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Macrophage Mannose receptor (MRC1) mediates uptake of dextran in murine bone-marrow derived macrophages via a receptor-mediated endocytic process

ABSTRACT: Macrophage Mannose receptor (MRC1) mediates uptake of dextran in murine bone-marrow derived macrophages via a receptor-mediated endocytic process

PROVIDER: PRJNA995620 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25308902.fastq.gz	Fastqsanger.gz
	SRR25308903.fastq.gz	Fastqsanger.gz
	SRR25308904.fastq.gz	Fastqsanger.gz
	SRR25308905.fastq.gz	Fastqsanger.gz
	SRR25308906.fastq.gz	Fastqsanger.gz

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Macrophage Mannose receptor (MRC1) mediates uptake of dextran in murine bone-marrow derived macrophages via a receptor-mediated endocytic process

Project description:CRISPR/Cas9 whole genome screens identify regulators of dextran utpake

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Regulation of circulating mannosylated proteome by macrophage mannose receptor, Mrc1

Project description:Abundance of secreted proteins is tightly regulated in circulation, and its dysregulation forms a basis for development of pathology. N-glycosylation has been shown to be a decisive factor in determining the half-life of these proteins. Exoglycosidases remodel the proteins and exposure of cryptic ligands of endocytic lectin receptors determine their half-lives. We have devised a strategy for non-denaturing enrichment of these mannosylated proteins upon Mrc1 lectin receptor deficiency. Data-independent acquisition mass spectrometry was used to quantify these proteins post-enrichment by mannose-binding lectin (Concanavalin A). We find ligand profile of Mrc1 comprises of over 200 proteins, linking inflammation, organ dysfunction and sepsis to turnover of mannosylated blood proteome. Mannosylated proteome was profiled in mouse plasma upon Mrc1 knock-out and in human plasma upon sepsis. Pathway enrichment was performed to draw parallels between Mrc1 deficiency in mice and sepsis in human.

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Impact of asialoglycoprotein receptor and mannose receptor deficiency on murine plasma N-glycome profiles

Project description:The asialoglycoprotein receptor (ASGPR) and the mannose receptor 1 (MRC1) are C-type lectins that identify and remove glycoproteins from circulation. ASGPR recognizes terminal galactose and N-acetylgalactosamine, whereas MRC1 recognizes terminal mannose, fucose, and N-acetylglucosamine. The effects of ASGPR and MRC1 deficiency on the N-glycosylation of individual circulating proteins have been studied. However, the impact on the homeostasis of the major plasma glycoproteins is debated and their glycosylation has not been mapped with high molecular resolution in this context. Therefore, we evaluated the total plasma N-glycome and plasma proteome of ASGR1 and MRC1 deficient mice.

2023-10-24 | PXD042269 | Pride

Mannose receptor (MRC1) mediates uptake of dextran by bone marrow-derived macrophages.

Project description:Macrophages survey their environment using receptor-mediated endocytosis and pinocytosis. Receptor-mediated endocytosis allows internalization of specific ligands, whereas pinocytosis nonselectively internalizes extracellular fluids and solutes. CRISPR/Cas9 whole-genome screens were used to identify genes regulating constitutive and growth factor-stimulated dextran uptake in murine bone marrow-derived macrophages (BMDM). The mannose receptor c-type 1 (MRC1/CD206) was a top hit in the screen. Targeted gene disruptions of Mrc1 reduced dextran uptake but had little effect on fluid-phase uptake of Lucifer yellow. Other screen hits also differentially affected the uptake of dextran and Lucifer yellow, indicating internalization by separate mechanisms. Visualization of dextran and Lucifer yellow uptake by microscopy showed enrichment of dextran in small puncta, which was inhibitable by mannan, a ligand of MRC1. In contrast, Lucifer yellow predominantly was internalized in larger macropinosomes. In addition, IL4-treated BMDMs internalized more dextran than untreated BMDM correlating with increased MRC1 expression. Therefore, dextran is not an effective marker for pinocytosis in BMDMs since it is internalized by receptor-mediated process. Numerous genes that regulate dextran internalization in primary murine macrophages were identified in the whole-genome screens, which can inform understanding of the regulation of MRC1 expression and MRC1-mediated uptake in macrophages.

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Tumor-associated macrophages derived from circulating inflammatory monocytes degrade collagen through cellular uptake

Project description:Physiologic turnover of interstitial collagen is mediated by a sequential pathway, in which collagen is fragmented by pericellular collagenases, endocytosed by specific collagen receptors, and routed to lysosomes for degradation by lysosomal cathepsins. Here, we used intravital microscopy to investigate if malignant tumors, which are characterized by high rates of extracellular matrix turnover, utilize a similar collagen degradation pathway. Tumors of epithelial, mesenchymal, or neural crest origin all displayed vigorous endocytic collagen degradation with an abundance of cells engaged in this process. These cells were identified as tumor-associated macrophage (TAM)-like cells that degraded collagen in a mannose receptor-dependent manner. Accordingly, increased intra-tumoral collagen was observed in mannose receptor-deficient mice. Whole transcriptome profiling uncovered a distinct extracellular matrix-catabolic signature of these collagen-degrading TAMs. Lineage-ablation studies revealed that collagen-degrading TAMs originated from circulating CCR2+ monocytes. The study identifies a novel function of TAMs in altering the tumor microenvironment through endocytic collagen turnover and establishes macrophages as centrally engaged in tumor-associated collagen degradation.

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2022-06-21 | PXD022546 | Pride

Mannose receptor (CD206) N-glycosylation

Project description:To explore the influence of glycosylation on mannose receptor (MR) binding to glycan ligands, we used the mouse CTLD4-7, fused to the Fc-portion of human IgG (MR-Fc) and human full-length MR. A detailed N- and O-glycopeptide analysis was performed using tryptic glycopeptides. In addition the samples were partially treated with different exoglycosidases to increase glycopeptide coverage.

2023-03-11 | PXD034781 | Pride

Endocytic vesicles act as vehicles for glucose uptake in response to growth factor stimulation

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Diverse Fgfr1 signaling pathways and endocytic trafficking regulate early mesoderm development II

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