Gelsolin, an actin-depolymerizing protein expressed both in extracellular fluids and in the cytoplasm of a majority of human cells, has been recently implicated in a variety of both physiological and pathological processes. Its extracellular isoform, called plasma gelsolin (pGSN), is present in blood, cerebrospinal fluid, milk, urine, and other extracellular fluids. This isoform has been recognized as a potential biomarker of inflammatory-associated medical conditions, allowing for the prediction of illness severity, recovery, efficacy of treatment, and clinical outcome. A compelling number of animal studies also demonstrate a broad spectrum of beneficial effects mediated by gelsolin, suggesting therapeutic utility for extracellular recombinant gelsolin. In the review, we summarize the current data related to the potential of pGSN as an inflammatory predictor and therapeutic target, discuss gelsolin-mediated mechanisms of action, and highlight recent progress in the clinical use of pGSN.
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http://dx.doi.org/10.3390/ijms19092516 | DOI Listing |
Int J Mol Sci
November 2024
Department of Emergency Medicine, School of Medicine, University of Maryland, Baltimore, MD 21250, USA.
Physiol Rep
November 2024
Department of Emergency Medicine, University of Maryland School of Medicine, Baltimore, Maryland, USA.
J Neurophysiol
December 2024
Department of Emergency Medicine, University of Maryland School of Medicine, Baltimore, Maryland, United States.
Newborn (Clarksville)
March 2024
Global Newborn Society, Clarksville Maryland, United States of America.
Talanta
January 2025
State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, 130022, China; School of Applied Chemistry and Engineering, University of Science and Technology of China, Hefei, 230026, China. Electronic address:
Biomolecular interaction acts a pivotal part in understanding the mechanisms underlying the development of Alzheimer's disease (AD). Herein, we built a biosensing platform to explore the interaction between gelsolin (GSN) and different β-amyloid protein 1-42 (Aβ) species, including Aβ monomer (m-Aβ), Aβ oligomers with both low and high levels of aggregation (LLo-Aβ and HLo-Aβ) via dual polarization interferometry (DPI). Real-time molecular interaction process and kinetic analysis showed that m-Aβ had the strongest affinity and specificity with GSN compared with LLo-Aβ and HLo-Aβ.
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