Benzodiazepines are among the most widely used therapeutic drugs because of their sedative and anxiolytic effects mediated through modulation of GABAA receptors. Another recognition site for these drugs, termed the peripheral-type (or mitochondrial) benzodiazepine receptor, is much more prevalent throughout the body for which a physiologic and pharmacologic role has just been found. This drug receptor plays a central role in the regulation of steroidogenesis by mediating the rate-limiting step in this biosynthetic pathway, which is transport of cholesterol to inner mitochondrial membranes. Although once considered by many to be an insignificant drug-binding site because a specific function remained elusive for many years, peripheral-type benzodiazepine receptors are now viewed with renewed interest because certain benzodiazepines such as diazepam may exert secondary effects on steroid production under appropriate physiologic conditions. Elucidation of this receptorial role should initiate new studies to examine in more detail the pharmacologic profile of drugs that bind to these sites and provides a novel target for the treatment of certain types of endocrine disorders.
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Prog Retin Eye Res
May 2024
Laboratory for Experimental Immunology of the Eye, Department of Ophthalmology, University of Cologne, Faculty of Medicine and University Hospital Cologne, Cologne, Germany; Centre for Molecular Medicine Cologne (CMMC), University of Cologne, Cologne, Germany. Electronic address:
Translocator protein (18 kDa) (Tspo), formerly known as peripheral benzodiazepine receptor is a highly conserved transmembrane protein primarily located in the outer mitochondrial membrane. In the central nervous system (CNS), especially in glia cells, Tspo is upregulated upon inflammation. Consequently, Tspo was used as a tool for diagnostic in vivo imaging of neuroinflammation in the brain and as a potential therapeutic target.
View Article and Find Full Text PDFBiochimie
September 2024
Department of Pharmacology and Pharmaceutical Sciences, Alfred E. Mann School of Pharmacy and Pharmaceutical Sciences, University of Southern California, Los Angeles, CA 90089, USA. Electronic address:
Translocator protein (TSPO, 18 kDa), previously known as peripheral-type benzodiazepine receptor, is an evolutionarily conserved and tryptophan-rich 169-amino-acid protein located on the outer mitochondrial membrane. TSPO plays a crucial role in various fundamental physiological functions and cellular processes. Its expression is altered in pathological conditions, thus rendering TSPO a potential tool for diagnostic imaging and an appealing therapeutic target.
View Article and Find Full Text PDFJ Med Chem
July 2021
Dipartimento di Biotecnologie, Chimica e Farmacia (Dipartimento di Eccellenza 2018-2022), Università di Siena, Via A. Moro 2, 53100 Siena, Italy.
Translocator protein 18 kDa [TSPO or peripheral-type benzodiazepine receptor (PBR)] was identified in the search of binding sites for benzodiazepine anxiolytic drugs in peripheral regions. In these areas, binding sites for TSPO ligands were recognized in steroid-producing tissues. TSPO plays an important role in many cellular functions, and its coding sequence is highly conserved across species.
View Article and Find Full Text PDFBrain Res Bull
December 2020
Operating Room, 7th Medical Center of the Chinese PLA General Hospital, Beijing, 100700, China. Electronic address:
The translocator protein (TSPO), once known as peripheral-type benzodiazepine receptor, was reported to be related with several physiological functions. Etifoxine is a clinically available anxiolytic drug, and has recently shown neuroprotective effects as a TSPO ligand. The aim of the present study was to investigate the influence of etifoxine on LPS-induced neuroinflammation and cognitive dysfunction.
View Article and Find Full Text PDFArch Insect Biochem Physiol
October 2020
College of Bioscience and Biotechnology, Shenyang Agricultural University, Shenyang, China.
In this study, glutathione-S-transferase pull-down combined with mass spectrometry techniques were used to identify the candidate proteins interacting with protein tyrosine phosphatase of the Bombyx Mori nucleopolyhedrovirus in the B. mori (BmNPV-PTP) brain. A total of 36 proteins were identified from BmNPV-PTP coprecipitate samples by searching the NCBI_Bombyx Mori database with the original mass spectrum data.
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