Student Leadership Development Initiative: Benefits of a Unique Medical Student Organization.

BACKGROUND: The Student Leadership Development Initiative was founded at the Medical College of Wisconsin to unite local physician leaders with Medical College of Wisconsin students to develop leadership skills and prepare for careers expanding beyond clinical practice. METHODS: An anonymous survey was distributed to 246 current and past Student Leadership Development Initiative participants, probing confidence in leadership skills, professional goals, and the perceived importance of leadership training. Feedback interviews were also conducted. RESULTS: Respondents reported improvement in areas such as compassion, leadership, and development of career goals. The perceived benefit for developing professional goals and compassion are positively related (P < 0.01) to the number of sessions attended. DISCUSSION: Survey results highlight the importance of leadership training in medical education and suggest an integration strategy for a successful leadership training platform.

Acquired Factor V Inhibitor After Antibiotic Therapy: A Clinical Case Report and Review of the Literature.

Acquired factor V inhibitor (aFVi) is an exceptionally rare hematologic condition that can range from incidental laboratory abnormalities to life-threatening hemorrhage. Bovine thrombin was formerly the most common cause of this condition; however, the decreased use of bovine thrombin in surgical procedures has led to a shift in the cause of aFVi toward antibiotic use and malignancies. Here we present a case of an 80-year-old Caucasian female on long-term warfarin therapy who presented with epistaxis and an elevated international normalized ratio, and a history of cephalosporin antibiotic use. We review the published literature beginning in 2016 to identify the evolving causes of aFVi. Additionally, we propose that stress-mediated immune regulation may contribute to antibody formation, preventing the interaction between factor V and the damaged phospholipid membranes. This case highlights the evolving causes of aFVi and should prompt physicians to consider this diagnosis in coagulopathies that do not correct with traditional therapies.

Disseminated M. bovis Infection and Vertebral Osteomyelitis following Immunotherapy for Bladder Cancer.

The use of BCG in immunotherapy for bladder cancer has been in practice for over 40 years. However, uncommon, serious complications can occur with the therapy. Here, we present a case of vertebral osteomyelitis secondary to dissemination of BCG following immunotherapy, an exceedingly rare presentation of an already rare complication.

Tumor Necrosis Factor-α Trimer Disassembly and Inactivation via Peptide-Small Molecule Synergy.

Aberrant signaling by tumor necrosis factor-α (TNFα) is associated with inflammatory diseases that can be treated with engineered proteins that inhibit binding of this cytokine to cell-surface receptors. Despite these clinical successes, there is considerable interest in the development of smaller antagonists of TNFα-receptor interactions. We describe a new 29-residue α/ß-peptide, a molecule that contains three ß-amino acid residues and three α-aminoisobutryic acid (Aib) residues, that displays potent inhibition of TNFα binding to TNFα receptor 1 (TNFR1) and rescues cells from TNFα-induced death. The complement of nonproteinogenic residues renders this α/ß-peptide highly resistant to proteolysis, relative to all-α analogues. The mechanism of inhibitory action of the new 29-mer involves disruption of the trimeric TNFα quaternary structure, which prevents productive binding to TNFα receptors. Unexpectedly, we discovered that peptide-induced trimer disruption can be promoted by structurally diverse small molecules, including a detergent commonly used during selection procedures. The discovery of this synergistic effect provides a new context for understanding previous reports on peptidic antagonists of TNFα-receptor interactions and suggests new avenues for future efforts to block signaling via proteins with an active form that is oligomeric, including other members of the TNFα family.