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(Received for publication, October 11, 1996)
From the Harvard Medical School, Thyroglobulin (Tg), the major protein secreted by
thyroid epithelial cells and precursor of thyroid hormones, is a large
dimeric glycoprotein with multiple disulfide bonds. The folding and
assembly of this complex molecule begins in the endoplasmic reticulum
(ER) and is likely to involve a variety of reactions catalyzed by
molecular chaperones (Kuznetsov, G., Chen, L. B., and Nigam, S. K. (1994) J. Biol. Chem. 269, 22990-22995). By
coimmunoprecipitation in rat thyroid cells, we were able to demonstrate
that BiP, grp94, ERp72, and grp170, four proteins believed to function
as specific molecular chaperones, complex with Tg during its
maturation. The same complex of the four putative chaperones with Tg
was observed in cells treated with tunicamycin, indicating that these
four ER chaperones stably associate with Tg when it is
misfolded/misassembled due to inhibition of its glycosylation. BiP,
grp94, and ERp72 were also found to associate with Tg in cells in which
misfolding was induced by perturbing ER calcium stores. To determine if
the assembly of a complex between the four chaperones and Tg under conditions of misglycosylation was unique to the maturation of this
particular secretory protein or a more general phenomenon, adenovirus-transformed rat thyroid cells that do not synthesize Tg were
analyzed. In these transformed cells, the only protein these same four
chaperones were found to complex with was a protein of approximately
200 kDa. This protein was subsequently identified as
thrombospondin, which, like Tg, is a large oligomeric secreted glycoprotein with multiple disulfide bonds. We therefore propose that
these ER chaperones complex together with a variety of large oligomeric
secretory glycoproteins as they fold and assemble in the ER.
Volume 272, Number 5,
Issue of January 31, 1997
pp. 3057-3063
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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