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Biology subjects

Jones, D. J. L.

Publications and source records attributed to Jones, D. J. L..

3 recordsLinked to original sources

Loss of PKN2 drives fibroblast reprogramming and extracellular matrix remodelling in pulmonary fibrosis

Introduction Idiopathic pulmonary fibrosis (IPF) is a progressive fibrotic lung disease characterised by aberrant fibroblast function, extracellular matrix (ECM) remodelling and defective tissue repair. Protein kinase N2 (PKN2) is associated with accelerated forced vital capacity decline in IPF, but its functional role in pulmonary fibrosis remains unknown. We hypothesised that PKN2 regulates fibroblast phenotype and tissue repair. Methods PKN2 expression was assessed in human lung tissue, induced sputum and primary airway and parenchymal fibroblasts from non-fibrotic controls and patients with interstitial lung disease (ILD). DNA methylation was profiled using the Illumina HumanMethylationEPIC array. PKN2 function was investigated by siRNA-mediated depletion in primary human lung fibroblasts using transcriptomic, proteomic and functional analyses. Tissue repair was assessed following pharmacological PKN inhibition in zebrafish. Results PKN2 expression was reduced in ILD lung tissue and primary airway and parenchymal fibroblasts and further suppressed by TGF-{beta}1. Differential methylation was identified across the PKN2 locus in both fibroblast populations. Integrated transcriptomic and proteomic profiling following PKN2 depletion revealed coordinated remodelling of ECM, cell adhesion, non-canonical WNT and VEGF pathways, including dysregulation of COL1A1, WNT, VEGF and MMP1. PKN2 loss increased VEGF and MMP-1 secretion and accelerated fibroblast wound closure. PKN inhibition altered epithelial organisation and collagen fibre alignment during zebrafish wound repair. Conclusion PKN2 loss drives fibroblast reprogramming and aberrant ECM remodelling, establishing PKN2 as an important regulator of pulmonary fibroblast homeostasis and tissue repair.

cell biology↗

The single nucleotide polymorphism rs1053230 modulates kynurenine 3-monooxygenase stability and is associated with cognitive and mood phenotypes

BackgroundThe single nucleotide polymorphism (SNP) rs1053230 within the kynurenine 3-monooxygenase (KMO) gene encodes either an arginine (CGC) or cysteine (TGC) at amino acid residue 452. The rs1053230 genotype is associated with alterations in KMO expression and activity, and impaired cognition. Additionally, KMO intronic SNP rs2275163 is associated with schizophrenia endophenotypes. However, the direct functional consequences of these SNPs on KMO function have never been investigated. MethodsHere we performed the first in vitro cell-based examination of the rs1053230 genotype on KMO expression, activity, cellular localisation and KMO-protein interactions, as well as examination of the effects of rs1053230 on schizophrenia-relevant clinical measures. We also examined the effects of rs2275163 genotype on KMO pre-mRNA stability and alternative splicing. ResultsHEK293T cells expressing KMO-Arg452 or KMO-Cys452 with a red fluorescent protein (RFP) tag produced equivalent levels of KMO mRNA, protein and enzymatic activity, and localised to mitochondria to the same extent. However, cycloheximide-mediated inhibition of protein translation revealed a striking reduction in protein stability of KMO-Arg452-RFP. KMO-RFP-trap pull-down followed by tandem liquid-chromatography-mass spectrometry (LC-MS/MS) identified dramatic differences in protein partners between KMO variants. Indeed, gene ontology-term enrichment analysis revealed that terms associated with synaptic function were more highly enriched amongst KMO-Cys452 interacting proteins. rs1053230 genotype was found to associate with chronic, trait-like depressive mood symptoms in patients. rs2275163 genotype had no effect on KMO pre-mRNA. ConclusionsDifferences in protein stability and protein-protein interactions may underlie the mechanisms by which the KMO rs1053230 genotype influences neuronal function, leading to cognitive differences in psychiatric conditions.

molecular biology↗

Proteomic analysis of extracellular vesicles released from endothelial cells in vitro reveals increased levels of E-selectin and dual specificity phosphatase 7 as a potential marker of TNFα-mediated apoptosis

Proteins can be actively packaged into extracellular vesicles (EVs) through mechanisms dependent on the stimulus that activated the cells. Identifying proteins released in endothelial EVs in response to stimuli relevant to cardiovascular disease (CVD) may therefore reveal potential biomarkers that provide information about the vascular endothelium. This study aimed to identify differentially expressed proteins in EVs released from human umbilical vein endothelial cells (HUVEC) in response to stimuli relevant to vascular endothelium activation. HUVEC were stimulated with TNF (10 ng/mL) or oxLDL (10 {micro}g/mL). Apoptosis was assessed using a flow cytometric DNA fragmentation protocol and caspase-3/7 activity assay. Size distributions of EVs were examined by nanoparticle tracking analysis. Isolated EVs were examined using tandem liquid-chromatography-mass spectrometry (LC-MS/MS). While treatment of HUVECs with TNF or oxLDL resulted in non-significant elevations in levels of EVs, only TNF increased apoptosis. Mass spectrometry quantified 1355 proteins and revealed significant differences in the proteome of EVs from TNF-treated HUVEC compared to EVs from oxLDL-treated or untreated cells. Several candidate biomarkers were significantly and differentially expressed in response to TNF, including E-selectin and dual specificity phosphatase 7. This study further associated E-selectin on endothelial-derived EVs with endothelial apoptosis and may offer a biomarker of endothelial damage in patients with CVD.

cell biology↗