Peroxisomal Properties with Potential Regulatory Implications: Selective ATP Requirement for Fatty Acid Oxidation and Membrane Protein Phosphorylation

Leighton, Federico; Nicovani, Sandra; Soto, Ubaldo; Skorin, C; Necochea, Cecilia

doi:10.1007/978-3-642-71325-5_16

Cited by 3 publications

(2 citation statements)

References 24 publications

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“…Third, the rate of fatty acid oxidation by peroxisome is strictly proportional to the ATP level of the cell. ATP enhances peroxisomal acyl-CoA oxidation and that effect disappears after disruption of the limiting membrane of isolated peroxisomes (23). The protein phosphorylation, mainly a 63 kDa peptide, exists in the limiting membrane, too.…”

Section: Discussionmentioning

confidence: 99%

Cytochemical localization of Mg++-ATPase and Ca++-ATPase on the limiting membrane of rat liver peroxisomes.

Makita

Hakoi

Araki

1990

Acta Histochem. Cytochem

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Section: Discussionmentioning

confidence: 99%

Cytochemical localization of Mg++-ATPase and Ca++-ATPase on the limiting membrane of rat liver peroxisomes.

Makita

Hakoi

Araki

1990

Acta Histochem. Cytochem

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“…Among the genes involved in peroxisome biogenesis (Pex genes), some of their products (peroxins) show ATPase activity (Gould and Valle 2000). In addition, ATP has been related to other peroxisomal functions, such as the ATP requirement for peroxisomal fatty acid oxidation in isolated hepatocytes (Leighton et al 1987), or with the apparent need for ATP to keep structure-linked latency in peroxisomes in situ (Wolvetang et al 1990a).…”

mentioning

confidence: 99%

Cytochemical and Biochemical Demonstration of an ATPase in Membranes of Human Peroxisomes

Koenig

Araya

Skorin

et al. 2002

J Histochem Cytochem.

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We demonstrated a neutral Mg-ATPase activity in human peroxisomal membranes. To establish the precise experimental conditions for detection of this ATPase, both cytochemical and biochemical characterizations were first carried out in liver peroxisomes from control and cipofibrate-treated rats. The results demonstrated an Mg-ATPase reaction in both normal and proliferated peroxisomes. The nucleotidase activity, with marked preference for ATP, was sensitive to the inhibitors N-ethylmaleimide and 7-chloro-4-nitro-benzo-2-oxadiazole (NBDCl). An ultrastructural cytochemical analysis was developed to evaluate the peroxisomal localization, which localized the reaction product to the peroxisomal membrane. These characteristics can help to differentiate the peroxisomal ATPase from the activity found in mitochondria and endoplasmic reticulum. The conditions established for detecting the rat peroxisomal ATPase were then applied to human peroxisomes isolated from liver and skin fibroblasts in culture. A similar Mg-ATPase activity was readily shown, both cytochemically and biochemically, in the membranes of human peroxisomes. These results, together with previous evidence, strongly support the presence of a specific ATPase in the human peroxisomal membrane. This ATPase may play a crucial role in peroxisome biogenesis.

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Intracellular cholesterol transport

Seedorf¹,

Brysch²,

Engel³

et al. 1995

Developments in Cardiovascular Medicine

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Peroxisomal Properties with Potential Regulatory Implications: Selective ATP Requirement for Fatty Acid Oxidation and Membrane Protein Phosphorylation

Cited by 3 publications

References 24 publications

Cytochemical localization of Mg++-ATPase and Ca++-ATPase on the limiting membrane of rat liver peroxisomes.

Cytochemical localization of Mg++-ATPase and Ca++-ATPase on the limiting membrane of rat liver peroxisomes.

Cytochemical and Biochemical Demonstration of an ATPase in Membranes of Human Peroxisomes

Intracellular cholesterol transport

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