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Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism. / Pougovkina, Olga; te Brinke, Heleen; Wanders, Ronald J. A. et al.

In: Journal of inherited metabolic disease, Vol. 37, No. 5, 2014, p. 709-714.

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Pougovkina O, te Brinke H, Wanders RJA, Houten SM, de Boer VCJ. Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism. Journal of inherited metabolic disease. 2014;37(5):709-714. doi: 10.1007/s10545-014-9684-9

Author

Pougovkina, Olga ; te Brinke, Heleen ; Wanders, Ronald J. A. et al. / Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism. In: Journal of inherited metabolic disease. 2014 ; Vol. 37, No. 5. pp. 709-714.

BibTeX

@article{6c39991764db480a99d17aa99dd7e572,
title = "Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism",
abstract = "Inherited disorders of acyl-CoA metabolism, such as defects in amino acid metabolism and fatty acid oxidation can present with severe clinical symptoms either neonatally or later in life, but the pathophysiological mechanisms are often incompletely understood. We now report the discovery of a novel biochemical mechanism that could contribute to the pathophysiology of these disorders. We identified increased protein lysine butyrylation in short-chain acyl-CoA dehydrogenase (SCAD) deficient mice as a result of the accumulation of butyryl-CoA. Similarly, in SCAD deficient fibroblasts, lysine butyrylation was increased. Furthermore, malonyl-CoA decarboxylase (MCD) deficient patient cells had increased levels of malonylated lysines and propionyl-CoA carboxylase (PCC) deficient patient cells had increased propionylation of lysines. Since lysine acylation can greatly impact protein function, aberrant lysine acylation in inherited disorders associated with acyl-CoA accumulation may well play a role in their disease pathophysiology",
author = "Olga Pougovkina and {te Brinke}, Heleen and Wanders, {Ronald J. A.} and Houten, {Sander M.} and {de Boer}, {Vincent C. J.}",
year = "2014",
doi = "10.1007/s10545-014-9684-9",
language = "English",
volume = "37",
pages = "709--714",
journal = "Journal of inherited metabolic disease",
issn = "0141-8955",
publisher = "Springer Netherlands",
number = "5",

}

RIS

TY - JOUR

T1 - Aberrant protein acylation is a common observation in inborn errors of acyl-CoA metabolism

AU - Pougovkina, Olga

AU - te Brinke, Heleen

AU - Wanders, Ronald J. A.

AU - Houten, Sander M.

AU - de Boer, Vincent C. J.

PY - 2014

Y1 - 2014

N2 - Inherited disorders of acyl-CoA metabolism, such as defects in amino acid metabolism and fatty acid oxidation can present with severe clinical symptoms either neonatally or later in life, but the pathophysiological mechanisms are often incompletely understood. We now report the discovery of a novel biochemical mechanism that could contribute to the pathophysiology of these disorders. We identified increased protein lysine butyrylation in short-chain acyl-CoA dehydrogenase (SCAD) deficient mice as a result of the accumulation of butyryl-CoA. Similarly, in SCAD deficient fibroblasts, lysine butyrylation was increased. Furthermore, malonyl-CoA decarboxylase (MCD) deficient patient cells had increased levels of malonylated lysines and propionyl-CoA carboxylase (PCC) deficient patient cells had increased propionylation of lysines. Since lysine acylation can greatly impact protein function, aberrant lysine acylation in inherited disorders associated with acyl-CoA accumulation may well play a role in their disease pathophysiology

AB - Inherited disorders of acyl-CoA metabolism, such as defects in amino acid metabolism and fatty acid oxidation can present with severe clinical symptoms either neonatally or later in life, but the pathophysiological mechanisms are often incompletely understood. We now report the discovery of a novel biochemical mechanism that could contribute to the pathophysiology of these disorders. We identified increased protein lysine butyrylation in short-chain acyl-CoA dehydrogenase (SCAD) deficient mice as a result of the accumulation of butyryl-CoA. Similarly, in SCAD deficient fibroblasts, lysine butyrylation was increased. Furthermore, malonyl-CoA decarboxylase (MCD) deficient patient cells had increased levels of malonylated lysines and propionyl-CoA carboxylase (PCC) deficient patient cells had increased propionylation of lysines. Since lysine acylation can greatly impact protein function, aberrant lysine acylation in inherited disorders associated with acyl-CoA accumulation may well play a role in their disease pathophysiology

U2 - 10.1007/s10545-014-9684-9

DO - 10.1007/s10545-014-9684-9

M3 - Article

C2 - 24531926

VL - 37

SP - 709

EP - 714

JO - Journal of inherited metabolic disease

JF - Journal of inherited metabolic disease

SN - 0141-8955

IS - 5

ER -

ID: 2328378