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3 results on '"Curtino JA"'

1. Enhancement by GOSPEL protein of GAPDH aggregation induced by nitric oxide donor and its inhibition by NAD(.).

Author

González MC, Romero JM, Ingaramo MC, Muñoz Sosa CJ, Curtino JA, and Carrizo ME

Subjects
Active Transport, Cell Nucleus, Cell Line, Cell Nucleus genetics, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) genetics, Humans, NAD genetics, Nitric Oxide genetics, Apoptosis physiology, Cell Nucleus metabolism, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) metabolism, NAD metabolism, Nitric Oxide metabolism
Abstract

Glyceraldehyde-3-phosphate dehydrogenase's (GAPDH's) competitor of Siah Protein Enhances Life (GOSPEL) is the protein that competes with Siah1 for binding to GAPDH under NO-induced stress conditions preventing Siah1-bound GAPDH nuclear translocation and subsequent apoptosis. Under these conditions, GAPDH may also form amyloid-like aggregates proposed to be involved in cell death. Here, we report the in vitro enhancement by GOSPEL of NO-induced GAPDH aggregation resulting in the formation GOSPEL-GAPDH co-aggregates with some amyloid-like properties. Our findings suggest a new function for GOSPEL, contrasting with its helpful role against the apoptotic nuclear translocation of GAPDH. NAD(+) inhibited both GAPDH aggregation and co-aggregation with GOSPEL, a hitherto undescribed effect of the coenzyme against the consequences of oxidative stress., (© 2016 Federation of European Biochemical Societies.)

Published
2016
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2. Structural and biochemical insight into glycogenin inactivation by the glycogenosis-causing T82M mutation.

Author

Carrizo ME, Romero JM, Issoglio FM, and Curtino JA

Subjects
Amino Acid Substitution, Animals, Apoenzymes chemistry, Apoenzymes genetics, Apoenzymes metabolism, Crystallography, X-Ray, Enzyme Activation, Glucosides metabolism, Glucosyltransferases genetics, Glycoproteins genetics, Glycosylation, Hydrogen Bonding, Hydrolysis, Models, Molecular, Muscles enzymology, Mutant Proteins genetics, Protein Conformation, Rabbits, Uridine Diphosphate Glucose metabolism, Glucosyltransferases chemistry, Glucosyltransferases metabolism, Glycogen Storage Disease genetics, Glycoproteins chemistry, Glycoproteins metabolism, Mutant Proteins chemistry, Mutant Proteins metabolism, Mutation
Abstract

The X-ray structure of rabbit glycogenin containing the T82M (T83M according to previous authors amino acid numbering) mutation causing glycogenosis showed the loss of Thr82 hydrogen bond to Asp162, the residue involved in the activation step of the glucose transfer reaction mechanism. Autoglucosylation, maltoside transglucosylation and UDP-glucose hydrolyzing activities were abolished even though affinity and interactions with UDP-glucose and positioning of Tyr194 acceptor were conserved. Substitution of Thr82 for serine but not for valine restored the maximum extent of autoglucosylation as well as transglucosylation and UDP-glucose hydrolysis rate. Results provided evidence sustaining the essential role of the lost single hydrogen bond for UDP-glucose activation leading to glycogenin-bound glycogen primer synthesis., (Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Published
2012
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3. The amphiphilic character of glycogenin.

Author

Carrizo ME, Miozzo MC, Maggio B, and Curtino JA

Subjects
Adsorption, Animals, Cattle, Lipid Bilayers, Phospholipids, Rabbits, Surface Properties, Thermodynamics, Glucosyltransferases chemistry, Glycogen biosynthesis, Glycoproteins chemistry
Abstract

This study describes for the first time the amphiphilicity of the protein moiety of proteoglycogen. Glycogenin but not proteoglycogen associates to phospholipid vesicles and forms by itself stable Gibbs and Langmuir monolayers at the air-buffer interface. The adsorption free energy (-6.7 kcal/mol) and the glycogenin collapse pressure (47 mN/m) are indicative of its high surface activity which can thermodynamically drive and retain the protein at the membrane interface to a maximum equilibrium adsorption surface pressure of 21 mN/m. The marked surface activity of glycogenin is further enhanced by its thermodynamically favorable penetration into zwitterionic and anionic phospholipids with a high cut-off surface pressure point above 30 mN/m. The strong association to phospholipid vesicles and the marked surface activity of glycogenin correspond to a high amphiphilic character which supports its spontaneous association to membrane interfaces, in which the de novo biosynthesis of glycogen was proposed to initiate.

Published
2001
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