The volume-outcome relationship in lung cancer surgery: The impact of the social determinants of health care delivery.

Is Video-Assisted Thoracic Surgery Lobectomy Better? Quality of Life Considerations

Dartmouth Atlas of Vascular Health Care review: Impact of hospital volume, surgeon volume, and training on outcome

Preoperative Evaluation of Patients With Interstitial Lung Disease

Surgery for Early-Stage Non-Small Cell Lung Cancer: A Systematic Review of the Video-Assisted Thoracoscopic Surgery Versus Thoracotomy Approaches to Lobectomy

Low-volume coronary artery bypass surgery: Measuring and optimizing performance

Perioperative Blood Transfusion Is Associated With Worse Clinical Outcomes in Resected Lung Cancer

PACIFIC: Time for a surgical IIIA uprising

Should Coronary Artery Bypass Grafting Be Regionalized?

Statins and Cardiac Surgery

Cytoreduction and the Optimization Of Immune Checkpoint Inhibition with Radiation Therapy

Epidemic of Lung Cancer in Patients With HIV Infection

Stigma May Exacerbate Disproportionately Low Guideline-Concordant Treatment Rates for Patients With Advanced-Stage Lung Cancer in the United States

More Rigor Needed in Systematic Reviews on “Waterpipe” (Hookah, Narghile, Shisha) Smoking

Surgical Assessment and Intraoperative Management of Mediastinal Lymph Nodes in Non-Small Cell Lung Cancer

During apoptosis, Smac (second mitochondria-derived activator of caspases)/DIABLO, an IAP (inhibitor of apoptosis protein)-binding protein, is released from mitochondria and potentiates apoptosis by relieving IAP inhibition of caspases. We demonstrate that exposure of MCF-7 cells to the death-inducing ligand, TRAIL (tumor necrosis factor-related apoptosis-inducing ligand), results in rapid Smac release from mitochondria, which occurs before or in parallel with loss of cytochrome c. Smac release is inhibited by Bcl-2/Bcl-xL or by a pan-caspase inhibitor demonstrating that this event is caspase-dependent and modulated by Bcl-2 family members. Following release, Smac is rapidly degraded by the proteasome, an effect suppressed by co-treatment with a proteasome inhibitor. As the RING finger domain of XIAP possesses ubiquitin-protein ligase activity and XIAP binds tightly to mature Smac, an in vitro ubiquitination assay was performed which revealed that XIAP functions as a ubiquitin-protein ligase (E3) in the ubiquitination of Smac. Both the association of XIAP with Smac and the RING finger domain of XIAP are essential for ubiquitination, suggesting that the ubiquitin-protein ligase activity of XIAP may promote the rapid degradation of mitochondrial-released Smac. Thus, in addition to its well characterized role in inhibiting caspase activity, XIAP may also protect cells from inadvertent mitochondrial damage by targeting pro-apoptotic molecules for proteasomal degradation.