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Biology subjects

Whitwell, H.

Publications and source records attributed to Whitwell, H..

3 recordsLinked to original sources

Organ on chip model of respiratory vascular interactions under COPD relevant oxidative stress

Oxidative stress-induced airway injury contributes to chronic obstructive pulmonary disease (COPD). Cardiovascular complications increase COPD morbidity and mortality, but mechanistic links between airway injury and vascular dysfunction remain unclear, largely due to limitations of in vitro models that fail to replicate the multicellular lung environment. We developed REVAS, a modular organ-on-chip platform to study human respiratory-vascular cell-cell interactions at baseline and under oxidative stress conditions. REVAS consists of two respiratory chips hosting airway epithelium and microvascular endothelium, and a vascular chip hosting pulmonary artery endothelial cells co-cultured with vascular support cells, including smooth muscle cells, pericytes and fibroblasts. We studied effects of vascular support and respiratory cells on vascular endothelial phenotype at baseline and under H2O2-induced epithelial oxidative stress using functional assays, proteomic and transcriptomic analyses. Multicellular environment enhanced vascular endothelial barrier function and promoted respiratory and vascular cell differentiation at baseline. Mural cells altered endothelial cell-matrix interactions, metabolism and cytoskeletal remodelling, while respiratory cells promoted endothelial aerobic respiration and quiescent phenotype. Epithelial oxidative stress triggered inflammatory gene expression across all respiratory and vascular cells alongside apoptotic, reparative and pro-angiogenic signalling in endothelial and mural cells, accompanied by increased release of COPD-relevant cytokines and chemokines, including IL-6, TNF-/{beta}, IL-8, CCL5, CXCL9, PDGF, TGF-{beta}. Comparative analyses with COPD endothelial datasets confirmed that REVAS recapitulates key features of disease-associated endothelial dysfunction. These findings demonstrate that airway epithelial injury drives downstream vascular responses linked to inflammation and vascular remodelling, establishing REVAS as a human-relevant platform for mechanistic and therapeutic evaluation of cell-cell interactions in COPD and related lung diseases. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=164 HEIGHT=200 SRC="FIGDIR/small/730087v1_ufig1.gif" ALT="Figure 1"> View larger version (59K): org.highwire.dtl.DTLVardef@e29fd8org.highwire.dtl.DTLVardef@6c3d22org.highwire.dtl.DTLVardef@21a53forg.highwire.dtl.DTLVardef@e7f432_HPS_FORMAT_FIGEXP M_FIG C_FIG REVAS: a microfluidic platform developed to model multicellular interactions between airway epithelium and pulmonary vasculature under basal and oxidative stress. COPD: Chronic Obstructive Pulmonary Disease; EMT: endothelial-to-mesenchymal transition; HsEpCs: human small airway epithelial cells; HPMVECs: human pulmonary microvascular endothelial cells; HPAECs: human pulmonary artery endothelial cells; HPASMCs: human pulmonary artery smooth mucle cells; HPFs: human pulmonary fibcroblasts; HPCs: human pericytes.

bioengineering↗

A novel type of gel-like proteasome condensate induced by toxic protein aggregates

Proteasomes reversibly form foci bodies in a liquid-liquid phase separation (LLPS)-dependent manner upon stress. We previously reported that internalized protein aggregates were targeted by proteasome-dense foci1, and proposed that such transient aggregate-associated droplets (TAADs) may facilitate aggregate removal2. Here we use quantitative imaging to show that TAADs represent a novel type of gel-like proteasome condensate. TAADs are irregular in shape and slow to disperse, sequestering proteasomes in agreement with our observation of confined diffusion3. We demonstrate that TAADs co-localize with cytosolic alpha-synuclein aggregates to facilitate their clearance. Inhibition of proteasome- or ubiquitination activity abolishes this aggregate clearance. We identify RAD23B necessary for TAAD formation, amid other co-localizing chaperones and (co-)proteins of the ubiquitin-proteasomes system. TAAD formation is associated with higher proteasomal substrate turnover whilst retaining overall catalytic efficiency, suggestive of altered degradation mechanisms upon aggregate engagement. Proteomics analysis reveals impact on key mitochondrial-associated processes even after TAAD-aggregate disengagement. Similar TAAD-aggregate co-localizations are found in iPSC-differentiated neurons and in disease-relevant samples, with no detection of compromised proteasome activity. Together, our results indicate a model where TAADs concentrate local proteasome activity, which facilitates aggregate clearance in healthy ageing cells. Potentially, should pathological aggregates persist, TAADs may remain engaged and conceivably sequester proteasomes from physiological activities, thus contributing to neurodegenerative disorders.

cell biology↗

A synaptic-astrocytic proteomic signature associated with synaptopathy in Alzheimer's Disease

Synapse loss is the greatest correlate of cognitive impairment in Alzheimers Disease (AD) and offers a therapeutic avenue alongside disease-modifying therapies. However, the events preceding synapse loss in the human condition have not been well characterised. In this study, we describe a pseudotemporal profile of alterations in the synaptic proteome prior to excitatory synapse loss in human post-mortem brain AD tissue using synapse proteomics and synaptome mapping techniques. In a region with early-stage disease pathology, the most predominant changes were pre-synaptic and featured changes in metabolism and exocytosis. In a mid-stage disease state, alongside initial synapse loss, there was a dominance of inhibitory synaptic changes. In a region with late-stage disease pathology and profound synapse loss, post-synaptic changes were most prevalent with a range of canonical synaptic transmission pathways reduced and differential excitatory synapse subtype pathology. Synapse loss was associated with changes in astrocytic proteins which were enriched for those at peri-synaptic astrocytic processes, including an upregulation of complement activation and endocytosis; a signature that differed from the astrocyte cytosolic proteome. Taken together, this provides evidence of a cascade of events leading to synapse loss with multiple points for therapeutic intervention to alleviate cognitive decline in AD. Data are available via ProteomeXchange with identifier PXD056052.

neuroscience↗