About

Daniel H. Foster is an Associate Professor and Chair of the Liberal Arts Department at the Peabody Conservatory of the Johns Hopkins University. He is a scholar with a particular interest in the intersection of music, literature, and drama. Foster is the author of Wagner’s Ring Cycle and the Greeks, published by Cambridge in 2010, and is currently working on a project titled From Bards to Blackface, or How the Minstrel Changed His Tune. His papers and articles have been published in various journals and outlets, including the Journal of American Drama and Theatre, Smithsonian Magazine, and the Huffington Post. He has previously served as a senior lecturer at the University of East Anglia and an associate professor at Duke University. At UEA, he was also the director of the media center, where he led the development of digital humanities projects and worked to incorporate technology into the classroom. Foster has produced and/or directed performances of Samuel Beckett’s All That Fall and Shakespeare’s As You Like It, among others. He received his Ph.D. from the University of Chicago’s Comparative Literature Department, earning honors for his dissertation on Richard Wagner’s use of classical Greek drama and poetry as models for his operatic treatment of German myth and national identity. He was awarded a Mellon Postdoctoral Fellowship by the University of Pennsylvania Humanities Forum and taught in Penn’s Music Department.

Research topics

• Chemistry
• Biology
• Cell biology
• Internal medicine
• Biochemistry

Selected publications

• RAB5C Increases Endothelial Release of VWF by Regulating Vesicle Trafficking

  Arteriosclerosis Thrombosis and Vascular Biology · 2026-01-15

  articleOpen access

  BACKGROUND: Abnormal levels of VWF (von Willebrand Factor) are a risk factor for venous thromboembolism (VTE) and bleeding. Genome-wide association studies for VWF have identified novel candidate genes that may regulate VWF levels in humans, including RAB5C (RAS [rat sarcoma]-associated protein RAB5C). We hypothesized that RAB5C regulates VWF release from endothelial cells. METHODS: We studied the effect of RAB5C on vesicle trafficking in human endothelial cells. We performed CRISPR (clustered regularly interspaced short palindromic repeats) interference targeting 2 genetic variants linked to altered VWF levels and evaluated RAB5C expression by reverse transcription–quantitative polymerase chain reaction. We silenced RAB5C or overexpressed RAB5C wild-type, constitutive active or dominant negative; and then, we measured VWF exocytosis from human umbilical vein endothelial cells to the media by ELISA. We performed proximity labeling and mass spectrometry to identify intracellular signaling pathways mediating the effects of RAB5C on VWF exocytosis. RESULTS: We found that 2 genetic variants (rs9915255 and rs9912088 identified by genome-wide association studies for VWF levels) regulate RAB5C expression in stem cell–derived endothelial cells. We next silenced or overexpressed RAB5C in endothelial cells to assess its effect on VWF release. RAB5C silencing decreased VWF release after histamine stimulation, whereas overexpression of RAB5C or constitutively active RAB5C increased endothelial VWF release. To explore the intracellular signaling pathway mediating the effects of RAB5C on VWF exocytosis, we performed proximity labeling and mass spectrometry. We identified 147 proteins proximal to RAB5C, many of which are involved in vesicle trafficking. From this screen, we identified SNAP29 (synaptosome-associated protein 29), a SNARE (soluble NSF [N-ethylmaleimide-sensitive factor] attachment receptor)-associated protein that plays a crucial role in vesicle fusion, as a key RAB5C interactor regulating VWF exocytosis. CONCLUSIONS: Taken together, our data demonstrate that RAB5C regulates VWF release in part through SNAP29 control of vesicle trafficking in endothelial cells. These findings validate genetic epidemiology data linking RAB5C to VWF levels in humans and provide new insights into the molecular mechanisms regulating VWF exocytosis.

  PublisherOA PDFDOI

• Characterizing molecular and behavioral changes arising from ROMK potassium channel deficiency in the cerebellum

  Frontiers in Behavioral Neuroscience · 2026-01-26

  articleOpen access

  The cerebellum is critically involved in both motor coordination and affective regulation, and growing evidence suggests that cerebellar dysfunction contributes to neuropsychiatric disorders. While much attention has focused on synaptic signaling and calcium homeostasis, the role of potassium channels in cerebellar function remains relatively understudied. Here, we investigated the role of the potassium channel ROMK (renal outer medulla K + channel) in cerebellar signaling and behavior using cre/loxP gene knockout in Pcp2cre-expressing cells. Surprisingly, ROMK expression was detected in a distinct cell population within the cerebellar granule layer, rather than in Purkinje cells, yet this expression was effectively targeted by Pcp2cre-mediated recombination. Mutant mice showed normal Purkinje cell density and soma size, but increased dendrite diameter. At the molecular level, we observed downregulation of cerebellar subtype-specific genes and potassium channel subunits, along with changes in markers of translational signaling. Increased presence of GFAP-positive cells further suggested underlying neuronal stress in the ROMK-deficient cerebellum. Behaviorally, ROMK-deficient mice exhibited clear impairments in motor coordination and heightened anxiety-like behavior in the elevated plus maze (EPM). Our findings link ROMK loss to molecular and cellular remodeling in the cerebellum and support the idea that ROMK contributes to neural circuits that regulate complex behaviors, providing a framework for further studies in this direction.

  PublisherOA PDFDOI

• Abstract 5740 Defining the impact of pathological mutations of the O-GlcNAc Transferase (OGT) in the brain

  Journal of Biological Chemistry · 2026-05-01

  articleOpen access
  PublisherDOI

• Inhibition of Cardiac p38 Highlights the Role of the Phosphoproteome in Heart Failure Progression

  ACS Omega · 2025-08-06 · 1 citations

  articleOpen accessSenior authorCorresponding

  Heart failure (HF) is a complex condition. Among altered signal transduction pathways associated with HF pathogenesis, the stress-activated p38 mitogen-activated protein kinase (Mapk) pathway has attracted attention for its role in HF progression and cardiac hypertrophy. However, the mechanisms by which p38-Mapk influences HF remain unclear. Addressing knowledge gaps may provide insight into why p38 inhibition has yielded inconsistent outcomes in clinical trials. Here, we investigate the effects of p38-Mapk inhibition via SB203580 on cardiac remodeling in a guinea pig model of HF and sudden cardiac death. Using an HF model with ascending aortic constriction and daily isoproterenol (ACi) administration, we assessed three groups: sham-operated controls, untreated ACi, and ACi treated with SB203580 (ACiSB). Cardiac function was evaluated by M-mode echocardiography. Proteome and phosphoproteome profiles were analyzed using multiplexed Tandem Mass Tag labeling and LC–MS/MS. Our findings demonstrate that SB203580 treatment protects against cardiac dysfunction in HF. Proteomic data indicate that SB203580 exerts broad protection of the cardiac phosphoproteome, inhibiting maladaptive p38-dependent phosphorylation, extending to Pka and Ampk networks, ultimately protecting the phosphorylation status of critical myofibrillar and Ca2+-handling proteins. Though SB203580 had a limited impact on widespread protein changes in HF, its biosignature revealed preserved mitochondrial energetics and reduced oxidative and inflammatory stress.

  PublisherOA PDFDOI

• Tuberculous meningitis alters the proteomic landscape of brain-derived extracellular vesicles

  bioRxiv (Cold Spring Harbor Laboratory) · 2025-12-08

  articleOpen access

  Tuberculous meningitis (TB meningitis), the deadliest form of Mycobacterium tuberculosis infection, leads to mortality and severe neurological disability despite standard therapy. Brain injury and microglial activation are major determinants of outcome, yet the mechanisms linking infection, inflammation and neuronal injury remain poorly understood. Extracellular vesicles (EVs), key mediators of cell-to-cell communication, have been investigated in pulmonary TB but their role in TB meningitis remains unexplored. We used our young rabbit model of TB meningitis to isolate pure, intact EVs from brain tissue (i.e., brain-derived EVs) from infected and uninfected rabbits and used nanoflow cytometry, transmission electron microscopy and protein quantification to characterize the EVs. Comparative proteomic profiling was performed by liquid chromatography-tandem mass spectrometry (LC-MS/MS), followed by in silico pathway, cell-type and protein-protein interaction analyses using DAVID, Enrichr, and STRING databases. We found that EV isolation from fresh and frozen tissue was equivalent and demonstrated that M. tuberculosis infection activated EV biogenesis. Despite preserved vesicle morphology, EVs from infected brain showed a significant proteomic shift characterized by enrichment of TB host defense, microglial and immune activation, metabolic excitotoxicity, and neuronal injury. These proteome dysregulations suggest that infection reprograms brain EV cargo toward proinflammatory and metabolic stress responses while depleting neuronal and mitochondrial components. Collectively, these data demonstrate that M. tuberculosis infection alters the cargo and abundance of brain-derived EV, highlighting their potential as biomarkers and mediators of host-pathogen interactions in TB meningitis.

  PublisherDOI

• P-033 Morphologic features associated with ischemic stroke in a matched case-control study of carotid webs

  2025-07-01

  article
  PublisherDOI

• Proteomic Insights into Cardiometabolic Remodeling in SARS-CoV-2-Infected Hamsters

  Journal of Molecular and Cellular Cardiology Plus · 2025-06-01

  articleOpen access
  PublisherDOI

• Pseudo-acetylation of ACTC1 K326 and K328 promotes dysinhibition of reconstituted human cardiac thin filaments

  Journal of Molecular and Cellular Cardiology · 2025-12-22

  articleOpen access
  PublisherOA PDFDOI

• Loss of O-GlcNAcylation in cardiac myocytes triggers the integrated stress response, contributing to heart failure

  Journal of Biological Chemistry · 2025-10-15 · 1 citations

  articleOpen access

  Heart failure (HF) is a significant global health problem, affecting an estimated 64 million people worldwide. At the core of HF is the progressive dysfunction and irreversible loss of cardiac myocytes. O-GlcNAc transferase (OGT) is a conserved enzyme that catalyzes the addition of N-acetyl-glucosamine (GlcNAc) to serine or threonine residues of intracellular proteins. This dynamic protein modification, termed O-GlcNAcylation, has been implicated in nutrient sensing, metabolic regulation and stress adaptation. The integrated stress response (ISR) is a pathway that enables cells to rapidly respond to acute environmental changes and cell damage. During ISR, the translation factor eIF2α is phosphorylated, shutting down general translation but favoring the rapid production of stress-adaptive proteins. However, prolonged activation of the ISR can be detrimental to cells. In this study, we found that inhibiting OGT activates the GCN2/eIF2α/Atf4 signaling axis of the ISR. Activation of this pathway could be blocked by ISRIB, a small molecule that opposes the activity of phosphorylated eIF2α. Mice with inducible deletion of OGT in adult cardiomyocytes developed HF, and treatment with ISRIB significantly delayed the progression to HF. Our study reveals the regulatory impact of O-GlcNAcylation on the ISR and highlights a new potential strategy for alleviating HF.

  PublisherDOI

• Retinoic acid signaling and metabolism in heart failure

  American Journal of Physiology-Heart and Circulatory Physiology · 2025-02-12 · 5 citations

  reviewOpen accessSenior author

  trans retinoic acid (ATRA), was elucidated in embryonic cardiac development, the role of the vitamin A metabolites, or retinoids, in adult heart physiology and heart and vascular disease, remains poorly understood. Studies have shown that low serum levels of retinoic acid correlate with higher all-cause and cardiovascular mortality, though the relationship between circulating retinol and ATRA levels, cardiac tissue ATRA levels, and intracellular cardiac ATRA signaling in the context of heart and vascular disease has only begun to be addressed. We have recently shown that patients with idiopathic dilated cardiomyopathy show a nearly 40% decline of in situ cardiac ATRA levels, despite adequate local stores of retinol. Moreover, we and others have shown that the administration of ATRA forestalls the development of heart failure (HF) in rodent models. In this review, we summarize key facets of retinoid metabolism and signaling and discuss mechanisms by which impaired ATRA signaling contributes to several HF hallmarks including hypertrophy, contractile dysfunction, poor calcium handling, redox imbalance, and fibrosis. We highlight unresolved issues in cardiac ATRA metabolism whose pursuit will help refine therapeutic strategies aimed at restoring ATRA homeostasis.

  PublisherDOI

Recent grants

• Targeting Metabo-Redox Network Vulnerability in Heart Failure and Sudden Death

  NIH · $2.1M · 2018–2023

• NIH Grant R21HL108052

  NIH · $457k · 2014

Frequent coauthors

• Jennifer E. Van Eyk

  Cedars-Sinai Smidt Heart Institute

  120 shared

• Anne M. Murphy

  University Hospitals of Leicester NHS Trust

  96 shared

• Brian O’Rourke

  Johns Hopkins Medicine

  90 shared

• Nazareno Paolocci

  Johns Hopkins Medicine

  49 shared

• Xiaoxu Shen

  Dongzhimen Hospital Affiliated to Beijing University of Chinese Medicine

  40 shared

• Kyriakos N. Papanicolaou

  Johns Hopkins Medicine

  40 shared

• Wei Dong Gao

  Johns Hopkins University

  40 shared

• Christopher I. Murray

  Cedars-Sinai Smidt Heart Institute

  38 shared

Education

• postdoctoral fellow, Medicine, Division of Cardiology

  Johns Hopkins School of Medicine

  2008

• postdoctoral fellow

  Boston Biomedical Research Institute

  2003

• postdoctoral fellow, Department of Physiology & Biophysics

  Boston University School of Medicine

  2003

• Ph.D., Biochemistry

  Queen's University

  2001

Awards & honors

• Mellon Postdoctoral Fellowship by the University of Pennsylv…