Hua Li

TL;DR: 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.

TL;DR: PBR is an indispensable element of the steroidogenic machinery and its presence is vital for hCG-induced steroidogenesis by Leydig cells.

TL;DR: 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.

TL;DR: 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.

TL;DR: Data demonstrate that PBR is an indispensable element of the steroidogenic machinery, where it mediates the delivery of the substrate cholesterol to the inner mitochondrial side chain cleavage cytochrome P-450.