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Dr. Mary Blair Bowers is recognized as a pioneer in biological electron microscopy, contributing significantly to the study of cell cytoskeleton and motility. She played a crucial role in advancing specimen preparation techniques for studying biological samples under an electron beam. Dr. Bowers' career spanned from her early work at Harvard University to her groundbreaking research at the National Heart Institute of NIH, focusing on cell structure and function relationships. Her dedication to microscopy education and service to various scientific organizations, including the Microscopy Society of America, highlights her lasting impact on the field. [Extracted from the article]

Akkermansia muciniphila is a bacterium commonly found in the human gastrointestinal tract that has received considerable interest as a potential probiotic for the improvement of gut health and overall metabolic function. A. muciniphila is enriched in the mucus layer of the intestinal lining, where it degrades mucin and plays a significant role in gut barrier maintenance and immune regulation. A higher abundance of A. muciniphila has been observed in the gut of healthy individuals relative to those with metabolic disorders, and multiple metabolic benefits, including improved glucose management, reduced body fat, and reduced inflammation have been linked to A. muciniphila . Current research on A. muciniphila primarily relies on mouse models, with limited human interventional studies available. While these animal studies offer valuable insights into the potential roles of A. muciniphila in health and disease, further clinical investigations in humans are needed to fully understand its impact. Here, we explore the current scope of A. muciniphila research and its potential as a therapeutic agent to improve gut and metabolic health while also emphasizing the need to optimize techniques to further improve studies of this organism.

Loss of proteostasis is a hallmark of aging and Alzheimer disease (AD). We identify β-hydroxybutyrate (βHB), a ketone body, as a regulator of protein solubility. βHB primarily provides ATP substrate during periods of reduced glucose availability, and regulates other cellular processes through protein interactions. We demonstrate βHB-induced protein insolubility is not dependent on covalent protein modification, pH, or solute load, and is observable in mouse brain in vivo after delivery of a ketone ester. This mechanism is selective for pathological proteins such as amyloid-β, and exogenous βHB ameliorates pathology in nematode models of amyloid-β aggregation toxicity. We generate libraries of the βHB-induced protein insolublome using mass spectrometry proteomics, and identify common protein domains and upstream regulators. We show enrichment of neurodegeneration-related proteins among βHB targets and the clearance of these targets from mouse brain. These data indicate a metabolically regulated mechanism of proteostasis relevant to aging and AD., Competing Interests: Declaration of interests J.C.N. and E.V. hold patents related to molecules described herein, licensed to BHB Therapeutics Ltd and Selah Therapeutics Ltd. J.C.N. and E.V. are co-founders with stock holdings, and BJS holds stock options, in BHB Therapeutics. J.C.N., E.V., and B.S. are co-founders with stock holdings in Selah Therapeutics., (Copyright © 2024 The Authors. Published by Elsevier Ltd.. All rights reserved.)

Quantum dots (QDs) are semiconducting inorganic nanocrystals, that have garnered interest in biological and medical spheres due, to their potential benefits in biomedical imaging and drug-delivery systems. Indium phosphide QDs shelled with zinc sulphide (InP/ZnS) are viewed as more biocompatible than previous heavy metal based QDs. However, little is known about how InP/ZnS QDs affect a key blood cell, the platelet. Understanding how platelets interact with QDs is critical as unwanted activation can lead to pathological thrombus formation. Herein, we demonstrate PEGylation of InP/ZnS QDs coated with lipoic acid (QD-LA) or coated with penicillamine (QD-Pen) surface ligands induced markedly less platelet aggregation, platelet-QD interactions, integrin activation, alpha granule secretion and restored platelet spreading in washed platelets in comparison to their non-PEGylated counterparts. Furthermore, in whole blood, PEGylation of QDs reduced the number of QDs in the thrombus, thereby helping to minimise the chance of dysfunctional thrombus formation. Overall, we show that QD PEGylation is important to help prevent QD mediated platelet activation. In combination with the most biocompatible coating, PEGylation markedly reduced platelet activation, widening the concentrations at which QDs were viable for development as potential drug delivery or imaging agents.