Actin is the major constituent of the cytoskeleton of almost all the eukaryotic cells. In vitro experiments have indicated that oxidant-stressed nonmuscle mammalian cells undergo remarkable changes in their morphology and in the structure of the actin cytoskeleton, often resulting in plasma membrane blebbing. Although the microfilament network is one of the earliest targets of oxidative stress. the mechanism by which oxidants change both the structure and the spatial organization of actin filaments is still a matter of debate and far from being fully elucidated. Starting from the 2-fold role of oxidants as injurious by-products of cellular metabolism and essential participants in cell signaling and regulation. this review attempts to,rather the most relevant information related to (i) the activation of mitogen-activated protein (MAP) kinase stress-activated protein kinase-2/p38 (SAPK2/p38) which, via MAP kinase-activated protein (MAPKAP) kinase 2/3. leads to the phosphorylation of the actin polymerization (F-actin) modulator 25/27 kDa heat shock protein (HSP25/27). whose phosphorylation is causally related to the regulation of microfilament dynamics following oxidative stress: (ii) the alteration of the redox state of actin or some actin regulatory proteins. The actin cytoskeleton response to oxidants is discussed on the basis of the growing hods of evidence indicating the actin system its the most sensitive constituent of the cytoskeleton to the oxidant attack.

The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself / I. Dalle Donne, R. Rossi, A. Milzani, P. Di Simplicio, R. Colombo. - In: FREE RADICAL BIOLOGY & MEDICINE. - ISSN 0891-5849. - 31:12(2001), pp. 1624-1632. [10.1016/S0891-5849(01)00749-3]

The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself

I. Dalle Donne;A. Milzani;R. Colombo
2001

Abstract

Actin is the major constituent of the cytoskeleton of almost all the eukaryotic cells. In vitro experiments have indicated that oxidant-stressed nonmuscle mammalian cells undergo remarkable changes in their morphology and in the structure of the actin cytoskeleton, often resulting in plasma membrane blebbing. Although the microfilament network is one of the earliest targets of oxidative stress. the mechanism by which oxidants change both the structure and the spatial organization of actin filaments is still a matter of debate and far from being fully elucidated. Starting from the 2-fold role of oxidants as injurious by-products of cellular metabolism and essential participants in cell signaling and regulation. this review attempts to,rather the most relevant information related to (i) the activation of mitogen-activated protein (MAP) kinase stress-activated protein kinase-2/p38 (SAPK2/p38) which, via MAP kinase-activated protein (MAPKAP) kinase 2/3. leads to the phosphorylation of the actin polymerization (F-actin) modulator 25/27 kDa heat shock protein (HSP25/27). whose phosphorylation is causally related to the regulation of microfilament dynamics following oxidative stress: (ii) the alteration of the redox state of actin or some actin regulatory proteins. The actin cytoskeleton response to oxidants is discussed on the basis of the growing hods of evidence indicating the actin system its the most sensitive constituent of the cytoskeleton to the oxidant attack.
actin cytoskeleton ; small heat shock proteins ; sulfhydryl oxidation ; S-thiolation ; methionine oxidation ; protein carbonylation ; free radicals
Settore BIO/06 - Anatomia Comparata e Citologia
2001
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/39488
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