Effect of Nitric Oxide on the Ligand-Binding Activity of Albumin

Kashiba-Iwatsuki, Misato; Miyamoto, Mitsuhiro; Inoue, Masayasu

doi:10.1006/abbi.1997.0258

Cited by 41 publications

(28 citation statements)

References 28 publications

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“…Although they both involve posttranslational protein modifications, phosphorylation is a catalytic process, whereas S nitrosylation is noncatalytic. Nitrosothiols are exceptionally labile as a result of their reactivity with intracellular reducing agents such as ascorbic acid and glutathione as well as reduced metal ions, especially Cu(I), and have tissue half-lives ranging from seconds to minutes (17,18).…”

Section: Discussionmentioning

confidence: 99%

Nitrosylcobalamin Promotes Cell Death via S Nitrosylation of Apo2L/TRAIL Receptor DR4

Tang¹,

Bauer²,

Morrison³

et al. 2006

Molecular and Cellular Biology

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We have previously demonstrated that nitrosylcobalamin (NO-Cbl), an analogue of vitamin B 12 that delivers nitric oxide (NO), had potent antiproliferative activity against several human cancer cell lines. NO-Cbl induced apoptosis via a death receptor/caspase-8 pathway. In this study, we demonstrate that a functional Apo2L/ TRAIL receptor was necessary for the induction of cell death by NO-Cbl. Furthermore, the Apo2L/TRAIL death receptor DR4 (TRAIL R1) was S nitrosylated following NO-Cbl treatment. Human melanoma (A375), renal carcinoma (ACHN), and ovarian carcinoma (NIH-OVCAR-3) cells were treated with NO-Cbl and subjected to the biotin switch assay; S-nitrosylated DR4 was detected in all three cell lines. NO-Cbl treatment did not cause S nitrosylation of DR5. The seven cysteine residues located in the cytoplasmic domain of DR4 were individually point mutated to alanines. NIH-OVCAR-3 cells expressing the DR4 C336A mutation lacked S nitrosylation following NO-Cbl treatment. Overexpression of wild-type DR4 sensitized cells to growth inhibition by NO-Cbl. Cells expressing the DR4 C336A mutant were more resistant to NO-Cbl and Apo2L/ TRAIL than were the other six C-A mutations or wild-type cells. The C336A mutant also displayed blunted caspase-8 enzymatic activity following NO-Cbl treatment compared to the other mutants. Thus, DR4 residue C336 becomes S nitrosylated and promotes apoptosis following NO-Cbl treatment.Mammalian cells have two major apoptotic pathways, the extrinsic and intrinsic pathways. The extrinsic pathway is triggered by members of the death receptor superfamily (Fas/ CD95, TNFR1, and TRAIL receptors DR4 and DR5). Binding of ligands to their cognate death receptors induces receptor clustering and the formation of a death-inducing signaling complex. The intrinsic apoptotic pathway is controlled by mitochondrial events.We have previously demonstrated the antitumor activity of nitrosylcobalamin (NO-Cbl), a prodrug based upon vitamin B 12 that delivers nitric oxide (NO). NO-Cbl induces the expression of tumor necrosis factor-related apoptosis-inducing ligand (Apo2L/TRAIL) and its receptors (DR4 and DR5) in ovarian carcinoma cells (4). NO-Cbl induces tumor cell apoptosis through the extrinsic apoptotic pathway rather than the mitochondrion-dependent intrinsic pathway.Nitric oxide is a pleiotropic short-lived free radical that regulates blood vessel and airway tone, inflammation, and apoptosis. NO covalently modifies heme groups (as in guanylyl cyclase) and also nitrosylates protein sulfhydryl groups (S nitrosylation), an important posttranslational modification that affects signal transduction (27). Nitrosylation of cellular proteins regulates the normal physiologic ventilatory response to hypoxia (21), ion channel activity and neurotransmission (6), smooth muscle relaxation (19), and blood pressure regulation (8).In neurons, the plasma membrane N-methyl-D-aspartate receptor becomes S nitrosylated by neuronal nitric oxide synthase (NOS1), which modulates receptor activity (15). Recently, S nitrosylatio...

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Section: Discussionmentioning

confidence: 99%

Nitrosylcobalamin Promotes Cell Death via S Nitrosylation of Apo2L/TRAIL Receptor DR4

Tang¹,

Bauer²,

Morrison³

et al. 2006

Molecular and Cellular Biology

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“…The flexibility of the N-terminal HSA domain is stressed by crystallography studies (58). In fact, the N-terminal binding affinity of HSA for Cu 2ϩ has been shown to be affected by oxidation of the remote cysteine residue 34 (59,60). Interestingly, oxidative processes are hallmarks of inflamed skin.…”

Section: Discussionmentioning

confidence: 99%

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation

Thierse

Moulon

Allespach

et al. 2004

The Journal of Immunology

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Nickel allergy clearly involves the activation of HLA-restricted, skin-homing, Ni-specific T cells by professional APCs. Nevertheless, knowledge concerning the molecular details of metal-protein interactions underlying the transport and delivery of metal ions to APC during the early sensitization phase and their interactions with HLA and TCRs is still fragmentary. This study investigates the role of human serum albumin (HSA), a known shuttling molecule for Ni2+ and an often-disregarded, major component of skin, in these processes. We show that Ni-saturated HSA complexes (HSA-Ni) induce and activate Ni-specific human T cells as potently as Ni salt solutions when present at equimolar concentrations classically used for in vitro T cell stimulation. However, neither HSA itself nor its Ni-binding N-terminal peptide are involved in determining the specificity of antigenic determinants. In fact, HSA could be replaced by xenogeneic albumins exhibiting sufficient affinity for Ni2+ as determined by surface plasmon resonance (Biacore technology) or atomic absorption spectroscopy. Moreover, despite rapid internalization of HSA-Ni by APC, it was not processed into HLA-associated epitopes recognizable by Ni-specific T cells. In contrast, the presence of HSA-Ni in the vicinity of transient contacts between TCR and APC-exposed HLA molecules appeared to facilitate a specific transfer of Ni2+ from HSA to high-affinity coordination sites created at the TCR/HLA-interface.

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“…For example, the limited binding capacity of circulating albumin for nitric oxide could be 1 mechanism of the decreased blood pressure and the need for pressors in hepatic failure when albumin-bound toxins reach critical blood levels. [18][19][20] Another probably nonspecific toxic effect arises from the influence on endothelial cells, which react with cell membrane damage and impaired prostacyclin pathways. 21 Specific effects of protein-bound toxins NOTE.…”

Section: Discussionmentioning

confidence: 99%

Liver Support by Extracorporeal Blood Purification: A Clinical Observation

Stange

Mitzner

Klammt

et al. 2000

Liver Transplantation

132

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Liver failure associated with excretory insufficiency and jaundice results in an endogenous accumulation of toxins involved in the impairment of cardiovascular, kidney, and cerebral function. Moreover, these toxins have been shown to damage the liver itself by inducing hepatocellular apoptosis and necrosis, thus creating a vicious cycle of the disease. We report a retrospective cohort study of 26 patients with acute or chronic liver failure with intrahepatic cholestasis (bilirubin level > 20 mg/dL) who underwent a new extracorporeal blood purification treatment. A synthetic hydrophilic/hydrophobic domain-presenting semipermeable membrane (pore size < albumin size, 100-nm thick) was used for extracorporeal blood detoxification using dialysis equipment. The opposite side was rinsed with ligandin-like proteins as molecular adsorbents that were regenerated online using a chromatography-like recycling system (molecular adsorbent recirculating system [MARS]). Bile acid and bilirubin levels, representing the previously described toxins, were reduced by 16% to 53% and 10% to 90% of the initial concentration by a single treatment of 6 to 8 hours, respectively. Toxicity testing of patient plasma onto primary rat hepatocytes by live/dead fluorescence microscopy showed cell-damaging effects of jaundiced plasma that were not observed after treatment. Patients with a worsening of Child-TurcottePugh (CTP) index before the treatments showed a significant improvement of this index during a period of 2 to 14 single treatments with an average of 14 days. After withdrawal of MARS treatment, this improvement was sustained in all long-term survivors. Ten patients represented a clinical status equivalent to the United Network for Organ Sharing (UNOS) status 2b (group A1), and all survived. Sixteen patients represented a clinical status equivalent to UNOS status 2a, and 7 of these patients survived (group A2), whereas 9 patients (group B) died. We conclude that in acute excretory failure caused by a chronic liver disease, this treatment provides a therapy option to remove toxins involved in multiorgan dysfunction secondary to liver failure. (Liver Transpl 2000;6: 603-613.)

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Effect of Nitric Oxide on the Ligand-Binding Activity of Albumin

Cited by 41 publications

References 28 publications

Nitrosylcobalamin Promotes Cell Death via S Nitrosylation of Apo2L/TRAIL Receptor DR4

Nitrosylcobalamin Promotes Cell Death via S Nitrosylation of Apo2L/TRAIL Receptor DR4

Metal-Protein Complex-Mediated Transport and Delivery of Ni2+ to TCR/MHC Contact Sites in Nickel-Specific Human T Cell Activation

Liver Support by Extracorporeal Blood Purification: A Clinical Observation

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