ArticleMolecular and cellular biology2006
Sodium nitroprusside promotes IRP2 degradation via an increase in intracellular iron and in the absence of S nitrosylation at C178.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 33 citations in OpenAlex.
- Mammalian iron metabolism and its control by iron regulatory proteins.Biochimica et biophysica acta · 2012Review
- Iron regulatory protein 1 outcompetes iron regulatory protein 2 in regulating cellular iron homeostasis in response to nitric oxide.The Journal of biological chemistry · 2011Article
- Regulation of cellular iron metabolism.The Biochemical journal · 2011Review
- Sodium nitroprusside-mediated alleviation of iron deficiency and modulation of antioxidant responses in maize plants.AoB PLANTS · 2010Article
- Iron-dependent degradation of IRP2 requires its C-terminal region and IRP structural integrity.BMC molecular biology · 2008Article
- Exposure to nitric oxide protects against oxidative damage but increases the labile iron pool in sorghum embryonic axes.Journal of experimental botany · 2008Article
- Iron-dependent degradation of apo-IRP1 by the ubiquitin-proteasome pathway.Molecular and cellular biology · 2007Article
- Molecular control of vertebrate iron homeostasis by iron regulatory proteins.Biochimica et biophysica acta · 2006Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
In iron-replete cells the posttranscriptional regulator IRP2 undergoes ubiquitination and proteasomal degradation. A similar response occurs in cells exposed to sodium nitroprusside (SNP), an NO-releasing drug. It has been proposed that nitroprusside ([Fe(CN)5NO]2-) fails to donate iron into cells and that it promotes IRP2 degradation via S nitrosylation at C178. This residue is located within a stretch of 73 amino acids, earlier proposed to define an iron-dependent degradation domain. Surprisingly, we show that IRP2 bearing a C178S mutation or a Delta73 deletion is sensitive to degradation not only by ferric ammonium citrate (FAC) but also by SNP. Moreover, FAC and SNP attenuate the RNA-binding activities of IRP2 and its homologue IRP1 with similar kinetics. Actinomycin D, cycloheximide, succinylacetone, and dimethyl-oxalylglycine antagonize IRP2 degradation in response to both FAC and SNP, suggesting a common mechanistic basis. IRP2 is not only sensitive to fresh, but also to photodegraded SNP and remains unaffected by S-nitrosoglutathione (GSNO), an established nitrosation agent. Importantly, both fresh and photodegraded SNP, but not GSNO, promote a >4-fold increase in the calcein-accessible labile iron pool. Collectively, these results suggest that IRP2 degradation by SNP does not require S nitrosylation but rather represents a response to iron loading.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.