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Eijkelkamp, N.

Publications and source records attributed to Eijkelkamp, N..

5 recordsLinked to original sources

The amyloid oligomer modulator anle138b has disease modifying effects in a human IAPP transgenic mouse model of type 2 diabetes mellitus (hIAPP Ob/Ob mice)

Aims/HypothesisType 2 diabetes mellitus (T2DM) is a common metabolic disease, characterized by impaired insulin action, often called "insulin resistance", in conjunction with a decline in insulin secretion by the pancreatic islet beta cells, referred to as "beta cell failure". Both conditions contribute to causing hyperglycemia, which is the central feature of T2DM. Cytotoxic aggregates of the beta cell hormone human islet amyloid polypeptide (hIAPP), promote T2DM pathogenesis by damaging the pancreatic islet beta cells and reducing insulin secretion. Anle138b is an amyloid oligomer modulator with demonstrated disease-modifying properties in mouse models of neurodegenerative diseases linked to protein aggregation, and is currently in a phase 2 clinical trial. We therefore tested whether anle138b can reduce hyperglycemia in a severe hIAPP transgenic mouse model of T2DM. MethodsAnle138b was administered orally via dietary admixture to male hIAPP Ob/Ob mice and Ob/Ob controls; blood glucose-, insulin-, and glycated hemoglobin (HbA1c) levels were measured at different timepoints over 34 weeks; in addition, the effects of anle138b on the histomorphology of the pancreatic islets was determined. Finally, anle138b effects on mitochondrial toxicity of hIAPP aggregates was assessed in vitro. ResultsOral administration of anle138b in male hIAPP Ob/Ob mice potently reduced hyperglycemia and glycated HbA1c levels compared to non-treated mice (at 34 weeks, mean glucose level non-treated: 30 {+/-} 1.3 mM, treated: 15 {+/-} 2.2 mM (p < 0.001); at 32 weeks, mean HbA1c level non-treated: 77 {+/-} 3.3 mM/M, treated: 41 {+/-} 5.3 mM/M (p < 0.01)), in a hIAPP-dependent way. In addition, anle138b increased both the number of pancreatic islets as well as the overall islet beta cell mass (by 54% and 58%, respectively) in hIAPP Ob/Ob mice. In vitro, anle138b inhibited toxic effects of hIAPP on mitochondria, such as mitochondrial swelling (decreased by 92%, p < 0.01), release of cytochrome c (decreased by 63.7%, p < 0.001) and lowered mitochondrial membrane potential (increased by 62%, p < 0.001). Conclusions/InterpretationCollectively, our results indicate that anle138b is a promising clinical drug candidate for preserving islet function and reducing hyperglycemia in T2DM, in part by mitigating mitochondrial dysfunction. Research in ContextO_ST_ABSWhat is already known about this subject?C_ST_ABSO_LIType 2 diabetes mellitus (T2DM) is characterized by hyperglycemia, which stems from impaired insulin action coupled with declining insulin secretion from pancreatic islet beta cells. C_LIO_LIAggregation of the beta cell hormone human islet amyloid polypeptide (hIAPP) plays a crucial role in the loss and dysfunction of the insulin-secreting beta cells. C_LIO_LIThe small-molecule anle138b effectively modulates the aggregation of amyloidogenic proteins in neurodegenerative conditions such as Alzheimers and Parkinsons disease. C_LI What is the key question?O_LICan the oligomer modulator anle138b ameliorate the diabetic phenotype in a severe hIAPP transgenic mouse model of T2DM (hIAPP Ob/Ob) ? C_LIO_LIWhat are the new findings? C_LIO_LIOral treatment of hIAPP Ob/Ob mice with anle138b causes reduced hyperglycemia and reduced glycated hemoglobin (HbA1c) levels, in a hIAPP-dependent manner. C_LIO_LIAnle138b increases pancreatic islet number and beta cell mass and restores the inverse relation between insulin and glucose in hIAPP Ob/Ob mice. C_LIO_LIIn vitro anle138b inhibits toxic effects of hIAPP aggregates on mitochondria. C_LI How might this impact on clinical practice in the foreseeable future?O_LIAnle138b could be introduced as a promising clinical drug candidate for slowing down disease progression of T2DM. C_LI

pathology↗

Transfer of IgG from Long COVID patients induces symptomology in mice

SARS-CoV-2 infections worldwide led to a surge in cases of Long COVID, a post-infectious syndrome. It has been hypothesized that autoantibodies play a crucial role in the development of Long COVID and other syndromes, such as fibromyalgia and myalgic encephalomyelitis/chronic fatigue syndrome (ME/CFS). In this study, we tested this hypothesis by passively transferring total IgG from Long COVID patients to mice. Using Glial Fibrillary Acidic Protein (GFAP) and type-I interferon expression, we stratified patients into three Long COVID subgroups, each with unique plasma proteome signatures. Remarkably, IgG transfer from the two subgroups, which are characterized by higher plasma levels of neuronal proteins and leukocyte activation markers, induced pronounced and persistent sensory hypersensitivity with distinct kinetics. Conversely, IgG transfer from the third subgroup, which are characterized by enriched skeletal and cardiac muscle proteome profiles, reduced locomotor activity in mice without affecting their motor coordination. These findings demonstrate that transfer of IgG from Long COVID patients to mice replicates disease symptoms, underscoring IgGs causative role in Long COVID pathogenesis. This work proposes a murine model that mirrors Long COVIDs pathophysiological mechanisms, which may be used as a tool for screening and developing targeted therapeutics.

immunology↗

Inflammation-induced mitochondrial and metabolic disturbances in sensory neurons control the switch from acute to chronic pain

Pain often persists in patients with inflammatory diseases, even when the inflammation has subsided. The molecular mechanisms leading to this failure in resolution of inflammatory pain and the transition to chronic pain are poorly understood. Mitochondrial dysfunction in sensory neurons has been linked to chronic pain, but its role in resolution of inflammatory pain is unclear. Transient inflammation causes neuronal plasticity, called hyperalgesic priming, which impairs resolution of hyperalgesia induced by a subsequent inflammatory stimulus. We identified that hyperalgesic priming in mice caused disturbances in mitochondrial respiration, oxidative stress, and redox balance in dorsal root ganglia (DRG) neurons. Preventing these priming-induced disturbances restored resolution of inflammatory hyperalgesia. Concurrent with these mitochondrial and metabolic changes, the expression of ATPSc-KMT, a mitochondrial methyltransferase, was increased in DRG neurons in primed mice. ATPSc-KMT overexpression in DRG neurons of naive mice induced similar mitochondrial and metabolic changes as observed after priming, leading to failure in pain resolution. Inhibition of mitochondrial respiration, knockdown of ATPSCKMT expression, or NAD+ supplementation were sufficient to restore resolution of inflammatory pain and prevent chronic pain development. Thus, inflammation-induced mitochondrial-dependent disturbances in DRG neurons promote failure in inflammatory pain resolution and drive the transition to chronic pain.

neuroscience↗

Human IAPP is a driver of painful diabetic peripheral neuropathy

Peripheral neuropathy is a frequent complication of type 2 diabetes mellitus (T2DM). We investigated whether human islet amyloid polypeptide (hIAPP), which forms pathogenic aggregates that damage pancreatic islet {beta}-cells in T2DM, is involved in T2DM-associated peripheral neuropathy. In vitro, hIAPP incubation with sensory neurons reduced neurite outgrowth and increased levels of mitochondrial reactive oxygen species. Transgenic hIAPP mice that have elevated plasma hIAPP levels without hyperglycemia developed peripheral neuropathy as evidenced by pain-associated behavior and reduced intra-epidermal nerve fiber (IENF) density. Similarly, hIAPP Ob/Ob mice that have hyperglycaemia in combination with elevated plasma hIAPP levels had signs of neuropathy, although more aggravated. In wild-type mice, intraplantar and intravenous hIAPP injections induced long-lasting allodynia and decreased IENF density. Non-aggregating murine IAPP, mutated hIAPP (Pramlintide), or hIAPP with pharmacologically inhibited aggregation did not induce these effects. T2DM patients had reduced IENF density and more hIAPP oligomers in the skin compared to non-T2DM controls. Thus, we provide evidence that hIAPP aggregation is neurotoxic and mediates peripheral neuropathy in mice. The increased abundance of hIAPP aggregates in the skin of T2DM patients supports the notion that hIAPP is a potential contributor to T2DM neuropathy in humans. Graphic abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=132 SRC="FIGDIR/small/471098v2_ufig1.gif" ALT="Figure 1"> View larger version (29K): org.highwire.dtl.DTLVardef@323953org.highwire.dtl.DTLVardef@15195feorg.highwire.dtl.DTLVardef@14e7311org.highwire.dtl.DTLVardef@16488bd_HPS_FORMAT_FIGEXP M_FIG C_FIG

neuroscience↗

Macrophages transfer mitochondria to neurons to resolve inflammatory pain

The current paradigm is that inflammatory pain passively resolves following the cessation of inflammation. Yet, in a substantial proportion of patients with inflammatory diseases, resolution of inflammation is not sufficient to resolve pain, resulting in chronic pain. Mechanistic insight how inflammatory pain is resolved is lacking. Here we show that macrophages actively control resolution of inflammatory pain remotely from the site of inflammation by transferring mitochondria to sensory neurons. During resolution of inflammatory pain in mice, M2-like macrophages infiltrate the dorsal root ganglia that contain the somata of sensory neurons, concurrent with the recovery of oxidative phosphorylation in sensory neurons. The resolution of pain and the transfer of mitochondria requires expression of CD200 Receptor (CD200R) on macrophages and the non-canonical CD200R-ligand iSec1 on sensory neurons. Our data reveal a novel mechanism for active resolution of inflammatory pain. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=172 SRC="FIGDIR/small/940445v3_ufig1.gif" ALT="Figure 1"> View larger version (36K): org.highwire.dtl.DTLVardef@1048f6org.highwire.dtl.DTLVardef@1262306org.highwire.dtl.DTLVardef@c58261org.highwire.dtl.DTLVardef@f2d4a0_HPS_FORMAT_FIGEXP M_FIG C_FIG

neuroscience↗