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J. Biol. Chem., Vol. 259, Issue 8, 5306-5309, Apr, 1984
YS Chao, TT Yamin, GM Thompson and PA Kroon
We determined the site of synthesis of apolipoprotein (apo) E and apo-A- I
in rabbit by measuring in vitro translational activity of their mRNAs from
the liver and from the intestine. Poly(A+) RNA isolated from liver and
intestinal epithelium of rabbits fed either a chow diet or a
cholesterol-rich diet was translated in vitro in the rabbit reticulocyte
lysate system using [35S] methionine as the labeled precursor. Newly
synthesized apolipoproteins were immunoprecipitated with specific antisera
and quantitated after electrophoresed on 10% polyacrylamide slab gels in
the presence of 0.2% sodium dodecyl sulfate. The levels of liver apo-E and
apo-A-I mRNAs from chow-fed rabbits are 0.41 and 0.002% of total
translatable mRNA, respectively. The level of liver apo-A-I mRNA in the
rabbit is approximately 500-fold lower than the reported level of apo-A-I
mRNA in rat and human livers. Rabbit intestinal apo-E and apo-A-I mRNAs
levels are 0.0036 and 0.67%, respectively. Our results indicate that in
rabbits apo-E is synthesized primarily in the liver and that apo-A-I is
synthesized primarily in the intestine. When rabbits are fed a
cholesterol-rich diet, liver and intestinal apo-E in mRNA levels and
intestinal apo-A-I mRNA levels are not changed. In contrast, the liver
apo-A-I mRNA level increases 5-fold in response to the cholesterol-rich
diet. However, because the intestinal liver apo-A-I mRNA level is so low,
the 5-fold induction only increases liver mRNA levels to 2.7% of the
corresponding intestinal apo-A-I mRNA level.
Tissue-specific expression of genes encoding apolipoprotein E and apolipoprotein A-I in rabbits
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