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Glyceraldehyde‐3‐phosphate dehydrogenase tetramer dissociation and amyloid fibril formation induced by negatively charged membranes
Author(s) -
Cortez Leonardo M.,
Ávila César L.,
Torres Bugeau Clarisa M.,
Farías Ricardo N.,
Morero Roberto D.,
Chehín Rosa.
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.12.012
Subject(s) - glyceraldehyde 3 phosphate dehydrogenase , tetramer , chemistry , membrane , fibril , dehydrogenase , biochemistry , biophysics , enzyme , biology
Glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH) is a multifunctional enzyme related with Huntington's, Parkinson's and Alzheimer's diseases. The ability of negatively charged membranes to induce a rapid formation of GAPDH amyloid fibrils has been demonstrated, but the mechanisms by which GAPDH reaches the fibrillar state remains unclear. In this report, we describe the structural changes undergone by GAPDH at physiological pH and temperature conditions right from its interaction with acidic membranes until the amyloid fibril is formed. According to our results, the GAPDH‐membrane binding induces a β‐structuring process along with a loss of quaternary structure in the enzyme. In this way, experimental evidences on the initial steps of GAPDH amyloid fibrils formation pathway are provided.