{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTSPO is an 18‐kDa protein highly conserved across species and localized primarily in the outer mitochondrial membrane, where it binds cholesterol and various drugs. In this capacity, TSPO is intimately involved in a range of fundamental cellular processes—including cholesterol import, steroidogenesis, regulation of mitochondrial bioenergetics, and the modulation of apoptotic pathways through reactive oxygen species generation. Genetic variations such as the Ala147Thr polymorphism can alter TSPO ligand‐binding affinity and influence downstream functions, including pregnenolone production and cellular responses to stress and cytotoxic agents. These molecular roles underscore TSPO’s importance not only in maintaining cellular metabolic homeostasis but also in mediating cellular sensitivity to pharmacological interventions and apoptotic signals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its core bioenergetic and steroidogenic functions, TSPO has been exploited as an in vivo marker of neuroinflammation because its expression generally increases in activated microglia and, in many cases, astrocytes following central nervous system injury or inflammatory challenge. Accordingly, TSPO‐targeted radioligands have been widely applied in positron emission tomography (PET) studies to monitor neuroinflammatory states in disorders such as depression, schizophrenia, multiple sclerosis, epilepsy and prodromal psychosis. However, the interpretation of TSPO PET signals is complicated by significant interindividual variability arising from codominant genetic polymorphisms—which affect ligand binding affinity—and by the fact that TSPO is not exclusively expressed in activated microglia. As such, quantitative PET studies must account for these genetic and cellular differences to accurately reflect underlying neuroinflammatory processes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its utility in central nervous system imaging, altered TSPO expression is observed in a variety of peripheral pathologies. Elevated TSPO levels have been associated with aggressive tumor phenotypes in cancers such as breast, colorectal, and prostate carcinomas, whereas aberrant TSPO expression is also noted in retinal inflammation, atherosclerotic plaques and other neurodegenerative as well as metabolic disorders. Moreover, TSPO expression in diseased tissues often reflects contributions from multiple cell types—including activated microglia, astrocytes, endothelial cells and vascular smooth muscle cells—with binding characteristics that vary according to cell phenotype and disease state. This diversity in TSPO’s cellular expression and ligand‐binding patterns reinforces its role as both a diagnostic biomarker and a potential therapeutic target, while also highlighting important species‐ and context‐specific differences that must be considered when designing and interpreting TSPO‐targeted interventions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "19", "end_ref": "46"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Amani Batarseh, Vassilios Papadopoulos "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of translocator protein 18 kDa (TSPO) expression in health and disease states."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Endocrinol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.mce.2010.06.013"}], "href": "https://doi.org/10.1016/j.mce.2010.06.013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20600583"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20600583"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Leo Veenman, Yulia Shandalov, Moshe Gavish "}, {"type": "b", "children": [{"type": "t", "text": "VDAC activation by the 18 kDa translocator protein (TSPO), implications for apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Bioenerg Biomembr (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10863-008-9142-1"}], "href": "https://doi.org/10.1007/s10863-008-9142-1"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18670869"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18670869"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Fei Li, Jian Liu, Nan Liu, et al. 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