The cholesteryl ester transfer protein (CETP) raises cholesterol levels in the brain.

The cholesteryl ester transfer protein (CETP) is a lipid transfer protein responsible for the exchange of cholesteryl esters and triglycerides between lipoproteins. Decreased CETP activity is associated with longevity, cardiovascular health, and maintenance of good cognitive performance. Interestingly, mice lack the CETP-encoding gene and have very low levels of LDL particles compared with humans.

Embedded in the Membrane: How Lipids Confer Activity and Specificity to Intramembrane Proteases.

Proteases, sharp yet unforgivable tools of every cell, require tight regulation to ensure specific non-aberrant cleavages. The relatively recent discovered class of intramembrane proteases has gained increasing interest due to their involvement in important signaling pathways linking them to diseases including Alzheimer's disease and cancer. Despite tremendous efforts, their regulatory mechanisms have only started to unravel.

Alternative Processing of the Amyloid Precursor Protein Family by Rhomboid Protease RHBDL4.

The amyloid precursor protein (APP) is an ubiquitously expressed cell surface protein and a key molecule in the etiology of Alzheimer disease. Amyloidogenic processing of APP through secretases leads to the generation of toxic amyloid β (Aβ) peptides, which are regarded as the molecular cause of the disease. We report here an alternative processing pathway of APP through the mammalian intramembrane rhomboid protease RHBDL4.

Impact of amyloid precursor protein hydrophilic transmembrane residues on amyloid-beta generation.

Amyloid-β (Aβ) peptides are likely the molecular cause of neurodegeneration observed in Alzheimer's disease. In the brain, Aβ42 and Aβ40 are toxic and the most important proteolytic fragments generated through sequential processing of the amyloid precursor protein (APP) by β- and γ-secretases. Impeding the generation of Aβ42 and Aβ40 is thus considered as a promising strategy to prevent Alzheimer's disease.