Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1997-3-13
pubmed:abstractText
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/KAR2 protein, yeast, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Thyroglobulin, http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin, http://linkedlifedata.com/resource/pubmed/chemical/endoplasmic reticulum glycoprotein..., http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated protein 170, http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated proteins
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3057-63
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9006956-Animals, pubmed-meshheading:9006956-Blotting, Western, pubmed-meshheading:9006956-Cell Line, pubmed-meshheading:9006956-Centrifugation, Density Gradient, pubmed-meshheading:9006956-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:9006956-Endoplasmic Reticulum, pubmed-meshheading:9006956-Fungal Proteins, pubmed-meshheading:9006956-Glycoproteins, pubmed-meshheading:9006956-Glycosylation, pubmed-meshheading:9006956-HSP70 Heat-Shock Proteins, pubmed-meshheading:9006956-Membrane Glycoproteins, pubmed-meshheading:9006956-Membrane Proteins, pubmed-meshheading:9006956-Molecular Chaperones, pubmed-meshheading:9006956-Protein Folding, pubmed-meshheading:9006956-Rats, pubmed-meshheading:9006956-Thyroglobulin, pubmed-meshheading:9006956-Thyroid Gland, pubmed-meshheading:9006956-Tunicamycin
pubmed:year
1997
pubmed:articleTitle
Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum.
pubmed:affiliation
Harvard Medical School, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't