Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase

Andre Laval Samson; Anja Sylvia Knaupp; Itamar Kass; Oded Kleifeld; Emilia Maria Marijanovic; Victoria Anne Hughes; Christopher Joseph Lupton; Ashley Maurice Buckle; Stephen Paul Bottomley; Robert Lindsay Medcalf

doi:10.1074/jbc.M114.570275

Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase

Andre Laval Samson, Anja Sylvia Knaupp, Itamar Kass, Oded Kleifeld, Emilia Maria Marijanovic, Victoria Anne Hughes, Christopher Joseph Lupton, Ashley Maurice Buckle, Stephen Paul Bottomley, Robert Lindsay Medcalf

Research output: Contribution to journal › Article › Research › peer-review

40 Citations (Scopus)

Abstract

Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.

Original language	English
Pages (from-to)	26922 - 26936
Number of pages	15
Journal	Journal of Biological Chemistry
Volume	289
Issue number	39
DOIs	https://doi.org/10.1074/jbc.M114.570275
Publication status	Published - 2014

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10.1074/jbc.M114.570275

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title = "Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase",

abstract = "Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.",

author = "Samson, {Andre Laval} and Knaupp, {Anja Sylvia} and Itamar Kass and Oded Kleifeld and Marijanovic, {Emilia Maria} and Hughes, {Victoria Anne} and Lupton, {Christopher Joseph} and Buckle, {Ashley Maurice} and Bottomley, {Stephen Paul} and Medcalf, {Robert Lindsay}",

year = "2014",

doi = "10.1074/jbc.M114.570275",

language = "English",

volume = "289",

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T1 - Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase

AU - Samson, Andre Laval

AU - Knaupp, Anja Sylvia

AU - Kass, Itamar

AU - Kleifeld, Oded

AU - Marijanovic, Emilia Maria

AU - Hughes, Victoria Anne

AU - Lupton, Christopher Joseph

AU - Buckle, Ashley Maurice

AU - Bottomley, Stephen Paul

AU - Medcalf, Robert Lindsay

PY - 2014

Y1 - 2014

N2 - Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.

AB - Background: GAPDH is a glycolytic enzyme that aggregates during disease. Cysteine oxidation is the putative cause of aggregation. Whether GAPDH aggregation influences disease is unknown. Results: Mutating Met-46 renders GAPDH resistant to free radical-induced aggregation. Conclusion: Methionine oxidation, rather than cysteine oxidation, is a primary event that instigates GAPDH aggregation. Significance: Mutating Met-46 in vivo should elucidate whether GAPDH aggregation causally contributes to disease.

UR - http://www.jbc.org/content/289/39/26922.full.pdf+html

U2 - 10.1074/jbc.M114.570275

DO - 10.1074/jbc.M114.570275

M3 - Article

SN - 0021-9258

VL - 289

SP - 26922

EP - 26936

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 39

ER -

Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase

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To investigate how the aggregation of proteins during neuronal injury promotes neurotoxic plasmin formation

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Oxidation of an exposed methionine instigates the aggregation of glyceraldehyde-3-phosphate dehydrogenase

Abstract

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To investigate how the aggregation of proteins during neuronal injury promotes neurotoxic plasmin formation

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