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Vilas, A.

Publications and source records attributed to Vilas, A..

3 recordsLinked to original sources

Clonal Hematopoiesis Instructs Maladaptive Tissue Repair to Promote Fibrosis

Tissue repair is increasingly recognized as a systemic process influenced by age-associated changes beyond the injured organ itself. Clonal hematopoiesis of indeterminate potential (CHIP), a common consequence of somatic evolution in hematopoietic stem cells, has been linked to inflammatory disorders, yet whether it directly regulates tissue remodeling remains unclear. Here, we integrate population genomics, preclinical models, and human lung analyses to examine the role of CHIP in fibrotic lung disease. In large cohorts, idiopathic pulmonary fibrosis (IPF) was associated with a distinct CHIP mutational spectrum enriched for non-DNMT3A variants and for larger mutant clones. In mouse models, hematopoietic mutations exacerbated bleomycin-induced fibrosis and reprogrammed macrophages toward inflammatory, profibrotic states, including expansion of a distinct, injury-responsive SPP1+ population conserved in human disease. CHIP-associated macrophages were sufficient to directly promote fibroblast activation and alter epithelial differentiation, linking hematopoietic genotype to parenchymal remodeling. Consistently, a CHIP-derived macrophage transcriptional signature predicted adverse outcomes in independent IPF cohorts. Notably, immune and epithelial alterations were detectable even in the absence of overt injury, indicating that CHIP establishes a primed tissue environment permissive for maladaptive repair. Together, these findings identify clonal hematopoiesis as a systemic regulator of tissue repair and demonstrate that somatic evolution in blood can actively instruct organ remodeling through immune-parenchymal interactions. This framework supports the possibility that disease-associated selective pressures may shape clonal architecture with functional consequences for organ health.

immunology↗

High conformational flexibility of phosphomannomutase 2: Implications for functioning mechanisms, stability and pharmacological chaperone design

Phosphomannomutase 2 (PMM2) is a critical enzyme in the N-glycosylation pathway, and its defect is the cause of the most common congenital disorder of glycosylation. Despite its biological relevance, the understanding of PMM2 is limited, as the catalytic mechanism and required conformational dynamics remain unknown. In this study, we investigated murine PMM2 (Pmm2) to elucidate its structural flexibility and functional insights. High-resolution crystal structures of Pmm2 in both apo and activator-bound forms provided a more detailed model of the protein, underscoring the role of three ionic cofactors that are essential for dimerization, catalysis, and stability. The Pmm2 structures also provided eight distinct conformations of the protein subunit, highlighting its dynamic nature. Structural comparisons among Pmm2, human PMM2 and other phosphomannomutases helped define the architecture of the enzyme as a dimer assembled by the rigid association of the cap domains, which provide a flat platform from which the core domains of each subunit protrude in a flexible manner. Molecular dynamics (MD) simulations of the human and murine PMM2s further emphasized the enzymes substantial conformational flexibility, revealing extensive core domain movements and suggesting potential inter-subunit communication within the dimer. This study refines the model of PMM2 function, demonstrating its dynamic role in substrate binding, intermediate reorientation, and product release. The observed flexibility provides new opportunities to target specific enzyme states, enabling the development of pharmacological chaperones.

biochemistry↗

Transcriptional Characterization of the Stromal and Endothelial Bone Marrow Microenvironment during Progression from MGUS to Multiple Myeloma

The role of the non-immune bone marrow microenvironment (BME) in the transition from monoclonal gammopathy of undetermined significance (MGUS) into clinically active multiple myeloma (MM) remains incompletely defined. To address this, we transcriptionally profiled endothelial cells (EC), mesenchymal stem cells (MSC) and MM cells at single-cell resolution from two genetically engineered mouse models (BIc{gamma}1 and MIc{gamma}1) that recapitulate MGUS to MM progression. Our analysis revealed distinct transcriptional trajectories in EC and MSC, uncovering stage-specific BME-PC interactions shaping disease progression. EC acquired a stress phenotype during MGUS transitioning to angiogenesis in MM, while MSC exhibited early impaired differentiation capacity during MGUS that persisted in MM. Notably, an interferon (IFN)-associated MM signature was detected in EC and MSC from the BIc{gamma}1 model but was absent in the more aggressive MIc{gamma}1 model. Treatment with bortezomib, lenalidomide, and dexamethasone remodeled the BME by suppressing MM-IFN signaling, promoting an adaptive response in EC, and restoring osteogenic potential in MSC-- shifting the niche toward a less tumor-permissive state. Importantly, the MM-IFN signature was validated in patients across the MGUS-to-MM spectrum, supporting the translational relevance of our findings. Together, these data define novel dynamic and targetable alterations in the non-immune BME during myeloma progression. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=97 SRC="FIGDIR/small/589777v5_ufig1.gif" ALT="Figure 1"> View larger version (28K): org.highwire.dtl.DTLVardef@1a0ef62org.highwire.dtl.DTLVardef@c44014org.highwire.dtl.DTLVardef@4b1df6org.highwire.dtl.DTLVardef@19c29a2_HPS_FORMAT_FIGEXP M_FIG C_FIG

cancer biology↗