F. Giannoni et al., COMPLEMENTATION OF APOLIPOPROTEIN-B MESSENGER-RNA EDITING BY HUMAN LIVER ACCOMPANIED BY SECRETION OF APOLIPOPROTEIN B48, The Journal of biological chemistry, 269(8), 1994, pp. 5932-5936
Mammalian small intestine secretes a truncated apolipoprotein B (apoB4
8) species as a result of tissue-specific post-transcriptional RNA edi
ting. The human liver, by contrast, contains only unedited apoB mRNA a
nd secretes only apoB100. We have recently isolated a cDNA clone from
rat small intestine which encodes an apoB mRNA editing protein, REPR (
Teng, B., Burant, C. F., and Davidson, N. O. (1993) Science 260, 1816-
1819). The current study demonstrates that homogenates of Xenopus oocy
tes expressing REPR confer editing ability upon S100 extracts prepared
from human liver when tested on a synthetic apoB RNA template in vitr
o. Transfection of REPR into HepG2 cells resulted in editing of endoge
nous apoB mRNA and the appearance of an apoB48-like protein in the med
ia. Extracts prepared hom these transfected cells edit mammalian apoB
RNA templates when incubated alone and with enhanced efficiency in the
presence of chicken intestinal S100 extracts. The results suggest tha
t human liver expresses factor(s) which are critical to apoB mRNA edit
ing and which allow functional complementation of REPR in vivo.