Publications by authors named "Annemarie Aue"

Article Synopsis
  • Plexus injuries lead to chronic issues like paralysis, sensory loss, and pain, prompting interest in how the dorsal root ganglia (DRG) are affected following such injuries.
  • A study involving 13 patients revealed that in about half, the typical cell structure of DRG was lost replaced by connective tissue, while others maintained their cellular integrity, although those with preserved neurons reported less pain.
  • The findings suggest two distinct patient groups: those with neuronal preservation who might benefit from anti-inflammatory treatments, and those with neuronal loss needing further research for potential regenerative therapies.
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Pulmonary fibrosis is a chronic and progressive disease with limited therapeutic options. Nitric oxide (NO) is suggested to reduce the progression of pulmonary fibrosis via NO-sensitive guanylyl cyclase (NO-GC). The exact effects of NO-GC during pulmonary fibrosis are still elusive.

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Background: The origin of αSMA-positive myofibroblasts, key players within organ fibrosis, is still not fully elucidated. Pericytes have been discussed as myofibroblast progenitors in several organs including the lung.

Methods: Using tamoxifen-inducible PDGFRβ-tdTomato mice (PDGFRβ-CreER; R26tdTomato) lineage of lung pericytes was traced.

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Pain syndromes are often accompanied by complex molecular and cellular changes in dorsal root ganglia (DRG). However, the evaluation of cellular plasticity in the DRG is often performed by heuristic manual analysis of a small number of representative microscopy image fields. In this study, we introduce a deep learning-based strategy for objective and unbiased analysis of neurons and satellite glial cells (SGCs) in the DRG.

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Phosphodiesterase 3 (PDE3) exists in two isoforms (PDE3A and PDE3B) and is known to act as cGMP-inhibited cAMP-degrading PDE. Therefore, PDE3 may likely be involved in the interaction between the two second messenger pathways. NO-sensitive guanylyl cyclase (NO-GC) is the most important cytosolic generator of cGMP.

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Merkel cell polyomavirus (MCPyV) is regarded as a major causal factor for Merkel cell carcinoma (MCC). Indeed, tumor cell growth of MCPyV-positive MCC cells is dependent on the expression of a truncated viral Large T antigen (LT) with an intact retinoblastoma protein (RB)-binding site. Here we determined the phosphorylation pattern of a truncated MCPyV-LT characteristically for MCC by mass spectrometry revealing MCPyV-LT as multi-phospho-protein phosphorylated at several serine and threonine residues.

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Article Synopsis
  • Merkel cell carcinoma (MCC) cell growth relies on the MCPyV Large T antigen (LT), specifically the intact retinoblastoma protein (RB)-binding site, unlike other polyomaviruses.
  • * Nuclear localization is crucial for LT function, but a specific nuclear localization sequence is not necessary for either LT's nuclear accumulation or MCC cell proliferation.
  • * Key regions of the MCPyV, beyond the RB-binding domain, are largely unnecessary for tumor cell growth, but the MUR1 region may stabilize LT expression in MCC cells, while HSC-70 interaction plays a significant role in LT function.
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