Nitrosative protein tyrosine modifications: biochemistry and functional significance

Yeo, Woon‐Seok; Lee, Soo Jae; Lee, J.; Kim, Kwang Pyo

doi:10.5483/bmbrep.2008.41.3.194

Cited by 66 publications

(55 citation statements)

References 92 publications

(75 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…5 It has been known that the targeted nitration of certain tyrosine residues may be biochemically correlated with the structure-function relationship of nitrated proteins. 6,7 The nitration of protein tyrosine residues may result in dramatic changes in protein structure and consequently alter its function, which link nitrosative stress to altered molecular functions in disease [8][9][10][11] The nitrated sites (356Y and 366Y) of sphingosine-1-phosphate lyase 1(SIP lyase 1) are located in the catalytic domain of the protein.…”

Section: Introductionmentioning

confidence: 99%

Mass Spectrometry Analysis of In Vitro Nitration of Carbonic Anhydrase II

Lee¹,

Kang²,

Cho³

et al. 2014

Bulletin of the Korean Chemical Society

View full text Add to dashboard Cite

Protein tyrosine nitration is considered as an important indicator of nitrosative stresses and as one of the main factors for pathogenesis of inflammation and neuronal degeneration. In this study, we investigated various nitrosative modifications of bovine carbonic anhydrase II (CAII) through qualitative and semi-quantitative analysis using the combined strategy of Fourier transformation ion cyclotron resonance mass spectrometry (FT-ICR MS) and ion-trap tandem mass spectrometry (IT-MS/MS). FT-ICR MS and its spectra were used for the search of the pattern of nitrosative modifications. Identification of nitrosatively modified tyrosine sites were executed through IT-MS/MS. In addition, we also tried to infer the reason for the site-specific nitrosative modifications in CAII. In view of the above purpose, we have explored-i) the side chain accessibility, ii) the electrostatic environment originated from the acidic/basic amino acid residues neighboring to the nitrosatively modified site and iii) the existence of competing amino acid residues for nitration.

show abstract

Section: Introductionmentioning

confidence: 99%

Mass Spectrometry Analysis of In Vitro Nitration of Carbonic Anhydrase II

Lee¹,

Kang²,

Cho³

et al. 2014

Bulletin of the Korean Chemical Society

View full text Add to dashboard Cite

show abstract

“…Instead, it inhibits VHL recruitment, stabilizing the transactive form of HIF-1␣ in normoxic cells. NO is released in many pathophysiological conditions, including inflammation and blood clotting (Vadseth et al, 2004;Yeo et al, 2008). In these conditions, a variety of mediators may interfere with the NO effects on the regulation of HIF-1␣.…”

mentioning

confidence: 99%

Nitric Oxide Donor, (±)-S-Nitroso-N-acetylpenicillamine, Stabilizes Transactive Hypoxia-Inducible Factor-1α by Inhibiting von Hippel-Lindau Recruitment and Asparagine Hydroxylation

Park

Ahn²,

Oh³

et al. 2008

Mol Pharmacol

View full text Add to dashboard Cite

We have confirmed that the NO donor (Ϯ)-S-nitroso-Nacetylpenicillamine (SNAP) stabilizes the transactive form of hypoxia-inducible factor-1␣ (HIF-1␣), leading to the induction of HIF-1␣ target genes such as vascular endothelial growth factor and carbonic anhydrase 9. Activation of HIF-1␣ should require inhibition of the dual system that keeps it inactive. One is ubiquitination, which is triggered by hydroxylation of HIF-1␣-proline and the subsequent binding of E3 ubiquitin ligase, the von Hippel Lindau (VHL) protein. The other is hydroxylation of HIF-1␣-asparagine, which reduces the affinity of HIF-1␣ for its coactivator, cAMP responsive element binding protein/p300. We examined the effects of the NO donor SNAP on proline and asparagine hydroxylation of HIF-1␣ peptides by measuring the activities of the corresponding enzymes, HIF-1␣-specific proline hydroxylase 2 (PHD2) and the HIF-1␣-specific asparagine hydroxylase, designated factor inhibiting HIF-1␣ (FIH-1), respectively. We found that the SNAP did not prevent PHD2 from hydroxylating the proline of HIF-1␣. Instead, it blocked the interaction between VHL and the proline-hydroxylated HIF-1␣, but only when the reducing agents Fe(II) and vitamin C were limiting. The fact that the absence of cysteine 520 of HIF-1␣ abolishes its responsiveness to SNAP suggests that this residue mediates the inhibition by SNAP of the interaction between VHL and HIF-1␣, presumably by S-nitrosylation of HIF-1␣. Unlike PHD2, asparagine hydroxylation by FIH-1 was directly inhibited by SNAP, but again only when reducing agents were limiting. Substitution of cysteine 800 of HIF-1␣ with alanine failed to reverse the inhibitory effects of SNAP on asparagine hydroxylation, implying that FIH-1, not its substrate HIF-1␣, is inhibited by SNAP.Hypoxia-inducible factor-1 (HIF-1), a heterodimeric transcription factor, is a master transcription activator responsible for gene induction under hypoxic conditions (Semenza, 2000). It is composed of an ␣ subunit and a ␤ subunit. HIF-1␣ is ubiquitinated and rapidly degraded under normoxic conditions (Jaakkola et al., 2001). The stability and activity of the ␣ subunit of HIF-1 are regulated by post-translational modification, specifically by hydroxylation. Proline residues 402 and 564 of the oxygen-dependent degradation domain (ODD; amino acids 401-603 of human HIF-1␣) are hydroxylated, mainly by HIF-1␣-specific proly-4-hydroxylase 2 (PHD2)

show abstract

“…Based on changes of these two ratios, a decrease intracellular and extracellular antioxidative capacity in obese animals makes them a potentially more vulnerable target for reactive oxygen species (ROS) and nitrogen oxygen species (NOS) to attack and harm cellular homeostasis resulting in hard consequences on many intracellular reactions, including involvement of proteins, lipids, DNA, and RNA. As evidence of this much higher pro-oxidative environment in obese rats, one of the possible candidate molecules representing protein damage is 3-nitrotyrosine [27,28]. 3-nitrotyrosine (3-NT) is modified (damaged) amino acid by NOS and capable change proteins properties which will lead to change enzymes activity.…”

Section: Discussionmentioning

confidence: 99%