Elongated Isoform of Aquaporin-4 Can Enhance Clearance of Amyloid- β from the Brain

Researchers here report on an interesting discovery relating to the way in which aquaporin-4 functions in clearance of molecular waste from the brain. An uncommon isoform of aquaporin-4 has a role in clearing excess amyloid-β, and possibly many other forms of molecular waste. Given that a failure of clearance of molecular waste from the brain is apparently involved in many neurodegenerative conditions, approaches that enhance clearance are promising. Increased amounts of this more effective isoform can be achieved via a variety of strategies in mice, and in mice engineered to generate excess amyloid-β, this results in a reduction of amyloid-β in the brain. This is quite interesting, but further work is required to determine a useful way to implement this shift in protein isoforms in humans. Every once in a while, the brain protein aquaporin 4 is synthesized with an extra little tail on the end. Scientists already knew that the cell's protein-building machinery occasionally fails to stop where it should. When the machinery doesn't stop - a phenomenon known as readthrough - it creates extended forms of proteins that sometimes function differently than the regular forms. "At first, we thought it couldn't possibly be relevant. But then we looked at the gene sequence, and it was conserved across species. And it had this really striking pattern in the brain: it was only in structures that are important for waste clearance. So that's when we got excited." Research...
Source: Fight Aging! - Category: Research Authors: Tags: Daily News Source Type: blogs