LAUSR

potentiation appeared to be cytokine independent (data not shown). Endothelial amyloids are heat stable, protease resistant, and RNase and DNase insensitive (1). They exhibit certain features of prion disease (10); for example, they are self-replicating and transmissible among cells (1). Here, we provide evidence that nosocomial pneumonia induces lung endothelial production of t and Ab oligomeric species that impair neurological information processing, supporting the hypothesis that these amyloids contribute to insidious end-organ dysfunction and suggesting the need for a larger cohort trial addressing this issue. In our studies, injurious amyloids were detected in the cerebrospinal fluid of infected, but not in uninfected, patients. However, our current sample size is small, and we have not determined whether other bacteria, viruses, fungi, or inflammatory conditions, such as the systemic inflammatory response syndrome, also elicit this endotheliopathy. Our studies focus on the acute consequences of infection-induced amyloids; it remains unknown as to whether the mechanisms tested here represent a cause of progressive and persistent memory loss in ICU patients. Indeed, in studies moving forward, it will be essential to determine the infection-induced t and Ab oligomer fate within the lung, blood, and other peripheral organs, including the brain. It will also be essential to determine whether infection-induced amyloid production and biodistribution contributes to cardiovascular disease, stroke, renal dysfunction, and pulmonary dysfunction in the aftermath of critical illness. n