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The role of asparagine (N)-linked oligosaccharide
chains in intracellular folding of the human chorionic gonadotropin
(hCG)-
Volume 270,
Number 20,
Issue of May 19, pp. 11851-11859, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Subunit Facilitate Correct Disulfide Bond Pairing
subunit was determined by examining the kinetics of folding
in Chinese hamster ovary (CHO) cells transfected with wild-type or
mutant hCG- genes lacking one or both of the asparagine
glycosylation sites. The half-time for folding of p1 into p2,
the rate-determining step in folding, was 7 min for wild-type
but 33 min for lacking both N-linked glycans. The
p1 p
2 half-time was 7.5 min in CHO cells expressing
the subunit missing the Asn-linked glycan and 10 min
for the
subunit missing the Asn-linked glycan. The
inefficient folding of hCG-
lacking both N-linked glycans
correlated with the slow formation of the last three disulfide bonds
(i.e. disulfides 23-72, 93-100, and 26-110)
to form in the hCG--folding pathway. Unglycosylated hCG- was
slowly secreted from CHO cells, and subunit-folding intermediates
retained in cells for more than 5 h were degraded into a hCG- core
fragment-like protein. However, coexpression of the hCG-
gene
enhanced folding and formation of disulfide bonds 23-72,
93-100, and 26-110 of hCG- lacking N-linked
glycans. In addition, the molecular chaperones BiP, ERp72, and ERp94,
but not calnexin, were found in a complex with unglycosylated, unfolded
hCG- and may be involved in the folding of this form. These
data indicate that N-linked oligosaccharides assist hCG-
subunit folding by facilitating disulfide bond formation.
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