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Muntjewerff, E. M.

Publications and source records attributed to Muntjewerff, E. M..

4 recordsLinked to original sources

T cells compete via reverse MHC class I signaling at the synapse with dendritic cells to secure Golgi recruitment for activation

Interleukin-12 (IL-12) is a key immunostimulatory cytokine produced by dendritic cells (DCs) upon infection that plays a central role in the activation and differentiation of cytotoxic T cells. Notably, IL-12 is secreted in a highly polarized manner from late endosomes or lysosomes at the contact interface between a DC and a T cell, known as the immunological synapse. However, the signaling mechanisms initiating this spatially restricted cytokine release remain poorly defined. Here, using artificial T cell mimics, beads coated with T cell surface ligands, we show that antigen recognition induces recruitment of the DCs microtubule organizing center (MTOC) and Golgi apparatus to the immunological synapse via reverse MHC class I signaling. Our results further indicate that the signaling pathways governing MTOC polarization are highly conserved in DCs, consistent with mechanisms described in other immune cell types. As newly synthesized IL-12 traffics through the Golgi, this intracellular reorientation facilitates localized release of IL-12 directly at the site of T cell engagement, likely enabling DCs to focus their stimulatory capacity on responsive T cells within the crowded environment of secondary lymphoid organs. Furthermore, by applying spatially patterned antibody arrays targeting MHC class I, we reveal that MTOC polarization is biased toward sites exhibiting the strongest reverse MHC class I signaling. This suggests that IL-12 is preferentially released at synapses formed with T cells displaying higher T cell receptor affinity, providing a mechanism for selection of the most potent T cell.

immunology↗

Loss of chromogranin A and catestatin affect pancreatic islet homeostasis, endocrine function, and neurotransmitters

Chromogranin A (CgA), a neuroendocrine pro-hormone, undergoes proteolytic cleavage to yield bioactive peptides, notably catestatin (CST) and pancreastatin (PST), which exert opposing effects on metabolic and inflammatory processes. Using CgA and CST knockout (KO) mice, this study investigated their roles in pancreatic endocrine function, morphology, neurotransmitter dynamics, and systemic glucose homeostasis. CST deficiency induced insulin resistance, altered islet architecture, and heightened catecholamine levels, whereas CgA-KO mice lacking both CST and PST exhibited improved insulin sensitivity due to absence of PST. CST suppressed gluconeogenesis and enhanced glucagon regulation, while PST promoted insulin resistance and glucose production. Spatial mass spectrometry revealed altered neurotransmitter and polyamine profiles in pancreatic islets, implicating disrupted nerve-immune-islet interactions. CSTs modulation of catecholaminergic and inflammatory pathways positions it as a key regulator in the neuro-immune-endocrine axis. These findings highlight the therapeutic potential of targeting CgA-derived peptides, especially CST, for managing diabetes and metabolic-inflammatory diseases through precise peptide-based interventions.

immunology↗

The anti-inflammatory peptide Catestatin blocks chemotaxis

Increased levels of the anti-inflammatory peptide catestatin (CST), a cleavage product of the pro-hormone chromogranin A, correlates with less severe outcomes in hypertension, colitis and diabetes. However, it is unknown how CST reduces the infiltration of monocytes and macrophages in inflamed tissues. Here, we report that CST blocks leukocyte migration towards inflammatory chemokines. By in vitro and in vivo migration assays, we show that although CST itself is weakly chemotactic, it blocks migration of monocytes and granulocytes to inflammatory attracting factor CC-chemokine ligand 2 (CCL2) and macrophage inflammatory protein 2 (MIP-2). Moreover, it directs CX3CR1+ macrophages away from pancreatic islets. These findings support the emerging notion that CST is a key anti-inflammatory modulator.

cell biology↗

Chromogranin A regulates gut permeability via the antagonistic actions of its proteolytic peptides

AimA leaky gut barrier has been implicated in the initiation and progression of a multitude of diseases, e.g., inflammatory bowel disease, irritable bowel syndrome, celiac disease, and colorectal cancers. Here we show how pro-hormone Chromogranin A (CgA), produced by the enteroendocrine cells, and Catestatin (CST: hCgA352-372), the most abundant CgA-derived proteolytic peptide, affect the gut barrier. MethodsColon tissues from region-specific CST-knockout (CST-KO) mice, CgA-knockout (CgA-KO) and WT mice were analyzed by immunohistochemistry, ultrastructural and flowcytometry studies. FITC-dextran assays were used to measure intestinal barrier function. Mice were supplemented with CST or CgA fragment pancreastatin (PST: CgA250-301). The microbial composition of cecum was determined. CgA and CST levels were measured in blood of IBD patients. ResultsCST-KO mice displayed (i) elongated tight, adherens junctions and desmosomes similar to IBD patients, and (ii) gut inflammation. Consistently, plasma FITC-dextran measurements showed increased intestinal paracellular permeability in the CST-knockout mice. This correlated with a higher ratio of Firmicutes to Bacteroidetes, a dysbiotic pattern commonly encountered in various diseases. Supplementation of CST-knockout mice with recombinant CST restored paracellular permeability and reversed inflammation, whereas CgA-knockout mice supplementation with CST and/or PST in CgA-KO mice showed that intestinal paracellular permeability is regulated by the antagonistic roles of these two peptides: CST reduces and PST increases permeability. ConclusionThe pro-hormone CgA regulates the intestinal paracellular permeability. CST is both necessary and sufficient to reduce permeability and primarily acts via antagonizing the effects of PST.

physiology↗