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J. Biol. Chem., Vol. 268, Issue 3, 1757-1762, 01, 1993
E Szczesna-Skorupa and B Kemper
The mechanism of retention of cytochrome P450 in the endoplasmic reticulum
is unknown, and the membrane topology of the N-terminal region remains
controversial. To address these problems, a sequence of 29 amino acids
encoding an internal N-glycosylation site of rabbit cytochrome P450 2C2 was
attached to the N terminus of cytochrome P450 2C1. This protein is
glycosylated at a single site in a cell-free translation system containing
microsomal membranes, as indicated by gel mobility and sensitivity to
endoglycosidase H. When expressed in COS1 cells, an immunoreactive species
with the same gel mobility as the in vitro synthesized glycosylated product
was detected. Treatment with endoglycosidase H changed its mobility to that
of unglycosylated hybrid cytochrome P450 2C1. These results indicate that
in intact cells, as in the cell-free system, the N terminus of cytochrome
P450 is luminally oriented which is not consistent with a hairpin loop
conformation. Sensitivity of the glycosylated protein to endoglycosidase H
suggests that the protein does not reach the Golgi compartments. When
transfected cells were incubated at low temperatures to inhibit retrograde
transport from the intermediate pre-Golgi compartment into the endoplasmic
reticulum, localization of cytochrome P450 was not changed, as assayed by
subcellular fractionation and immunofluorescent staining. These
observations suggest that cytochrome P450 is restricted to the endoplasmic
reticulum membrane by a mechanism different from recycling through the
intermediate compartment, which is a pathway utilized by soluble
endoplasmic reticulum proteins.
An N-terminal glycosylation signal on cytochrome P450 is restricted to the endoplasmic reticulum in a luminal orientation
Department of Physiology and Biophysics, University of Illinois, Urbana 61801.
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