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Identification of Neutral Cholesterol Ester Hydrolase, a Key Enzyme Removing Cholesterol from Macrophages*
It is shown that the murine orthologue of KIAA1363, designated as neutral cholesterol ester hydrolase (NCEH), is a microsomal nCEH with high expression in murine and human macrophages.
Ablation of neutral cholesterol ester hydrolase 1 accelerates atherosclerosis.
The Critical Role of Neutral Cholesterol Ester Hydrolase 1 in Cholesterol Removal From Human Macrophages
NCEH1 is expressed in human atheromatous lesions, where it plays a critical role in the hydrolysis of CE in human macrophage foam cells, thereby contributing to the initial part of reverse cholesterol transport in human atherosclerosis.
Targeting of neutral cholesterol ester hydrolase to the endoplasmic reticulum via its N-terminal sequence[S]
NCEH is targeted to the ER of macrophages, where it hydrolyzes CE to deliver cholesterol for efflux out of the cells.
Five amino acid residues in cysteine-rich domain of human T1R3 were involved in the response for sweet-tasting protein, thaumatin.
Critical molecular regions for elicitation of the sweetness of the sweet‐tasting protein, thaumatin I
The threshold value for sweetness was higher for R82K than for thaumatin I, indicating that not only the positive charge but also the structure of the side chain of the arginine residue at position 82 influences the sweetness of thaumarin, whereas only thepositive charge of the K67 side chain affects sweetness.
Contribution of L-Type Ca2+ Channels to Early Afterdepolarizations Induced by IKr and IKs Channel Suppression in Guinea Pig Ventricular Myocytes
- M. Yamada, Keisuke Ohta, Atsunori Niwa, N. Tsujino, Tsutomu Nakada, M. Hirose
- BiologyJournal of Membrane Biology
- 20 June 2008
An essential mechanism underlying EADs caused by suppression of the delayed rectifier IKr and/or IKs channels is the failure to completely deactivate ICa,L channels.
High-yield Secretion of the Recombinant Sweet-Tasting Protein Thaumatin I
Large amounts of homogeneous recombinant thaumatin allowed for preparation of high-quality crystals in the presence of cryoprotective glycerol used in high-resolution x-ray structural analysis to help further understand the perception of the sweet taste of thaumarin.
The cysteine-rich domain of human T1R3 is necessary for the interaction between human T1R2-T1R3 sweet receptors and a sweet-tasting protein, thaumatin.
A Hypersweet Protein: Removal of The Specific Negative Charge at Asp21 Enhances Thaumatin Sweetness
The complex model between the T1R2-T1R3 sweet receptor and thaumatin, derived from tethered docking in the framework of the wedge model, confirmed that each of the positively charged residues critical for sweetness is close to a receptor residue of opposite charge to yield optimal electrostatic interaction.