2008
DOI: 10.1016/j.jsbmb.2008.09.005
|View full text |Cite
|
Sign up to set email alerts
|

Protein disulfide isomerase is a multifunctional regulator of estrogenic status in target cells

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

3
39
0

Year Published

2009
2009
2018
2018

Publication Types

Select...
8
1

Relationship

2
7

Authors

Journals

citations
Cited by 30 publications
(42 citation statements)
references
References 54 publications
3
39
0
Order By: Relevance
“…PDI can function as a high-capacity intracellular 17b-estradiol (E 2 ) binding protein, increasing the concentration and accumulation of E 2 in cultured cells. Intracellular PDI-bound E 2 can be released from PDI upon a reduction in E 2 levels, and the released E 2 can increase estrogen receptormediated transcriptional activity and mitogenic activity in cultured cells (Fu et al, 2008). Moreover, the binding of E 2 by PDI also reduces the availability of this hormone.…”
Section: (A) (B)mentioning
confidence: 99%
See 1 more Smart Citation
“…PDI can function as a high-capacity intracellular 17b-estradiol (E 2 ) binding protein, increasing the concentration and accumulation of E 2 in cultured cells. Intracellular PDI-bound E 2 can be released from PDI upon a reduction in E 2 levels, and the released E 2 can increase estrogen receptormediated transcriptional activity and mitogenic activity in cultured cells (Fu et al, 2008). Moreover, the binding of E 2 by PDI also reduces the availability of this hormone.…”
Section: (A) (B)mentioning
confidence: 99%
“…Moreover, the binding of E 2 by PDI also reduces the availability of this hormone. PDI also modulates the estrogen receptor (ER), being an important regulator of the ERa/ERb ratio by altering ERa and ERb levels in opposite directions, a change which is expected to modify cellular responses to estrogens in different target tissues (Fu et al, 2008). For instance, while ERa mediates the proliferative effect of estrogens in breast cancer cells, ERb seems to be anti-proliferative, negatively regulating ERa transactivation (Zhao et al, 2007).…”
Section: (A) (B)mentioning
confidence: 99%
“…PDI is also a subunit of certain proteins, whereas PDILs have roles as components of peptide-loading complexes or in protein retention in the ER (Noiva 1999). PDI also functions in other cellular compartments or on the cell surface, and may function in cell-cell interactions (Noiva 1999;Kim et al 2009), transport of nitrous oxide (an intracellular signalling molecule) and estrogens (Sliskovic et al 2005;Fu et al 2008), activation of tissue factor (a major initiator of blood coagulation) (Manukyan et al 2008), and accumulation of misfolded proteins in neuro-degenerative diseases (Nakamura & Lipton 2009). It also has roles in apoptosis during ER stress caused by accumulation of misfolded proteins (Jeong et al 2008) and accelerating ERAD (ERassociated degradation) (Ushioda et al 2008).…”
Section: Introductionmentioning
confidence: 99%
“…Immunoblot and immunofluorescence analysis were carried out to further confirm the differential protein levels observed in total cellular proteins (annexin-2, cathepsin D, profilin, protein disulfide isomerase A1 and Histone deacetylase 1 (HDAC1)) across MDA-MB-231, MCF-7 and MCF-10A (Figure 6 D~H). These proteins have been reported to play important roles in cytoskeleton regulation, proteolysis, calcium regulation, protein disulfide bond rearrangement and chromatin assembly during tumorigenesis (Feldner and Brandt, 2002;Liaudet-Coopman et al, 2006;Sharma and Sharma, 2007;Fu et al, 2008a;Kawai et al, 2003). The results of the immunoblotting indicate that cathepsin D and protein disulfide isomerase (PDI) showed up-regulation in MCF-7 cells but down-regulation in MDA-MB-231 compared to the two protein expressions in MCF-10A.…”
Section: Validation Of Characterized Breast Cancer Markers Through Immentioning
confidence: 99%