Nitrosylated human serum albumin (SNO-HSA) induces apoptosis in tumor cells

Katayama, Naohisa; Nakajou, Keisuke; Ishima, Yu; Ikuta, Shotaro; Yokoe, Jun ichi; Yoshida, Fumika; Suenaga, Atsushi; Maruyama, Toru; Kai, Toshiya; Otagiri, Masaki

doi:10.1016/j.niox.2009.09.003

Cited by 30 publications

(34 citation statements)

References 28 publications

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“…THE DIRECT ANTICANCER ACTION OF POLY-SNO-HSA VIA APOPTOSIS Previously, poly-SNO-HSA was incubated with various cancer cells, and we observed that this HSA form had the ability to induce the apoptosis of cancer cells. [16][17][18] Via activation of the intrinsic apoptosis pathway, apoptosis occurred in various cancer cells such as murine colon cancer, C26 cells, and a variant of Yoshida sarcoma, LY-80 cells, both in vivo and in vitro.…”

Section: Poly-sno-hsa As a Carrier For The Tar-geted Delivery Of No Tmentioning

confidence: 99%

“…These data suggest that poly-SNO-HSA is not a reliably long-lasting NO donor. 39) To construct a superior NO delivery carrier, we investigated the factors involved in the stability of S-nitroso on poly-SNO-HSA. Previous findings demonstrated that a polyethylene glycol (PEG) elevated the stability of S-nitroso compounds, because the PEG acts as a stabilizer of S-nitroso bonding.…”

Section: Perspectives Of Poly-sno-hsa As An Anti-cancer Drugmentioning

confidence: 99%

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Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers

Ishima

2017

Biological & Pharmaceutical Bulletin

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Biomacromolecules (>40 kDa) have been developed as drug delivery system (DDS) carriers of low-molecular weight drugs to promote these drugs' uptake by cancer tissues via enhanced permeability and retention (EPR) effects. Human serum albumin (HSA) has been found to accumulate in cancer tissues via this EPR effect. HSA is the most abundant protein in serum, which performs essential physiological functions such as the transportation of many endogenous and exogenous ligands. Nitric oxide (NO) is a very small ligand of HSA; it is a unique and diffusible molecular messenger that plays a central role in mammalian physiology. Key words human serum albumin; nitric oxide; S-nitrosation; drug delivery system; anticancer activity; enhanced permeability and retention effect HUMAN SERUM ALBUMIN AS THE KEY PLAY-ER IN THE NITRIC OXIDE TRAFFIC SYSTEM IN HUMANSA gas modulator, nitric oxide (NO), plays an important role in the human body.1-7) A small amount of NO is synthesized by endothelial and neuronal NO synthases. Its actions, including the relaxation of vascular smooth muscle, are pleiotropic. 8,9) However, NO can sometimes be cytotoxic. For instance, a large amount of NO inhibits the growth of cancer cells and induces cell death via apoptosis. 10,11) Many studies have identified that the apoptosis of cancer cells (directly) and the inhibition of cancer progression (indirectly) have relevance to NO.12) Unfortunately, the T 1/2 of NO is so extremely short (<5 s) that NO without a carrier cannot be applied as a therapeutic biological agent. Thus, NO releasing compounds with pharmacological activity have been synthesized around the world.For a long-acting and safe NO donor, we examined the possibility of developing a 'NO traffic protein' as a superior NO carrier. This 'NO traffic protein' would include (1) a NO binding protein with the superior efficiency of S-nitrosation, (2) superior stability of the S-nitroso form in human blood, and (3) the superior efficiency of NO transfer in selected cells which require NO. As a candidate for creating such a NO traffic protein, we selected human serum albumin (HSA), because HSA has high biocompatibility and good biodegradability, and because 'endogenous' S-nitrosothiols in serum are largely related to HSA. 13,14) Endogenous HSA has one Snitrosated site at Cys-34 thiol. The endogenous S-nitrosated HSA (SNO-HSA) was named 'Mono-SNO-HSA,' which has significantly superior stability compared with low molecular weight (LMW) S-nitrosothiols.

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Section: Poly-sno-hsa As a Carrier For The Tar-geted Delivery Of No Tmentioning

confidence: 99%

Section: Perspectives Of Poly-sno-hsa As An Anti-cancer Drugmentioning

confidence: 99%

Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers

Ishima

2017

Biological & Pharmaceutical Bulletin

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“…The final concentration was adjusted to 2 mM Poly-SNO-HSA. This sample and that designated HSA were stored at −80°C until use [3]. Protein concentrations were determined by the BCA assay.…”

Section: Synthesis Of Poly-sno-hsamentioning

confidence: 99%

“…We have selected human serum albumin (HSA) as a NO-carrier, because S-nitrosated HSA appears to act as a reservoir of NO in vivo and, therefore, is expected to be a clinically feasible biocompatible pharmacological agent with a long half-life. We have produced poly-S-nitrosated HSA (Poly-SNO-HSA) using a chemical linker such as imminothiolane or N-succinimidyl S-acetylthioacetate, and found that this HSA form can induce apoptosis via activation of the intrinsic apoptosis pathway in murine colon 26 carcinoma (C26) cells and in the rat tumor cell line-LY-80 (a variant of Yoshida sarcoma) both in vivo and in vitro [2,3].…”

Section: Introductionmentioning

confidence: 99%

Elucidation of the therapeutic enhancer mechanism of poly-S-nitrosated human serum albumin against multidrug-resistant tumor in animal models

Ishima

Hara

Kragh‐Hansen

et al. 2012

Journal of Controlled Release

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“…21,22) We previously reported that nitrosylated HSA has an antibiotic effect on bacteria and antitumor effects in human cancer cells. [23][24][25][26][27][28] Therefore, TDI has the potential for serving as a useful carrier of NO compared to the WT molecule.…”

Section: Discussionmentioning

confidence: 99%

Recombinant Human Serum Albumin Containing 3 Copies of Domain I, Has Significant <i>in Vitro</i> Antioxidative Capacity Compared to the Wild-Type

Matsushita

Nishi

Iwao

et al. 2017

Biological & Pharmaceutical Bulletin

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Human serum albumin (HSA), the most abundant protein in serum, functions as carrier of drugs and contributes to maintaining serum colloid osmotic pressure. We report herein on the preparation of a genetic recombinant HSA, in which domains II and III were changed to domain I (triple domain I; TDI). Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) results indicated that the purity of the TDI was equivalent to that of the wild type (WT). Both far-and near-UV circular dichroism (CD) spectra of the TDI showed that its structural characteristics were similar to the WT. Ligand binding capacity was examined by an ultrafiltration method using 3-carboxy-4-methyl-5-propyl-2-furanpropanoic acid (CMPF) and ketoprofen as markers for site I and site II, respectively. The binding capacity of TDI for both ligands was lower than that for the wild type. TDI significantly suppressed the oxidation of dihydrorhodamine 123 (DRD) by H 2 O 2 compared to the WT. Our current results suggest that TDI has great potential for further development as HSA a product having antioxidative functions.

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Nitrosylated human serum albumin (SNO-HSA) induces apoptosis in tumor cells

Cited by 30 publications

References 28 publications

Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers

Albumin-Based Nitric Oxide Traffic System for the Treatment of Intractable Cancers

Elucidation of the therapeutic enhancer mechanism of poly-S-nitrosated human serum albumin against multidrug-resistant tumor in animal models

Recombinant Human Serum Albumin Containing 3 Copies of Domain I, Has Significant <i>in Vitro</i> Antioxidative Capacity Compared to the Wild-Type

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