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Sepsis-associated encephalopathy (SAE) is a severe neurological syndrome marked by widespread brain dysfunctions due to sepsis, yet the underlying mechanisms remain elusive. The current study, using a Lipopolysaccharide (LPS)-induced septic rat model, revealed the hyperphosphorylation of tau and cognitive impairments, accompanied by the release of inflammatory cytokines and activation of glial cells in the hippocampal dentate gyrus region of septic rats. Proteomic and bioinformatic analyses identified C-X-C motif chemokine ligand 10(CXCL10) as a central regulator of neuroinflammation. LPS triggered CXCL10 secretion in astrocytes, and astrocyte-conditioned medium from LPS-treated astrocytes induced tau hyperphosphorylation and synaptic deficits. Recombinant CXCL10 recapitulated these effects in vitro and in vivo. Blocking CXCL10-CXCR3 interaction reversed tau phosphorylation, synaptic impairment, and cognitive decline. Mechanistically, CXCL10-CXCR3 interaction activated CaMKII, driving tau hyperphosphorylation, while CaMKII inhibition restored synaptic protein levels. These findings establish CXCL10 as a key driver of tau pathology in SAE and suggest CXCL10-CXCR3 as a therapeutic target for sepsis-induced cognitive impairments.
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http://dx.doi.org/10.1007/s12264-025-01445-w | DOI Listing |
J Integr Neurosci
August 2025
CIBA Center for Advanced Biomedical Research, School of Medicine, Autonomous University of Queretaro, 76010 Querétaro, México.
Background: Neurofibrillary tangles, composed of hyperphosphorylated tau, have been implicated in the cognitive impairments observed in Alzheimer's disease. While the precise mechanism remains elusive, cognitive deficits in Alzheimer's disease have been associated with disrupted brain network activity. To investigate this mechanism, researchers have developed several tau transgenic models.
View Article and Find Full Text PDFFront Pharmacol
August 2025
Department of Physiology, Dongguk University College of Korean Medicine, Gyeongju, Republic of Korea.
Introduction: The development of new drugs for Alzheimer's disease (AD) remains a major challenge due to the disorder's complex and multifactorial nature. 2'-Fucosyllactose (2'-FL), a human milk oligosaccharide, has demonstrated promising neuroprotective properties. However, its effects on AD-related cognitive decline are not yet fully understood.
View Article and Find Full Text PDFTurk J Biol
June 2025
Department of Biochemistry, School of Pharmacy, Hacettepe University, Ankara, Turkiye.
Background/aim: Tau protein, which is crucial for sustaining the cytoskeletal network by assisting microtubule construction, contributes significantly to the pathophysiology of Alzheimer's disease (AD). The hyperphosphorylation of tau causes it to detach from microtubules (MTs), leading to the formation of neurofibrillary tangles (NFTs) in neurons, which ultimately results in cell death. Thionine (TH), a cationic phenothiazine-structured compound, has been the topic of extensive research due to its interesting physicochemical properties.
View Article and Find Full Text PDFCurr Alzheimer Res
September 2025
Department of Biochemistry, General Medicine Practice Program, Batterjee Medical College, Jeddah, Saudi Arabia.
A serine/threonine kinase with a wide variety of substrates, Glycogen Synthase Kinase-3 (GSK-3) is widely expressed. GSK-3 is a key player in cell metabolism and signaling, modulating numerous cellular functions and playing significant roles in both healthy and diseased states. The two histopathological features of Alzheimer's disease, the intracellular neurofibrillary tangles composed of hyperphosphorylated tau, and the extracellular senile plaques composed of beta-amyloid, have been linked to GSK-3.
View Article and Find Full Text PDFNeuropeptides
September 2025
Department of Physiology and Cell Biology, The National Institute for Biotechnology in the Negev, and the School of Brain Sciences and Cognition, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Despite extensive research into Alzheimer's disease (AD), few therapeutic strategies have successfully addressed its core pathology at the synaptic level. Small peptides represent a promising class of therapeutic agents capable of modulating key molecular pathways involved in amyloid toxicity, tau hyperphosphorylation, and synaptic degeneration. Their unique ability to cross biological barriers, interact with intracellular targets, and be modified for enhanced stability positions them as viable candidates for next-generation treatments targeting cognitive decline in AD.
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