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Bedford, G. C.

Publications and source records attributed to Bedford, G. C..

4 recordsLinked to original sources

Induction of hysteretic chromatin states by CRISPRa reveals locus-specific encoding of transcriptional memory

Transcriptional memory is a phenomenon that allows cells to 'remember' prior stimulatory history, which can alter subsequent gene expression patterns and shape development, immunity, and disease. Although various epigenetic adaptations have been implicated, it remains unclear whether the mechanics of transcription alone are sufficient to install durable memory independently of complex activation and global phenotypic changes induced by inflammatory and environmental stimuli. Here, we employ CRISPR activation (CRISPRa) to uncouple gene activation from global signaling and test whether memory can be established selectively by a local transcriptional pulse in primary mesenchymal stromal cells (MSCs). Key stimulus-responsive genes (IDO1, CXCL11) remain sensitized for weeks after either IFN{gamma} exposure or locus-specific CRISPRa perturbations. Histone PTM profiling links this memory to epigenetic hysteresis involving persistent loss of promoter H3K27me3. Single-molecule chromatin mapping by DAF-seq showed that this adaptation does not coincide with gains in promoter accessibility, but suggests it supports increased transcription factor reacquisition in rechallenged cells. Finally, while H3K27me3 loss appears to be a key hallmark of strongly induced memory genes, multi-omic analyses showed that persistent H3K27me3 hysteresis also occurs at a small subset of non-memory genes. Coordination of H3K27me3 hysteresis with additional cis factors therefore likely shapes transcriptional memory in a locus-specific fashion, underscoring the utility of targeted CRISPRa perturbations for dissecting these responses.

molecular biology↗

Loss of Syndecan-3 Drives a Pro-inflammatory, EndMT-prone Phenotype in Aortic Valve Endothelial Cells

The earliest events in calcific aortic valve disease (CAVD) occur at the valve endothelium, where the cells lining the leaflet undergo NF-kappaB (Nuclear Factor kappa B)-driven inflammatory activation and endothelial-to-mesenchymal transition (EndMT). The endothelial glycocalyx (EG) sets the threshold at which endothelial cells (ECs) respond to such cues, yet its composition and function in the aortic valve remain almost entirely uncharacterized. Here we define the cell-surface proteoglycan (CPG) landscape of human aortic valve endothelial cells (HAVECs) under inflammatory stimulation and identify syndecan-3 (SDC3) as a regulator of valve endothelial activation. Among the proteoglycans examined, SDC3 was highly expressed and inflammation-responsive. Silencing SDC3 in unstimulated HAVECs was sufficient to upregulate NF-kappaB pathway components and the leukocyte adhesion molecules vascular cell adhesion molecule-1 (VCAM1), intercellular adhesion molecule-1 (ICAM1), and E-selectin, and it amplified their induction upon TNF-alpha challenge. Pharmacological inhibition of IKKbeta; abolished this difference, placing SDC3 upstream of NF-kappaB, while SDC3 overexpression attenuated tumor necrosis factor-alpha (TNF-alpha)-induced VCAM1, the inverse of the knockdown effect. Loss of SDC3 further primed HAVECs toward a mesenchymal, EndMT-prone phenotype under transforming growth factor-beta 2 (TGF-beta2) stimulation, marked by increased smooth muscle protein 22-alpha (SM22alpha) and reduced platelet endothelial cell adhesion molecule (PECAM1/CD31). Together, these findings identify SDC3 as an endogenous restraint on the inflammatory and mesenchymal programs that characterize the endothelial phase of CAVD and establish the valve endothelial glycocalyx as a previously unappreciated yet potent regulator of aortic valve endothelial dysfunction. Preserving or augmenting SDC3 may warrant investigation as a means of holding valve endothelial cells in a quiescent state.

pathology↗

Tailoring a CRISPR/Cas-based Epigenome Editor for Programmable Chromatin Acylation and Decreased Cytotoxicity

CRISPR-based epi-editors can robustly modulate cellular transcription and chromatin structure, but off-target activity and cytotoxicity limit their utility. Here, we engineer the acyl-CoA binding pocket of the human p300 histone acyltransferase to reduce its cytotoxicity and tune its acylation profile when fused to dCas9. We discover a single amino acid substitution (I1417N) that decreases cytotoxicity related to exogenous p300 overexpression yet preserves dCas9-p300 mediated histone acetylation and gene activation. We find that dCas9-p300 I1417N is less perturbative to the transcriptome and proteome of human cells, and that this behavior is driven by favorable stability kinetics. We also develop a crotonylation-biased dCas-p300 variant (I1395G) that selectively deposits histone crotonylation and activates transcription from endogenous promoters at levels comparable to wild-type p300. The p300 variants generated here enhance epi-editing capabilities and demonstrate that engineering of catalytic domains can be a powerful strategy for tailoring enzymatic activities and mitigating effector-driven toxicity in epi-editing.

synthetic biology↗

Persistent tailoring of MSC activation through genetic priming

Mesenchymal stem/stromal cells (MSCs) are an attractive platform for cell therapy due to their safety profile and unique ability to secrete broad arrays of immunomodulatory and regenerative molecules. Yet, MSCs are well known to require preconditioning or priming to boost their therapeutic efficacy. Current priming methods offer limited control over MSC activation, yield transient effects, and often induce expression of pro-inflammatory effectors that can potentiate immunogenicity. Here, we describe a genetic priming method that can both selectively and sustainably boost MSC potency via the controlled expression of the inflammatory-stimulus-responsive transcription factor IRF1 (interferon response factor 1). MSCs engineered to hyper-express IRF1 recapitulate many core responses that are accessed by biochemical priming using the proinflammatory cytokine interferon-{gamma} (IFN{gamma}). This includes the upregulation of anti-inflammatory effector molecules and the potentiation of MSC capacities to suppress T cell activation. However, we show that IRF1-mediated genetic priming is much more persistent than biochemical priming and can circumvent IFN{gamma}-dependent expression of immunogenic MHC class II molecules. Together, the ability to sustainably activate and selectively tailor MSC priming responses creates the possibility of programming MSC activation more comprehensively for therapeutic applications. GRAPHICAL ABSTRACT O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=158 SRC="FIGDIR/small/578489v1_ufig1.gif" ALT="Figure 1"> View larger version (49K): org.highwire.dtl.DTLVardef@8be46aorg.highwire.dtl.DTLVardef@40fcdeorg.highwire.dtl.DTLVardef@995a21org.highwire.dtl.DTLVardef@1ec53d0_HPS_FORMAT_FIGEXP M_FIG C_FIG

bioengineering↗