| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| We have previously demonstrated that several endoplasmic reticulum ( ER ) proteins , including BiP , ERp 72 , grp 94 , and protein disulfide isomerase , bind to a denatured thyroglobulin ( Tg ) affinity column and can be specifically eluted by ATP ( Nigam , S . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| Microsomal triglyceride ( TG ) transfer protein ( MTP ) is an endoplasmic reticulum lumenal protein consisting of a 97 kDa subunit and protein disulfide isomerase . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| The presence of protein disulfide isomerase in colloid globules and in the secretory product of cultured thyrocytes suggests its involvement in the extracellular multimerization of human TG . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| In vitro , the combined action of ROS and PDI , in the presence of free glutathione ( reduced / oxidized ) , increased the solubility of this misassembled Tg and partially restored the ability of Tg to synthesize hormones . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| Here , the protein disulfide isomerase ( PDI ) and / or peroxidase induced oligomerization of unfolded thyroglobulins , which were prepared by treating bovine Tg with heat , urea or thiol / urea , was investigated using SDS PAGE analyses . ^^^ Meanwhile , PDI catalyzed oligomerization , time and pH dependent , was the most remarkable with unfolded / reduced Tg , which was prepared from a treatment with urea / DTT , while the thermally unfolded Tg was less sensitive . ^^^ However , PDI showed no remarkable effect on the peroxidase mediated oligomerization of either the unfolded or unfolded / reduced Tg . ^^^ Additionally , the reductive deoligomerization of oligomeric Tg was exerted by PDI in an excessively reducing state . ^^^ Based on these results , it is proposed that PDI catalyzes the oligomerization of Tg through the disulfide linkage and its deoligomerization in the molecular fate , and this process may require a specific molecular form of Tg , optimally unfolded / reduced , in a proper redox state . . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| To establish the formation of Tg multimers , the partially unfolded / reduced Tg or deoxycholate treated / reduced Tg was subjected to protein disulfide isomerase ( PDI ) mediated multimerization . ^^^ Oxidized glutathione / PDI mediated formation of multimeric Tg forms , requiring at least an equivalent molar ratio of PDI / Tg monomer , decreased with increasing concentration of reduced glutathione ( GSH ) , suggesting the oxidizing role of PDI . ^^^ Additional support was obtained when PDI alone , at a PDI / Tg molar ratio of 0 . 3 , expressed a rapid multimerization . ^^^ Independently , the exposure of partially unfolded Tg to GSH resulted in Tg multimerization , enhanced by PDI , according to thiol disulfide exchange . ^^^ Present results suggest that the oxidase as well as isomerase function of PDI may be involved in the multimerization of partially unfolded Tg or deoxycholate treated Tg . . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| We investigated the secretion and cell surface expression of PDI and other chaperones in the FRTL 5 thyroid cell line , and then studied the characteristics of the interaction between TG and PDI . ^^^ We observed on living cells or membrane preparations that PDI specifically binds TG in acidic conditions , and that only BD is involved in binding . ^^^ Surface plasmon resonance analysis of TG / PDI interactions indicated : 1 ) that PDI bound TG but only in acidic conditions , and that it preferentially recognized immature molecules , and 2 ) BD is involved in binding even if cysteine rich modules are deleted . ^^^ The notion that PDI acts as an `` escort ' ' for immature TG in acidic post endoplasmic reticulum compartments is discussed . . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| Here , we investigated the role of two molecular chaperones , protein disulfide isomerase ( PDI ) and immunoglobulin heavy chain binding protein ( BiP ) , present in the follicular lumen , on the multimerization process due to oxidation using both native Tg and its N terminal domain ( NTD ) . ^^^ In vitro , PDI decreased multimerization of Tg and even suppressed the formation of NTD multimers . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| In an attempt to determine the depolymerization process , various types of Tg multimers , which were generated from deoxycholate treated / reduced Tg , partially unfolded Tg or partially unfolded / reduced Tg , were subjected to various GSH ( reduced glutathione ) reducing systems using protein disulfide isomerase ( PDI ) , glutathione reductase ( GR ) , glutaredoxin or thioredoxin reductase . ^^^ The Tg multimers generated from deoxycholate treated / reduced Tg were depolymerized readily by the PDI / GSH system , which is consistent with the reductase activity of PDI . ^^^ The PDI / GSH induced depolymerization of the Tg multimers , which were generated from either partially unfolded Tg or partially unfolded / reduced Tg , required the simultaneous inclusion of glutathione reductase , which is capable of reducing glutathionylated mixed disulfide ( PSSG ) . ^^^ Overall , under the net GSH condition , the depolymerization of Tg multimers might be mediated by PDI , which is assisted by other reductive enzymes , and the mechanism for depolymerizing the Tg multimers differs according to the type of Tg multimer containing different degrees and types of disulfide linkages . . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| Inhibition of ER glucosidase activity blocked formation of a subgroup of Tg adducts containing ERp 57 while causing increased Tg adduct formation with protein disulfide isomerase ( PDI ) , delayed adduct resolution , perturbed oxidative folding of Tg monomers , impaired Tg dimerization , increased Tg association with BiP / GRP78 and GRP 94 , activation of the unfolded protein response , increased ER associated degradation of a subpopulation of Tg , partial Tg escape from ER quality control with increased secretion of free monomers , and decreased overall Tg secretion . ^^^ These data point towards mixed disulfides with the ERp 57 oxidoreductase in conjunction with calreticulin / calnexin chaperones acting as normal early Tg folding intermediates that can be `` substituted ' ' by PDI adducts only at the expense of lower folding efficiency with resultant ER stress . . ^^^ |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
|
| Interacting proteins: P01266 and P07237 |
Pubmed |
SVM Score :0.0 |
| NA |
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