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Poempner, N.

Publications and source records attributed to Poempner, N..

5 recordsLinked to original sources

A Multicenter Confirmatory Randomized-Controlled Study of rhNRGβ1 Protein Replacement Therapy in a Murine Model of NF2-related Schwannomatosis

BackgroundPrevious exploratory studies identified recombinant human Neuregulin-1 {beta} (rhNRG{beta}1) as a promising therapeutic strategy for inhibiting the growth of Nf2-deficient schwannomas by promoting cellular differentiation. Because robust confirmation across independent laboratories is essential for advancing promising preclinical findings toward clinical translation, we conducted a multicenter, randomized, controlled confirmatory study under stringent preclinical standards. MethodsIn a pre-registered trial (DOI: 10.17590/asr.0000304), 216 mice (Nf2-flox;P0-Cre;Nefh- Cre) were randomized at three independent research sites. Following a standardized sciatic nerve crush, mice received systemic rhNRG{beta}1 (10 {micro}g/kg) or vehicle for 13 weeks. Rigorous quality measures included double-blinding, standardized surgery, centralized data management, and an automated Fiji macro for objective nerve thickness quantification (Primary Outcome). Secondary molecular outcomes included Western blot and in-depth, quantitative proteomics and phosphoproteomics. All methods were SOP-based for reproducible and comparable results across the three study centers ResultsThe primary confirmatory analysis revealed no reduction in nerve thickness in the rhNRG{beta}1 group (pbest case imputation = 0.076 and pworst case imputation = 0.533). Secondary analyses via quantitative Western blotting and DIA proteomics demonstrated that core biochemical markers of Schwann cell differentiation (MBP, ERBB2) remained unchanged across all centers. Based on the absence of macroscopic or primary biochemical effects, further histological analysis was omitted to avoid scientific redundancy. High-depth profiling of a predefined 60-protein functional marker panel confirmed a remarkably stable tumor proteome across all replication sites and both sexes, with no evidence of coordinated changes in key downstream oncogenic signaling pathways (Hippo/YAP, mTORC1, and RTK-Ras-MAPK) or metabolic signaling cascades. These findings indicate an absence of measurable target engagement under our tested dosing regimen, potentially reflecting pharmacokinetic or tissue-delivery limitations rather than an invalidation of the underlying biological pathway. ConclusionDespite high statistical power and rigorous methodology, this study could not confirm rhNRG{beta}1 as a robust therapeutic candidate for schwannoma growth arrest or shrinkage. These findings suggest that previously reported therapeutic effects were either highly context- dependent or could not be reproduced under adequately powered, rigorously controlled experimental conditions. As underpowered preclinical studies are more susceptible to random biological variation, our results highlight the importance of sufficient sample sizes alongside robust experimental design. Our study underscores the value of trial-like methodological standards in preclinical therapeutic evaluation to identify ineffective interventions (dead ends) early and strengthen translational decision-making. Although we could not confirm the previously reported efficacy of rhNRG{beta}1, the multicenter framework established here provides a methodological benchmark for robust preclinical testing in translational oncology, with the potential to improve reproducibility and the success of therapies progressing to early-phase clinical trials. From a translational perspective, these findings provide a robust foundation for optimizing future rhNRG{beta}1-based therapeutic approaches through improved dosing, delivery routes, and treatment schedules.

cancer biology↗

Acetylation-dependent remodeling of the secretory pathway shapes the senescence-associated secretome

Cellular senescence is characterized by stable cell cycle arrest and the senescence-associated secretory phenotype (SASP), which drives tissue remodeling and inflammation. Underlying SASP with its increased secretion of cytokines and other secreted proteins is a massive reorganization of the secretory pathway. While transcriptional regulation of senescence has been extensively studied, the contribution of post-translational modifications (PTM) to secretory pathway regulation remains poorly understood. Here, we combined quantitative proteomics with multi-layered PTM profiling of phosphorylation, ubiquitination and acetylation to investigate how intracellular trafficking and secretion are regulated in senescence. Using doxorubicin-induced senescence as the primary model, we identified extensive proteome remodeling, with pronounced changes in ER-Golgi-associated pathways and secretory machinery. Acetylation emerged as the most prominently regulated PTM, particularly affecting proteins involved in vesicle trafficking and ER proteostasis. Comparable proteome and PTM remodeling were also observed in replicative senescence, indicating that these changes are not restricted to a single senescence model. Functional analyses revealed activation signatures of the acetyltransferases p300/CBP, linking global acetylation changes to enzymatic activity. Pharmacological inhibition of p300/CBP using A485 selectively modulated senescence-associated features without reversing growth arrest, consistent with a senomorphic-like effect during senescence establishment. Secretome profiling further demonstrated changes in the composition of secreted factors, consistent with modulation of the senescence-associated secretory phenotype. Together, these findings indicate that acetylation-dependent regulation of the secretory pathway shapes the senescence-associated secretome, revealing a mechanistic link between post-translational regulation, intracellular trafficking, and extracellular signaling in senescence.

Cell Biology↗

Transient protein phosphorylation promotes disease tolerance to sepsis

One of the enduring paradoxes of sepsis is that organs fail despite little evidence of irreversible tissue injury. Emerging evidence suggests that this state reflects a regulated metabolic shutdown within host tissues, yet whether such hypometabolism contributes to pathology or promotes survival remains unclear. This phenomenon resembles torpor, a physiological state of profound hypometabolism induced by environmental stress and mediated through reversible protein phosphorylation. Septic hypometabolism is identified here as a conserved tissue-specific metabolic adaptation which is characterized by transient activation of Glycogen Synthase Kinase (GSK)3{beta}. This activation reduced disease severity of bacterial sepsis without affecting the hosts pathogen burden, indicating that GSK3{beta} activity promotes disease tolerance to infection. Consistent with these findings, plasma signatures associated with GSK3{beta} inhibition correlated with worse clinical outcomes in patients with sepsis. Together, these results define septic hypometabolism as a torpor-like response and identify reversible phosphorylation as a key mechanism governing host adaptation to severe bacterial infection.

immunology↗

Aging reprograms the response to chronic stress

Chronic stress is thought to accelerate brain aging. We find this to be true in the brains of young mice, but reversed in the old. Using chronic variable stress in young (2-month) and aged (24-month) mice, we show that aged animals perceive stress physiologically but exhibit stress-responses that differ from those of young mice on behavioral, synaptic, and molecular levels. Multi-Omics profiling of prefrontal cortex and nucleus accumbens and 3D vasculature measurements reveals that stress in aged mice activates angiogenic programs that oppose aging-related patterns. Our results demonstrate that stress cannot be universally conceptualized as an aging accelerator, but instead engages age-specific programs with opposite directionality in young and old animals.

neuroscience↗

Automated workflow for BioID improves reproducibility and identification of protein-protein interactions

Proximity dependent biotinylation is an important method to study protein-protein interactions in cells, for which an expanding number of applications has been proposed. The laborious and time consuming sample processing has limited project sizes so far. Here, we introduce an automated workflow on a liquid handler to process up to 96 samples at a time. The automation does not only allow higher sample numbers to be processed in parallel, but also improves reproducibility and lowers the minimal sample input. Furthermore, we combined automated sample processing with shorter liquid chromatography gradients and data-independent acquisition to increase analysis throughput and enable reproducible protein quantitation across a large number of samples. We successfully applied this workflow to optimise the detection of proteasome substrates by proximity-dependent labelling.

biochemistry↗