Core Insights - Stroke is the second leading cause of death globally and a major factor in long-term disability, with its rising incidence closely linked to population aging [3] - Post-Stroke Emotional Disorder (PSED) significantly impacts patient recovery and quality of life, increasing the risk of stroke recurrence and mortality [3] Research Findings - A study published in the journal Neuron identified the role of Lcn2 from neutrophil extracellular traps (NETs) in the development of PSED, highlighting the interaction between the peripheral immune system and the central nervous system [4] - The research indicates that NETs in serum are a significant feature of PSED, controlled by the permeability of the blood-brain barrier (BBB) [6][7] - The study suggests that the release of Lcn2 protein from NETs promotes the proliferation of astrocytes, which is a core mechanism of PSED [6][7] - Transcranial direct current stimulation (tDCS) can alleviate PSED by reducing the release of Lcn2 [6][7] Implications - The findings illustrate a unique peripheral-central immune interaction pattern following BBB damage, emphasizing the potential of non-invasive stimulation in reshaping the neuroimmune environment [9]

Core Insights - The article discusses the critical role of thyroid hormone transport to the brain for normal neural development, mediated by the transport proteins MCT8 and OATP1C1 [2][3]. Group 1: Research Findings - A recent study published in the journal Cell by researchers from Baylor College of Medicine and the National Institutes of Health provides structural insights into the transport mechanisms of thyroid hormones via MCT8 and OATP1C1 [4][5]. - The study utilized cryo-electron microscopy to analyze the structures of MCT8 and OATP1C1 in complex with active thyroid hormones T3 and its precursor T4, achieving resolutions of 2.9 Å and 2.3 Å respectively [7]. - Key findings include the high transport specificity of MCT8 for thyroid hormones, the selective transport mechanism of OATP1C1 for thyroxine, and the discovery of a conserved extracellular regulatory site in OATP1C1 that can be allosterically inhibited by E1G [9][11].