Niemann-Pick C1-like 1 protein (NPC1L1) is the putative intestinal sterol transporter and the molecular target of ezetimibe, a potent inhibitor of cholesterol absorption. To address the role of NPC1L1 in cholesterol trafficking in intestine, the regulation of cholesterol trafficking by ezetimibe was studied in the human intestinal cell line, CaCo-2. Ezetimibe caused only a modest decrease in th...

The potential role of liver fatty acid binding protein (L-FABP) in modulating cellular sterol distribution was examined in mouse L-cell fibroblasts transfected with cDNA encoding L-FABP. L-cells were chosen because they contain only a small amount of endogenous FABP which does not bind [3H]cholesterol, does not enhance intermembrane sterol transfer, and whose content is unaltered by the express...

We describe a continuous-flow, automated determination of total cholesterol in serum, which is based on enzymatic hydrolysis of cholesterol esters, oxidation of cholesterol by cholesterol oxidase, and colorimetric measurement of liberated perioxide with 4-aminoantipyrine, phenol, and peroxidase. Free cholesterol is determined with the same AutoAnalyzer II manifold and reagents, except that chol...

Cholesterol biosensor has been fabricated by covalently coupling cholesterol oxidase (ChOx) via glutaraldehyde onto electrochemically prepared polyaniline film in presence of TritonX-100 [4-(1,1,3,3-tetramethylbutyl) phenyl polyethylene glycol], a non-ionic surfactant onto indium-tin-oxide (ITO) glass substrate. These ChOx/PANITX-100/ITO bioelectrodes have been characterized using Fourier trans...

Cholesterol was assayed on the Greiner GSA II and the Technicon SMA 12/60 and SMA II autoanalyzers, with Allain's entirely enzymic method (Allain et al. (1974), Clin. Chem. 20, 470--475). The coefficients of variation in the results over a period of one month were less than 6% with the GSA II and the SMA II, but up to 9% on the SMA 12/60. Although the accuracy of the enzymic method depends on t...

Despite considerable research effort, the molecular mechanisms of Mycobacterium tuberculosis (Mtb) virulence remain unclear. Cholesterol oxidase (ChoD), an extracellular enzyme capable of converting cholesterol to its 3-keto-4-ene derivative, cholestenone, has been proposed to play a role in the virulence of Mtb. Here, we verified the hypothesis that ChoD is capable of modifying the bactericida...