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Translocator protein (18kDa): new nomenclature for the peripheral-type benzodiazepine receptor based on its structure and molecular function.
TLDR
Translocator protein (18kDa) is proposed as a new name, regardless of the subcellular localization of the protein, to represent more accurately its sub cellular role (or roles) and putative tissue-specific function (or functions). Expand
Translocator protein (18 kDa) (TSPO) as a therapeutic target for neurological and psychiatric disorders
TLDR
The translocator protein (18 kDa) (TSPO) is localized primarily in the outer mitochondrial membrane of steroid-synthesizing cells, including those in the central and peripheral nervous system, which is a prerequisite for steroid synthesis. Expand
In search of rat stem Leydig cells: identification, isolation, and lineage-specific development.
TLDR
It is concluded that cells in the neonatal rat testis with the abilities to proliferate and expand indefinitely in vitro (self renew) and differentiate when transplanted into host rat testes, colonize the interstitium and subsequently differentiate in vivo are likely to be the sought-after SLCs. Expand
Peripheral-type benzodiazepine receptor function in cholesterol transport. Identification of a putative cholesterol recognition/interaction amino acid sequence and consensus pattern.
TLDR
Exercise of PBR in Escherichia coli DE3 cells induced the ability to take up cholesterol in a time-dependent, temperature-sensitive, and energy-independent manner, and site-directed mutagenesis in the carboxy-terminal region demonstrated that bacteria expressing the mutant PBR proteins do not accumulate cholesterol, suggesting that amino acids Y153 and R156 are involved in the interaction of the receptor with cholesterol. Expand
Peripheral benzodiazepine receptor in cholesterol transport and steroidogenesis
TLDR
PBR is an indispensable element of the steroidogenic machinery and its presence is vital for hCG-induced steroidogenesis by Leydig cells. Expand
NMDA Receptor-Nitric Oxide Transmission Mediates Neuronal Iron Homeostasis via the GTPase Dexras1
TLDR
A signaling cascade in neurons whereby stimulation of NMDA receptors activates nNOS, leading to S-nitrosylation and activation of Dexras1, which, via PAP7 and DMT1, physiologically induces iron uptake and appears to mediate NMDA neurotoxicity. Expand
Peripheral-type benzodiazepine receptor (PBR) in human breast cancer: correlation of breast cancer cell aggressive phenotype with PBR expression, nuclear localization, and PBR-mediated cell
TLDR
Examination of expression, characteristics, localization, and function of PBR in a battery of human breast cancer cell lines differing in their invasive and chemotactic potential as well as in several human tissue biopsies suggest that PBR expression, nuclear localization,and PBR-mediated cholesterol transport into the nucleus are involved in human breast cancers cell proliferation and aggressive phenotype expression, thus participating in the advancement of the disease. Expand
Identification of a dynamic mitochondrial protein complex driving cholesterol import, trafficking, and metabolism to steroid hormones.
TLDR
A bioactive, multimeric protein complex spanning the OMM and IMM unit that is responsible for the hormone-induced import, segregation, targeting, and metabolism of cholesterol is identified. Expand
Steroid production in the thymus: implications for thymocyte selection
TLDR
Data indicate that locally produced glucocorticoids, because of their antagonism of TCR-mediated signaling for death, may be a key element of antigen-specific thymocyte selection. Expand
Cholesterol binding at the cholesterol recognition/ interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide.
TLDR
Results show that TAT-CRAC binds cholesterol and competes for cholesterol interaction with endogenous PBR, suggesting that the cytosolic carboxyl-terminal domain of PBR is responsible for taking up and bringing steroidogenic cholesterol into the mitochondria. Expand
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