Title |
A Protein Disulfide Isomerase/Thioredoxin-1 Complex Is Physically Attached to Exofacial Membrane Tumor Necrosis Factor Receptors: Overexpression in Chronic Lymphocytic Leukemia Cells
|
---|---|
Published in |
Antioxidants & Redox Signaling, August 2012
|
DOI | 10.1089/ars.2012.4789 |
Pubmed ID | |
Authors |
Anita Söderberg, Akter Hossain, Anders Rosén |
Abstract |
The 3D structures and functions of cysteine-rich receptors such as tumor necrosis factor receptors (TNFRs) are redox-modulated by dithiol-disulfide exchange. TNFR superfamily members participate in growth regulation in B-cell chronic lymphocytic leukemia (CLL), and tissue stromal cells interact with leukemia cells, profoundly affecting their viability via release of redox-active components, including cysteine, thioredoxin-1 (Trx1), and Trx reductase. Trx1 was previously shown to enhance release of TNF, which acts as an autocrine/paracrine growth factor in CLL. The nature of the mechanism is not known, however. Here, we investigated whether Trx1 and protein disulfide isomerase (PDI), a chaperone and Trx-family member, may interact with TNFRs. |
X Demographics
Geographical breakdown
Country | Count | As % |
---|---|---|
United States | 1 | 100% |
Demographic breakdown
Type | Count | As % |
---|---|---|
Scientists | 1 | 100% |
Mendeley readers
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 19 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 6 | 32% |
Researcher | 3 | 16% |
Student > Doctoral Student | 2 | 11% |
Professor > Associate Professor | 2 | 11% |
Student > Master | 1 | 5% |
Other | 3 | 16% |
Unknown | 2 | 11% |
Readers by discipline | Count | As % |
---|---|---|
Biochemistry, Genetics and Molecular Biology | 5 | 26% |
Agricultural and Biological Sciences | 4 | 21% |
Medicine and Dentistry | 3 | 16% |
Social Sciences | 1 | 5% |
Immunology and Microbiology | 1 | 5% |
Other | 2 | 11% |
Unknown | 3 | 16% |