Non-enzymic protein phosphorylation. Phosphorylation of 6-phosphogluconate dehydrogenase by acyl phosphates

Dallocchio, Franco; Matteuzzi, Maurizio; Bellini, Tiziana

doi:10.1042/bj2030401

Cited by 8 publications

(4 citation statements)

References 9 publications

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“…Phosphogluconate dehydrogenase activity is up-regulated in pertinent cortical regions of AD brains as a compensatory reaction to highly oxidative environments [79]. Phosphorylation of 6PGD has been previously demonstrated [80]. …”

Section: Discussionmentioning

confidence: 99%

Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer's disease subjects

Domenico

Sultana

Barone

et al. 2011

Journal of Proteomics

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Phosphorylation on tyrosine, threonine and serine residues represents one of the most important post-translational modifications and is a key regulator of cellular signaling of multiple biological processes that require a strict control by protein kinases and protein phosphatases. Abnormal protein phosphorylation has been associated with several human diseases including Alzheimer disease (AD). One of the characteristic hallmarks of AD is the presence of neurofibrillary tangles, composed of microtubule-associated, abnormally hyperphosphorylated tau protein. However, several others proteins showed altered phosphorylation levels in AD suggesting that deregulated phosphorylation may contribute to AD pathogenesis. Phosphoproteomics has recently gained attention as a valuable approach to analyze protein phosphorylation, both in a quantitave and a qualitative way. We used the fluorescent phosphospecific Pro-Q Diamond dye to identify proteins that showed alterations in their overall phosphorylation in the hippocampus of AD vs. control (CTR) subjects. Significant changes were found for 17 proteins involved in crucial neuronal process such as energy metabolism or signal transduction. These phosphoproteome data may provide new clues to better understand molecular pathways that are deregulated in the pathogenesis and progression of AD.

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Section: Discussionmentioning

confidence: 99%

Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer's disease subjects

Domenico

Sultana

Barone

et al. 2011

Journal of Proteomics

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“…6-Phosphogluconate dehydrogenase was phosphorylated by acetyl phosphate, carbamoyl phosphate, and 1, 3-bisphosphoglycerate (Dallocchio et al, 1982). This seems rather specific for 6phosphogluconate dehydrogenase, since other proteins were not phosphorylated under the same conditions (Dallocchio et al, 1982). The amount of phosphorus covalently bound to proteins by these methods is shown in Table I.…”

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confidence: 92%

Chemical phosphorylation of food proteins: an overview and a prospectus

Matheis¹,

Whitaker²

1984

J. Agric. Food Chem.

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“…Chemical phosphorylation of proteins was studied by several authors. Most studies (Taborsky, 1958;Ullman and Perlman, 1975;Willmitzer and Wagner, 1975;Dallocchio et al, 1982;Woo et al, 1982) were devoted to the mechanism of phosphorylation by using a variety of chemicals. Little information is available about the use of phosphorylation for changing the nutritional and functional properties of food proteins.…”

Section: Introductionmentioning

confidence: 99%

Physicochemical and Dynamic Properties of Caseins Modified by Chemical Phosphorylation

Medina

Colas

Meste

et al. 1992

Journal of Food Science

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Chemical phosphorylation of bovine caseins may be useful for changing their ihysiiochkmical properties. Depending on the pH of phoiohorvlation of caseins bv ohosuhorus oxvchloride (POClA covalent bon& between phosphaie 'groul~ and diiferent spe'cific &ino acids were formed. After casein phosphorylation, intermolecular associations may occur, as shown by electrophoresis. The solubility of modified casein was increased near the isoelectric point (pHi) and decreased at alkaline and acidic pH. In the presence of Ca++ at alkaline pH, the solubility of phosphorylated casein was lower than that of the control. Rheological parameters appeared to be efficient indices of structural changes occurring in proteins as a result of chemical modifications. Electron spin resonance studies showed that the flexibility of phosphorylated casein was higher than that of the control. phosphorylated casein was measured as a function of the level of phosphorylation and of the pH and ionic strength of the medium. The influence of the level of phosphorylation, pH and casein concentration on chain flexibility was evaluated by electron spin resonance (ESR) spectrometry. Viscosity measurements were also performed, in order to determine the flow behavior of casein solutions and their intrinsic viscosity. MATERIALS & METHODSCasein preparation Native bovine casein was obtained from skim milk by precipitation at the isoelectric point (pH 4.6) using 1M hydrochloric acid solution. The precipitate was washed, solubilized at pH 7 with sodium hydroxide, precipitated again and washed three more times. Finally, the casein was solubilized again at pH 7, freeze-dried and stored at 4°C in hermetically sealed bags.

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Non-enzymic protein phosphorylation. Phosphorylation of 6-phosphogluconate dehydrogenase by acyl phosphates

Cited by 8 publications

References 9 publications

Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer's disease subjects

Quantitative proteomics analysis of phosphorylated proteins in the hippocampus of Alzheimer's disease subjects

Chemical phosphorylation of food proteins: an overview and a prospectus

Physicochemical and Dynamic Properties of Caseins Modified by Chemical Phosphorylation

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