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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Biasiotto, Roberta Rizzuto, Rosario Aguiari, Paola Ciminale, Vincenzo Pinton, Paolo D'agostino, Donna M. |
| Description | Author Affiliation: Biasiotto R ( Department of Oncology and Surgical Sciences, University of Padova, I-35128 Padova, Italy.) |
| Abstract | Human T cell leukemia virus type 1 (HTLV-1) encodes p13, an 87-amino-acid protein that accumulates in the inner mitochondrial membrane. Recent studies performed using synthetic p13 and isolated mitochondria demonstrated that the protein triggers an inward potassium (K $^{+}$ ) current and inner membrane depolarization. The present study investigated the effects of p13 on mitochondrial inner membrane potential (Δ ψ ) in living cells. Using the potential-dependent probe tetramethyl rhodamine methyl ester (TMRM), we observed that p13 induced dose-dependent mitochondrial depolarization in HeLa cells. This effect was abolished upon mutation of 4 arginines in p13's α-helical domain that were previously shown to be essential for its activity in in vitro assays. As Δ ψ is known to control mitochondrial calcium (Ca $^{2+}$ ) uptake, we next analyzed the effect of p13 on Ca $^{2+}$ homeostasis. Experiments carried out in HeLa cells expressing p13 and organelle-targeted aequorins revealed that the protein specifically reduced mitochondrial Ca $^{2+}$ uptake. These observations suggest that p13 might control key processes regulated through Ca $^{2+}$ signaling such as activation and death of T cells, the major targets of HTLV-1 infection. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 6-7 |
| Volume Number | 1797 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2010-06-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Calcium Metabolism Human T-lymphotropic Virus 1 Membrane Potential, Mitochondrial Retroviridae Proteins Calcium Signaling HeLa Cells Genetics Pathogenicity Ion Transport Models, Biological Mutagenesis, Site-Directed Mutant Proteins Chemistry Protein Structure, Tertiary Recombinant Fusion Proteins Transfection Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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