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J. Biol. Chem., Vol. 269, Issue 37, 22990-22995, 09, 1994
G Kuznetsov, LB Chen and SK Nigam
We have previously demonstrated that several endoplasmic reticulum (ER)
proteins, including BiP, ERp72, grp94, and protein disulfide isomerase,
bind to a denatured thyroglobulin (Tg) affinity column and can be
specifically eluted by ATP (Nigam, S.K., Goldberg, A.L., Ho, S., Rohde,
M.F., Bush, K.T., and Sherman, M.Y. (1994) J. Biol. Chem. 269, 1744- 1749).
Using chemical cross-linking, we now demonstrate that BiP, ERp72, and grp94
associate with Tg in two types of cultured thyroid cells, FRTL-5 and PCC13.
Whereas BiP could be coimmunoprecipitated with anti-Tg antibodies in the
absence of cross-linking, only trace amounts of ERp72 and grp94 were
coimmunoprecipitated. Likewise, in both cell types, anti-BiP antibodies
were able to coimmunoprecipitate Tg in the absence of cross-linking, though
ERp72 and grp94 were only minimally present. Coprecipitation of BiP and Tg
was abolished when ATP and Mg2+ were added to cell lysates. In contrast,
after cross-linking, there was a large increase in the amount of ERp72 and
grp94 that coimmunoprecipitated with anti-Tg antibodies, although there was
only a slight increase in BiP. Similarly, in cross-linked lysates, grp94
and ERp72 were also coimmunoprecipitated with anti-BiP antibodies. An
apparently novel 200-kDa protein was also consistently immunoprecipitated
by anti-BiP antibodies in both cell types. In addition, anti-ERp72
antibodies coimmunoprecipitated Tg, BiP, and grp94 only after
cross-linking. Analysis of uncross-linked and cross-linked samples by
sucrose density gradient centrifugation confirmed that Tg, BiP, grp94, and
ERp72 are present together in high molecular weight complexes only after
treatment of cells with cross-linking reagent. These results suggest that
ERp72, as well as BiP and grp94, function as molecular chaperones in the
maturation of Tg, potentially as part of a macromolecular complex.
Several endoplasmic reticulum stress proteins, including ERp72, interact with thyroglobulin during its maturation
Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Boston, Massachusetts.
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