Search bioRxiv⌕ Search

Biology subjects

de Koning, L.

Publications and source records attributed to de Koning, L..

7 recordsLinked to original sources

Exploiting pair correlation function to describe biological tissue structure

Multiplexed imaging technologies now enable the simultaneous profiling of hundreds to thousands of molecular targets in intact tissues, providing unprecedented insight into cellular heterogeneity and spatial organization. While data generation has rapidly matured, the quantitative analysis of spatial structure remains challenging and poorly standardized, particularly across biological length scales. Existing approaches, such as distance-based metrics, neighborhood analyses and graph neural networks, either capture only local interactions or sacrifice interpretability for predictive power. Here we introduce PCF-SiM (Pair Correlation Function Sigmoid Modeling), a scalable and interpretable framework that leverages parametric modeling of the pair correlation function to quantify spatial organization in multiplexed imaging data. PCF-SiM compresses complex spatial patterns into a small set of biologically meaningful parameters, enabling robust comparisons across cell types, samples and conditions. Applying PCF-SiM to diverse public spatial transcriptomics datasets, we demonstrate its ability to detect condition-dependent tissue remodeling in a mouse colitis model. We further extend the framework with a co-scaling strategy that identifies cell types participating in shared spatial structures. Using newly generated clinical datasets from Hashimotos thyroiditis and uveal melanoma liver metastases, PCF-SiM reveals hierarchical organization of autoimmune infiltrates and coordinated spatial interactions between lymphatic endothelial cells and tumor-infiltrating lymphocytes. Finally, we show that reliable inference of tissue-scale architecture requires whole-slide imaging, exposing intrinsic limitations of tumor microarray-based spatial analyses. Together, PCF-SiM provides a principled and interpretable approach for spatial analysis of multiplexed imaging data.

bioinformatics↗

Lineage commitment pathways epigenetically oppose oncogenic Gαq/11-YAP signaling in dormant disseminated uveal melanoma

Uveal melanoma (UM) can remain in clinical dormancy for decades only to later produce lethal metastases. Using Gq/11mut/BAP1wt UM xenograft models and human metastatic samples, we identified NR2F1 as a key inducer of UM disseminated cancer cell (DCC) dormancy. Dormant UM DCCs upregulate NR2F1, neural crest genes and, along with suppression of proliferation programs, NR2F1 silences YAP1/TEAD1 transcription by altering histone H3 activation marks. YAP1 can reciprocally repress NR2F1, but inhibiting Gq/11 signaling or activating NR2F1 can arrest UM growth. NR2F1 knockout led to dormant DCC awakening and liver metastatic growth. NR2F1 and YAP1 inverse expression was confirmed in human livers carrying UM solitary, small DCC clusters as well as large metastases. Intriguingly, RNA-seq and Cut&Run analysis revealed that NR2F1 short-circuits oncogene signaling by repressing multiple G-protein signaling components. Our work provides previously unrecognized mechanistic insight into UM DCC dormancy and potential pathways for interception. Statement of significanceNR2F1 epigenetically suppresses genes associated with G-protein signaling, cell cycle, and YAP1/TEAD1 pathways, inducing dormancy in uveal melanoma (UM) disseminated cancer cells. This study unveils novel markers for UM dormancy and reactivation, positioning NR2F1 as a promising target for intercepting residual and UM metastatic disease.

cancer biology↗

Multicenter reverse-phase protein array data integration

Among the technologies available for protein biomarker discovery and validation, reverse-phase protein array (RPPA) benefits from unequalled sample throughput. Panels of high-quality antibodies enable the quantification by RPPA of protein abundance and posttranslational modifications in biological specimens with high precision and sensitivity. Incorporation of RPPA technology into clinical and drug development pipelines requires robust assays that generate reproducible results across multiple laboratories. We implemented the first international multicenter pilot study to investigate RPPA workflow variability. We characterized the proteomic responses of a series of breast cancer cells to two cancer drugs. This analysis quantified 86,832 sample spots, representing 108 biological samples, arrayed at three independent RPPA platforms. This unique integrated set of data is publicly available as a resource to the proteomic and cancer research communities to catalyse further analysis and investigation. We anticipate that this dataset will form a reference for the comparison of RPPA workflows and reagents, which can be expanded in the future, and will aid the identification of platform-robust treatment-marker antigens in breast cancer cells. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=95 SRC="FIGDIR/small/458377v1_ufig1.gif" ALT="Figure 1"> View larger version (17K): org.highwire.dtl.DTLVardef@e2fb2forg.highwire.dtl.DTLVardef@1d8f425org.highwire.dtl.DTLVardef@84dd60org.highwire.dtl.DTLVardef@e1ccf7_HPS_FORMAT_FIGEXP M_FIG C_FIG

biochemistry↗

Integrative analysis of multi-platform reverse-phase protein array data for the pharmacodynamic assessment of response to targeted therapies

Reverse-phase protein array (RPPA) technology uses panels of high-specificity antibodies to measure proteins and protein post-translational modifications in cells and tissues. The approach offers sensitive and precise quantification of large numbers of samples and has thus found applications in the analysis of clinical and pre-clinical samples. For effective integration into drug development and clinical practice, robust assays with consistent results are essential. Leveraging a collaborative RPPA model, we set out to assess the variability between three different RPPA platforms using distinct instrument set-ups and workflows. Employing multiple RPPA-based approaches operated across distinct laboratories, we characterised a range of human breast cancer cells and their protein-level responses to two clinically relevant cancer drugs. We integrated multi-platform RPPA data and used unsupervised learning to identify protein expression and phosphorylation signatures that were not dependent on RPPA platform and analysis workflow. Our findings indicate that proteomic analyses of cancer cell lines using different RPPA platforms can identify concordant profiles of response to pharmacological inhibition, including when using different antibodies to measure the same target antigens. These results highlight the robustness and the reproducibility of RPPA technology and its capacity to identify protein markers of disease or response to therapy.\n\nO_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=58 SRC=\"FIGDIR/small/769158v1_ufig1.gif\" ALT=\"Figure 1\">\nView larger version (19K):\norg.highwire.dtl.DTLVardef@3b72aeorg.highwire.dtl.DTLVardef@e62fe4org.highwire.dtl.DTLVardef@5238c3org.highwire.dtl.DTLVardef@ca925_HPS_FORMAT_FIGEXP M_FIG C_FIG

cancer biology↗

Integrative analysis of proteome and transcriptome dynamics during Bacillus subtilis spore revival

Bacillus subtilis forms highly resistant, metabolically inactive dormant spores upon nutrient limitation. These endospores pose challenges to the food and medical sectors. Spores reactivate their metabolism upon contact with germinants and develop into vegetative cells. The activation of the molecular machinery that triggers the progress of germination and spore outgrowth is still unsettled. To gain further insight in spore germination and outgrowth processes, the transcriptome and proteome changeover during spore germination and outgrowth to vegetative cells, was analysed. B. subtilis transcriptome analysis allow us to trace the different functional groups of genes expressed. For each time-point sample, the change in the spore proteome was quantitatively monitored relative to the reference proteome of 15N metabolically labelled vegetative cells. We observed until the phase transition, i.e. completion of germination, no significant change in the proteome. We have identified 36 transcripts present abundantly in the dormant spores. This number is in close agreement with the previous findings. These transcripts mainly belong to the genes encoding small acid soluble proteins (sspE, sspO, sspI, sspK, sspF) and proteins with uncharacterized functions. We observed in total 3152 differentially expressed genes, but only 323 differentially expressed proteins (total 451 proteins identified and quantified). Our data shows that 173 proteins from dormant spores, both spore unique proteins and protein shared with vegetative cells, are lost during the phase transitioning period. This loss is in addition to the active protein degradation, undertaken by the spore proteases such as Gpr, as germination and outgrowth proceeds. Further analysis is required to functionally interpret the observed protein loss. The observed diverse timing of the synthesis of different protein sets reveals a putative core-strategy of the revival of life starting from the B. subtilis spore.

microbiology↗

Towards the minimal proteome of life: Proteome profiles of Bacillus subtilis vegetative cells and spores

The method of 15N metabolic labelling of Bacillus subtilis enabled mass spectrometric quantification of relative protein levels in the vegetative cells and the spores of this model organism. A total of 1501 proteins have been identified from the combined spore and vegetative cell samples. From these 1086 proteins have been relatively and reproducibly quantified between spores and vegetative cells. Of the quantified proteins, 60% are common to the vegetative cells and spores, indicating that spores host a minimal set proteins sufficient for the resumption of metabolism upon completion of germination. The shared proteins represent, the most basic survival kit for life on earth that is known thus far.

microbiology↗

Slug/Snail2 is involved in the repression of proliferation genes by TGF-β in bronchial epithelial progenitor cells and is deregulated in abnormal epithelium

Slug/Snail2 belongs to the Epithelial-Mesenchymal Transition (EMT)-inducing transcription factors involved in development and diseases. Slug is expressed in adult stem/progenitor cells of several epithelia, making it unique among these transcription factors. To investigate Slug role in human bronchial epithelium progenitors, we studied primary bronchial basal/progenitor cells in an air-liquid interface culture system that allows regenerating a bronchial epithelium. To identify Slug downstream genes we knocked down Slug in basal/progenitor cells from normal subjects and subjects with COPD, a respiratory disease presenting anomalies in the bronchial epithelium and high levels of TGF-{beta} in the lungs. We show that normal and COPD bronchial basal/progenitors, even when treated with TGF-{beta}, express both epithelial and mesenchymal markers, and that the epithelial marker E-cadherin is not a target of Slug and, moreover, positively correlates with Slug. We reveal that Slug downstream genes responding to both differentiation and TGF-{beta} are different in normal and COPD progenitors, with in particular a set of proliferation-related genes that are among the genes repressed downstream of Slug in normal but not COPD. In COPD progenitors at the onset of differentiation in presence of TGF-{beta}, we show that there is positive correlations between the effect of differentiation and TGF-{beta} on proliferation-related genes and on Slug protein, and that their expression levels are higher than in normal cells. As well, the expression of Smad3 and {beta}-Catenin, two molecules from TGF-{beta} signaling pathways, are higher in COPD progenitors, and our results indicate that proliferation-related genes and Slug protein are increased by different TGF-{beta}-induced mechanisms. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=109 SRC="FIGDIR/small/674127v2_ufig1.gif" ALT="Figure 1"> View larger version (15K): org.highwire.dtl.DTLVardef@524a15org.highwire.dtl.DTLVardef@7dd1e5org.highwire.dtl.DTLVardef@5f3798org.highwire.dtl.DTLVardef@13ae179_HPS_FORMAT_FIGEXP M_FIG C_FIG

cell biology↗