scholarly journals Alternative polyadenylation of apolipoprotein B RNA is a major cause of B-48 protein formation in rat hepatoma cell lines transfected with human apoB-100 minigenes.

1994 ◽  
Vol 35 (12) ◽  
pp. 2200-2211
Author(s):  
T Heinemann ◽  
S Metzger ◽  
E A Fisher ◽  
J L Breslow ◽  
L S Huang
In Vitro ◽  
1982 ◽  
Vol 18 (2) ◽  
pp. 157-164 ◽  
Author(s):  
Everard H. Hughes ◽  
Herman A. J. Schut ◽  
Snorri S. Thorgeirsson

Planta Medica ◽  
1989 ◽  
Vol 55 (06) ◽  
pp. 567-568 ◽  
Author(s):  
Y. Adjibadé ◽  
B. Kuballa ◽  
P. Cabalion ◽  
M. Jung ◽  
J. Beck ◽  
...  

1986 ◽  
Vol 6 (5) ◽  
pp. 1722-1728
Author(s):  
M A Lambert ◽  
L R Simard ◽  
P N Ray ◽  
R R McInnes

Using antibody and plaque hybridization screening, we isolated rat argininosuccinate lyase (AS lyase) cDNA clones from a liver cDNA library prepared in the phage expression vector lambda gt11. Five overlapping cDNAs covering 1.7 kilobases of the estimated 2.0-kilobase AS lyase mRNA were characterized and confirmed as AS lyase sequences by hybrid selection. We examined the differential expression of AS lyase in rat liver and four rat hepatoma cell lines (7800C1, H4, HTC, and MH1C1). These cells exhibited a 60-fold range of AS lyase enzyme activity, with a direct correlation between activity, amount of AS lyase immunoreactive protein, and quantity of specific AS lyase mRNA. These observations suggest that the differences in AS lyase expression between rat liver and the hepatoma cell lines result from variations in AS lyase transcriptional activity or alterations in nuclear processing of AS lyase RNA.


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