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Micellar Choline-Acetyltransferase Complexes Exhibit Ultra-Boosted Catalytic Rate for Acetylcholine Synthesis-Mechanistic Insights for Development of Acetylcholine-Enhancing Micellar Nanotherapeutics.
Int J Mol Sci
December 2024
Division of Clinical Geriatrics, Centre for Alzheimer Research, Department of Neurobiology, Care Sciences and Society, Karolinska Institutet, 141 57 Stockholm, Sweden.
Choline-acetyltransferase (ChAT) is the key cholinergic enzyme responsible for the biosynthesis of acetylcholine (ACh), a crucial signaling molecule with both canonical neurotransmitter function and auto- and paracrine signaling activity in non-neuronal cells, such as lymphocytes and astroglia. Cholinergic dysfunction is linked to both neurodegenerative and inflammatory diseases. In this study, we investigated a serendipitous observation, namely that the catalytic rate of human recombinant ChAT (rhChAT) protein greatly differed in buffered solution in the presence and absence of Triton X-100 (TX100).
View Article and Find Full Text PDFPseudohelicene chemosensor displaying ternary signaling stimulated by hydrostatic pressure and solvent.
Chem Commun (Camb)
January 2025
Department of Chemistry, Institute of Science Tokyo, 2-12-1 Ookayama, Meguro-ku, Tokyo 152-8551, Japan.
Herein, we report the serendipitous discovery of a racemic chemosensor ([2]HA2) that outputs three signal patterns (1/0/-1) in response to two external stimuli (hydrostatic pressure and solvent); these signals can be observed by hydrostatic pressure spectroscopy.
View Article and Find Full Text PDFCombining multiple stressors blocks bacterial migration and growth.
Curr Biol
December 2024
Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address:
Article Synopsis
- Real-world organisms face multiple stressors simultaneously, but lab studies usually focus on single stressors in simplified conditions.
- This study uses microfluidics to apply both physical (shear flow) and chemical (hydrogen peroxide) stressors to the bacteria Pseudomonas aeruginosa, revealing that flow significantly enhances the effectiveness of HO on bacterial growth.
- The findings show that natural levels of these stressors interact in ways that limit bacterial movement and survival, emphasizing the importance of studying multiple stressors to better understand their true effects.
Allosteric modulation of the Lon protease via ssDNA binding and local charge changes.
J Biol Chem
November 2024
Department of Biochemistry and Molecular Biology, Molecular and Cellular Biology Program, University of Massachusetts, Amherst, USA. Electronic address:
The ATPase Associated with diverse cellular Activities (AAA+) family of proteases play crucial roles in cellular proteolysis and stress responses. Like other AAA + proteases, the Lon protease is known to be allosterically regulated by nucleotide and substrate binding. Although it was originally classified as a DNA binding protein, the impact of DNA binding on Lon activity is unclear.
View Article and Find Full Text PDFResponse to: Serendipitous adrenal hyperplasia in patients admitted to the emergency department is linked to increased mortality.
Arch Med Res
September 2024
Internal Medicine 1, Department of Clinical and Biological Sciences, San Luigi Gonzaga Hospital, University of Turin, Orbassano, Italy.
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