Malposition of a Femoral Tunneled Dialysis Catheter through a Patent Foramen Ovale.

Patent foramen ovale (PFO) is a common congenital abnormality of high prevalence in adults. Its clinical significance is magnified in a right-to-left shunt, where paradoxical embolism can have catastrophic outcomes involving the brain, heart, mesenteric circulation, or extremities. Right-to-left shunting through a PFO is caused by increased right atrial pressure, as seen in the setting of pulmonary artery hypertension or pulmonary embolism. This case highlights the relevance of central venous catheter placement in the setting of a PFO. While the patient did not experience clinical sequelae from line placement, she was at high risk for paradoxical embolus. Recognizing the possibility of a PFO during central venous catheter placement, especially in the setting of increased right pressures, should be a consideration of all interventional radiologists.

Phosphoproteomic profiling of human myocardial tissues distinguishes ischemic from non-ischemic end stage heart failure.

The molecular differences between ischemic (IF) and non-ischemic (NIF) heart failure are poorly defined. A better understanding of the molecular differences between these two heart failure etiologies may lead to the development of more effective heart failure therapeutics. In this study extensive proteomic and phosphoproteomic profiles of myocardial tissue from patients diagnosed with IF or NIF were assembled and compared. Proteins extracted from left ventricular sections were proteolyzed and phosphopeptides were enriched using titanium dioxide resin. Gel- and label-free nanoscale capillary liquid chromatography coupled to high resolution accuracy mass tandem mass spectrometry allowed for the quantification of 4,436 peptides (corresponding to 450 proteins) and 823 phosphopeptides (corresponding to 400 proteins) from the unenriched and phospho-enriched fractions, respectively. Protein abundance did not distinguish NIF from IF. In contrast, 37 peptides (corresponding to 26 proteins) exhibited a ≥ 2-fold alteration in phosphorylation state (p<0.05) when comparing IF and NIF. The degree of protein phosphorylation at these 37 sites was specifically dependent upon the heart failure etiology examined. Proteins exhibiting phosphorylation alterations were grouped into functional categories: transcriptional activation/RNA processing; cytoskeleton structure/function; molecular chaperones; cell adhesion/signaling; apoptosis; and energetic/metabolism. Phosphoproteomic analysis demonstrated profound post-translational differences in proteins that are involved in multiple cellular processes between different heart failure phenotypes. Understanding the roles these phosphorylation alterations play in the development of NIF and IF has the potential to generate etiology-specific heart failure therapeutics, which could be more effective than current therapeutics in addressing the growing concern of heart failure.