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Qi-Takahara Y, Morishima-Kawashima M, Tanimura Y, Dolios G, Hirotani N, Horikoshi Y, Kametani F, Maeda M, Saido TC, Wang R, Ihara Y. Longer forms of amyloid beta protein: implications for the mechanism of intramembrane cleavage by gamma-secretase. J Neurosci. 2005 Jan 12;25(2):436-45. PubMed.
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Yale University School of Medicine
Using a modified gel electrophoresis system, these investigators describe a series of longer forms of amyloid-β peptides in both transfected cells and transgenic brain tissue. These peptides include some that are 45, 46, and 48 amino acids long, which they believe are eventually processed to the usual 40 and 42 residue forms. These longer peptides are described as being either intracellular or secreted, but one has to wonder why such long hydrophobic peptides, which include almost the entire membrane-spanning segment of APP, ever leave the membrane at all. If some of these peptides do indeed remain embedded in the lipid bilayer, they could have unsuspected pathophysiological consequences.
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