David Ford, Ph.D.
Professor and Director of the CCR

Biochemical mechanisms responsible for the pathophysiological sequelae of macro and microvascular disease, including sepsis-caused microvascular dysfunction and multi-organ failure, atherosclerosis, and ischemic heart disease.

Office: DRC 325
Voice: (314) 977-9264

Research Interests

We are interested in the biochemical mechanisms responsible for the pathophysiological sequelae of vascular disease and organ failure. A recent focus in our lab has been on mechanisms responsible for multi-organ failure during sepsis. Death caused by sepsis is increasing in the U.S. and globally. We are examining changes at the blood/blood vessel interface that is altered during sepsis, leading to multi-organ failure.


The Ford lab has discovered molecules derived from activated leukocytes, including chlorinated lipids and reactive aldehyde-containing compounds. These novel molecules are being investigated as mediators of dysfunction at the blood/blood vessel interface. In particular, these molecules have important roles in activating endothelial cells and altering leukocyte function. Current and future studies are being directed to discovering molecules related to the leukocyte-produced lipids originally revealed by our lab as well as their potential pathophysiological roles. While these studies are based on the activation mechanisms of neutrophils, we are also mining deeper into the human metabolome and lipidome involved in sepsis using untargeted lipidomics and metabolomics approaches.

Research Highlights
Septic patients with acute respiratory distress syndrome display higher plasma concentrations of free 2-chlorofatty acids
Meyer et al J Clin Invest Insight 2017

Compared with subjects who never developed ARDS, those who developed ARDS within the first 6 days of sepsis have higher circulating levels of free 2-ClPA and free 2-ClSA on the day of ICU admission.


Myeloperoxidase-derived 2-chlorofatty acids contribute to human sepsis mortality via acute respiratory distress syndrome. Meyer NJ, Reilly JP, Feng R, Christie JD, Hazen SL, Albert CJ, Franke JD, Hartman CL, McHowat J, Ford DA. J Clin Invest Insight 2(23):e96432, 2017 (PMID: 29212955).

2-Chlorofatty acids localize to the endothelial cell Weibel Palade bodies leading to their mobilization

Human coronary artery endothelial cells were treated with the click-chemistry analog of 2-chloropalmitic acid. The click analog was clicked to an azide-TAMRA (red) to visualize the localization of 2-chloropalmitic acid. This co-localized with P-selectin and von Willebrand Factor (VWF) indicating the selective localization of 2-chloropalmitic acid with the Weibel Palade bodies.

Hartman et al J Lipid Res 2018 fig 3bc

2-Chlorofatty acids induce Weibel-Palade body mobilization. Hartman CL, Duerr MA, Albert CJ, Neumann WL, McHowat J, Ford DA. J Lipid Res 59(1):113-122, 2018 (PMID: 29167411).

2-Chlorofatty acids make neutrophils go NETs

Neutrophil extracellular traps (green strands/nets in image under 2-ClPA, 2-chloropalmitic acid) are selectively produced compared to palmitic acid. PMA (phorbol myristate acetate) is shown as a positive control for NET formation.

Palladino et al J Lipid Res 2018 fig 2A

2-Chlorofatty acids: Lipid mediators of neutrophil extracellular trap formation. Palladino END, Katunga LA, Kolar GR, Ford DA. J Lipid Res 59(8):1424-1432, 2018 (PMID: 29739865)


Recent Publications

Department of Biochemistry and Molecular Biology