Intracellular Localization of Endothelial Cell Annexins Is Differentially Regulated by Oxidative Stress

Sacre, Sandra

doi:10.1006/excr.2002.5469

Cited by 31 publications

(15 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The cluster is formed by two adjacent cysteine residues and the sulphur of a nearby methionine residue and is located in helices IIB and IIIE [38]. Annexin A1 from Arabidopsis thaliana (AnnAt1) participates in modulating the excessive levels of reactive oxygen species during oxidative burst in plants [39]. AnnAt1 from A. thaliana , expressed in Escherichia coli and Nicotiana benthamiana possesses peroxidase activity [40].…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, hydrogen peroxide accumulation in guard cells was reduced in plants over-expressing AnnAt1 and increased in knockout plants [41]. Plant AnnAt1 as most annexins, does not possess a nuclear localization sequence; however, translocation of the protein to the nucleus has been observed upon stress stimulation [39], [42]–[44]. Similarly, treatment of cells with H 2 O 2 has been shown to cause the translocation of mammalian annexin I from the cytoplasm to the nucleus [40].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Genotoxic Agents Promote the Nuclear Accumulation of Annexin A2: Role of Annexin A2 in Mitigating DNA Damage

et al. 2012

View full text Add to dashboard Cite

Annexin A2 is an abundant cellular protein that is mainly localized in the cytoplasm and plasma membrane, however a small population has been found in the nucleus, suggesting a nuclear function for the protein. Annexin A2 possesses a nuclear export sequence (NES) and inhibition of the NES is sufficient to cause nuclear accumulation. Here we show that annexin A2 accumulates in the nucleus in response to genotoxic agents including gamma-radiation, UV radiation, etoposide and chromium VI and that this event is mediated by the nuclear export sequence of annexin A2. Nuclear accumulation of annexin A2 is blocked by the antioxidant agent N-acetyl cysteine (NAC) and stimulated by hydrogen peroxide (H2O2), suggesting that this is a reactive oxygen species dependent event. In response to genotoxic agents, cells depleted of annexin A2 show enhanced phospho-histone H2AX and p53 levels, increased numbers of p53-binding protein 1 nuclear foci and increased levels of nuclear 8-oxo-2′-deoxyguanine, suggesting that annexin A2 plays a role in protecting DNA from damage. This is the first report showing the nuclear translocation of annexin A2 in response to genotoxic agents and its role in mitigating DNA damage.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Genotoxic Agents Promote the Nuclear Accumulation of Annexin A2: Role of Annexin A2 in Mitigating DNA Damage

et al. 2012

View full text Add to dashboard Cite

show abstract

“…-independently with phospholipid vesicles in vitro at pH 7.4, in the presence of 3 mM H 2 O 2 [202]. The expression and localization of annexins was investigated in chronically hyperoxically stressed endothelial cells [203]. In this study, annexin expression levels did not change significantly in response to hyperoxic stress, but immunofluorescence analysis revealed striking effects on the subcellular localization of certain annexins, including the redistribution of annexins A5 and A6 from the cytosol to the nucleus.…”

Section: Cellular Stress and Membrane Repairmentioning

confidence: 92%

The annexins: spatial and temporal coordination of signaling events during cellular stress

Monastyrskaya

Babiychuk

Draeger

2009

Cell. Mol. Life Sci.

125

View full text Add to dashboard Cite

Annexins are a family of structurally related, Ca2+-sensitive proteins that bind to negatively charged phospholipids and establish specific interactions with other lipids and lipid microdomains. They are present in all eukaryotic cells and share a common folding motif, the "annexin core", which incorporates Ca2+- and membrane-binding sites. Annexins participate in a variety of intracellular processes, ranging from the regulation of membrane dynamics to cell migration, proliferation, and apoptosis. Here we focus on the role of annexins in cellular signaling during stress. A chronic stress response triggers the activation of different intracellular pathways, resulting in profound changes in Ca2+ and pH homeostasis and the production of lipid second messengers. We review the latest data on how these changes are sensed by the annexins, which have the ability to simultaneously interact with specific lipid and protein moieties at the plasma membrane, contributing to stress adaptation via regulation of various signaling pathways.

show abstract

“…These enzymes are implicated in endocytosis, apoptosis, inflammation and fibrinolysis. In mammals, it has been suggested that annexins may contribute to the regulation of ROS levels during the oxidative burst, as described for annexin-1, annexin-5 and annexin-6 (Rhee, Kim, Huh, Kim, & Na, 2000;Sacre & Moss, 2002), and, consistent with this type of activity, the expression of annexins is induced by factors affecting the redox state of the cell (Tanaka et al, 2004). According to Rhee, Kim, Huh, and Kim (2000) annexins can be assimilated to stress proteins induced by heat or oxidative stress.…”

Section: Proteomics and Lipid Oxidationmentioning

confidence: 97%

Early post-mortem sarcoplasmic proteome of porcine muscle related to lipid oxidation in aged and cooked meat

Sayd¹,

Chambon²,

Laville³

et al. 2012

Food Chemistry

View full text Add to dashboard Cite

Intracellular Localization of Endothelial Cell Annexins Is Differentially Regulated by Oxidative Stress

Cited by 31 publications

References 37 publications

Genotoxic Agents Promote the Nuclear Accumulation of Annexin A2: Role of Annexin A2 in Mitigating DNA Damage

Genotoxic Agents Promote the Nuclear Accumulation of Annexin A2: Role of Annexin A2 in Mitigating DNA Damage

The annexins: spatial and temporal coordination of signaling events during cellular stress

Early post-mortem sarcoplasmic proteome of porcine muscle related to lipid oxidation in aged and cooked meat

Contact Info

Product

Resources

About