Search bioRxiv⌕ Search

bioRxiv · 10.1101/610162

TLR4-dependent signaling drives extracellular catabolism of low-density lipoprotein aggregates

Abstract

ObjectiveAggregation and modification of low-density lipoproteins (LDL) promotes their retention and accumulation in the arteries. This is a critical initiating factor during atherosclerosis. Macrophage catabolism of aggregated LDL (agLDL) occurs using a specialized extracellular, hydrolytic compartment, the lysosomal synapse (LS). Compartment formation by local actin polymerization and delivery of lysosomal contents by exocytosis promotes acidification of the compartment and degradation of agLDL. Internalization of metabolites such as cholesterol promotes foam cell formation, a process that drives atherogenesis. Further, there is accumulating evidence for the involvement of TLR4 and its adaptor protein MyD88 in atherosclerosis. Here, we investigated the role of TLR4 in catabolism of agLDL using the LS and foam cell formation.\n\nApproach and ResultsUsing bone marrow-derived macrophages (BMMs) from knockout mice, we find that TLR4 and MyD88 regulate compartment formation, lysosome exocytosis, acidification of the compartment and foam cell formation. Using siRNA, pharmacological inhibition and knockout BMMs, we implicate SYK, PI3 kinase and Akt in agLDL catabolism using the LS. Using bone marrow transplantation of LDL receptor knockout mice with TLR4KO bone marrow, we show that deficiency of TLR4 protects macrophages from lipid accumulation during atherosclerosis. Finally, we demonstrate that macrophages in vivo form an extracellular compartment and exocytose lysosome contents similar to that observed in vitro for degradation of agLDL.\n\nConclusionsWe present a mechanism in which interaction of macrophages with agLDL initiates a TLR4 signaling pathway, resulting in formation of the LS, catabolism of agLDL and lipid accumulation in vitro and in vivo.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Singh, R. K., Haka, A. S., Asmal, A., Barbosa-Lorenzi, V. C., Grosheva, I., Chin, H. F., Xiong, Y., Hla, T., Maxfield, F. R.. 2019-04-15. TLR4-dependent signaling drives extracellular catabolism of low-density lipoprotein aggregates. https://doi.org/10.1101/610162

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Endothelial Cell Specific Thioredoxin 1-Dependent Signaling in Oxygen-1 Induced Retinopathy

Purpose: Retinopathy of prematurity (ROP) is a leading cause of childhood blindness, characterized byoxidative stress and dysregulated angiogenesis in preterm infants with immature antioxidant systems.This study aimed to investigate the specific role of endothelial cell-specific thioredoxin 1 (TXN1), a crucial oxidoreductase, in oxygen-induced retinopathy, hypothesizing that the absence of endothelial TXN1 directly impairs angiogenesis and exacerbates hyperoxia-induced injury. Methods: We generated tamoxifen-inducible, endothelial cell-specific Txn1 knockout mice (Txn1-iECKO) and utilized the oxygen-induced retinopathy (OIR) model, exposing litters to 85% oxygen from postnatal day 7 (P7) to P12. Retinal vascular morphology during vaso-obliteration and neovascularization phases, endothelial cell proliferation, and apoptotic cell death were assessed. Furthermore, human retinal microvascular endothelial cells (HRMECs) with TXN1 knockdown were subjected to hyperoxic conditions, followed by comprehensive gene expression profiling using RT2 Profiler PCR arrays and Ingenuity Pathway Analysis. Results: Deletion of endothelial Txn1 significantly enhanced vascular regression during the hyperoxic vaso-obliteration phase at P12 and markedly exacerbated pathological neovascularization at P17. Txn1-deficient retinas exhibited significantly impaired endothelial cell proliferation during the vaso-obliteration phase, while apoptotic cell death remained unchanged. Transcriptomic analysis of TXN1-deficient HRMECs under hyperoxia revealed an enhanced activation of NRF2-mediated oxidative stress response pathways. Conclusions: These findings identify endothelial TXN1 as an essential and oxygen-dependent regulator of vascular development in ischemic retinopathy, primarily influencing endothelial proliferation and redox signaling. This suggests TXN1's crucial protective role and highlights its therapeutic potential to mitigate ROP progression by modulating endothelial cell responses to oxidative stress.

cell biology↗

A Dynamic Stem Cell State Links Environmental Cues to Skeletal and Regenerative Fates

Stem cells faithfully generate tissue architecture during development, yet how their identity and regenerative output are reshaped as anatomical niches mature and environmental signals change with aging and injury remains poorly understood. Rare skeletal stem cells (SSCs) across diverse skeletal sites are defined by combinations of cell-surface markers, precluding their genetic interrogation in vivo. Here, using spatially informed single cell transcriptomics, we identify Pannexin-3 (Panx3) to mark a dynamic functional state within bona fide SSCs and establish Panx3-CreERT2 mice for its longitudinal interrogation. Panx3 SSCs exhibit long-term clonal persistence, self-renewal and multipotency, whereas Panx3- SSCs can acquire this state. Successive SSC cohorts engage the Panx3 state during skeletal development, osteoanabolic stimulation expands pre-existing Panx3 SSC clones and injury induces it locally in previously unlabeled progenitors. Thus, anatomically distinct progenitors can converge on a common stem cell state in response to different environmental inputs. Three-dimensional reconstruction of chondrogenic niches further identifies signals that redirect Panx3-lineage cells towards stable cartilage, enabling durable regeneration in aged and osteoarthritic joints and with human SSCs. These findings establish anatomical origin, stem cell state and lineage fate as separable dimensions of stem cell identity and provide genetic access for interrogating and directing endogenous SSC function.

cell biology↗

Proteome-wide profiling reveals compartment-specific RNA buffering of protein aggregation during stress

Cellular adaptation to stress requires extensive remodeling of RNA metabolism. The rewiring of the RNA-protein interaction landscape and the assembly of biomolecular condensates are central to this response, yet the global stress-induced reorganization of macromolecular RNA-protein assemblies remains incompletely characterized. Here, we apply R-DeeP, a density gradient approach coupled to quantitative mass spectrometry, to profile the RNA-dependent sedimentation behaviour of the Saccha-romyces cerevisiae proteome during heat and salt stress. We demonstrate that stress triggers a profound, stress-specific reorganization of the RNA interactome. Many proteins undergo pronounced, selective shifts into high-molecular weight fractions, indicative of aggregation. RNase treatment markedly exacerbates this aggregation, consistent with the model that RNA acts as a general chaperone that keeps proteins with intrinsically disordered regions soluble. Strikingly, our data demonstrate that this protection is compartmentalised. Nuclear proteins are partially shielded from stress-induced aggregation. This protection coincides with the nuclear accumulation of RNA caused by a block of RNA export during stress, and RNase treatment abolishes this protection. Nuclear RNA retention may therefore act as a buffer that actively increases the local chaperoning capacity of the nucleus. In contrast, cytoplasmic proteins, including translation factors and ribonucleoprotein granule components, exhibit increased aggregation under stress. Fluorescence microscopy confirmed that increased biochemical aggregation in density gradients reflects changes in assembly state in vivo. For many stress-induced aggregators, these changes are visible as spatial reorganisation in stressed cells, such as the formation of foci. Our findings suggest that cells use subcellular RNA distribution to tune the condensation and/or aggregation threshold of proteins in a compartment-specific manner.

cell biology↗