 ◽  
Author(s):  
Matilde S. Ayuso-Parrilla ◽  
Roberto Parrilla

Life Sciences ◽  
1979 ◽  
Vol 25 (17) ◽  
pp. 1477-1487 ◽  
Author(s):  
Geoffrey H. Moyer ◽  
Garth E. Austin

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