title: Aggregated proteins accelerate but do not increase the aggregation of D-glyceraldehyde-3-phosphate dehydrogenase. Specificity of protein aggregation.
abstract: The effect of protein aggregates on the aggregation of D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) during unfolding and refolding has been studied. The aggregation of GAPDH follows a sigmoid course. The presence of protein aggregates increases the aggregation rate during unfolding and refolding of GAPDH but does not change the extent of aggregation and the final renaturation yield. It is suggested that protein aggregates function as seeds for aggregation via hydrophobic interaction with only GAPDH folding intermediates destined to aggregate and do not affect the distribution between pathways leading to correct folding and aggregation. Moreover, two different proteins do not interfere with each other during their simultaneous refolding together in a buffer. These findings provide insight into a mechanism by which cells prevent protein folding against the interference from aggregation of other proteins.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, China.
authors.forename: J
authors.initials: J
authors.lastname: Li
authors.forename: Z
authors.initials: Z
authors.lastname: Lin
authors.forename: C C
authors.initials: CC
authors.lastname: Wang
mesh_terms: D000818:Animals; D002417:Cattle; D019803:Glutathione Disulfide / Q000494:pharmacology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000032:analysis / Q000737:chemistry* / Q000187:drug effects; D019791:Guanidine / Q000494:pharmacology; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000737:chemistry* / Q000187:drug effects; D009132:Muscles / Q000201:enzymology; D010277:Parasympathomimetics / Q000494:pharmacology; D010710:Phosphates / Q000494:pharmacology; D017680:Potassium Compounds / Q000494:pharmacology; D011489:Protein Denaturation / Q000187:drug effects; D019704:Protein Disulfide-Isomerases / Q000032:analysis / Q000187:drug effects; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D011817:Rabbits; D012710:Serum Albumin, Bovine / Q000032:analysis / Q000187:drug effects; D013997:Time Factors
chemical_list: D010277:Parasympathomimetics; D010710:Phosphates; D017680:Potassium Compounds; D011506:Proteins; D012710:Serum Albumin, Bovine; C013216:potassium phosphate; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D009113:Muramidase; D019704:Protein Disulfide-Isomerases; D019791:Guanidine; D019803:Glutathione Disulfide