Hsp90 inhibition suppresses NF-κB transcriptional activation via Sirt-2 in human lung microvascular endothelial cells.

The ability of anti-heat shock protein 90 (Hsp90) drugs to attenuate NF-κB-mediated transcription is the major basis for their anti-inflammatory properties. While the molecular mechanisms underlying this effect are not clear, they appear to be distinct in human endothelial cells. We now show for the first time that type 2 sirtuin (Sirt-2) histone deacetylase binds human NF-κB target gene promoter and prevents the recruitment of NF-κB proteins and subsequent assembly of RNA polymerase II complex in human lung microvascular endothelial cells.

Addressing the process improvement science knowledge and skills of program directors and associate program directors.

Background: Process improvement (PI) science is relatively new to healthcare and has only recently been introduced to medical education. Most residency faculty lack training or experience in PI science activities. We assessed the impact of PI science education on the knowledge and attitudes of a group of residency and fellowship program directors and associate program directors using their respective Accreditation Council for Graduate Medical Education annual program evaluations (APEs) as an experiential object.