Effects of .ALPHA.1-Acid Glycoprotein on Erythrocyte Deformability and Membrane Stabilization.

Matsumoto, Kazuaki; Nishi, Katsuhide; Tokutomi, Yoshiko; Irie, Tetsumi; Suenaga, Atsushi; Otagiri, Masaki

doi:10.1248/bpb.26.123

Cited by 13 publications

(7 citation statements)

References 16 publications

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“…After incubation, the changes in human erythrocyte deformability were measured using a MCFAN KH-3 micro-channel system (MC Laboratories, Tokyo). 17,21) The deformability of human erythrocytes was expressed in s as the passing time of 100 ml of sample solution.…”

Section: Methodsmentioning

confidence: 99%

Antioxidant Combination Inhibits Reactive Oxygen Species Mediated Damage

Yanai

Shiotani

Hagiwara

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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We examined the preventive activity of naturally occurring antioxidants against three reactive oxygen species using a protein degradation assay. The hydroxyl, hypochlorite, and peroxynitrite radicals are typical reactive oxygen species generated in human body. Previously, we found that hydrophobic botanical antioxidants exhibited specific antioxidant activity against hydroxyl radicals, whereas anserine and carnosine mixture, purified from chicken extract and vitamin C, exhibited antioxidant activities against hypochlorite and peroxynitrite radicals respectively. Since ethanol, used as a solvent in the experiments, also showed an antioxidant action against the hydroxyl radical, we reassessed antioxidant activities using aqueous solutions of botanical antioxidants. Among the seven hydrophobic antioxidants examined, ferulic acid exhibited the strongest antioxidant activity against the hydroxyl radical. An antioxidant preparation of anserine-carnosine mixture, vitamin C, and ferulic acid prevented oxidative stress by reactive oxygen species. Loss of deformability in human erythrocytes and protein degradation caused by reactive oxygen species were completely inhibited.Key words: antioxidant combination; reactive oxygen species; anserine-carnosine; VC; VE Reactive oxygen species (ROS) markedly influence aging and the occurrence of chronic diseases such as diabetes, hypertension, arteriosclerosis, and cancer.

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Section: Methodsmentioning

confidence: 99%

Antioxidant Combination Inhibits Reactive Oxygen Species Mediated Damage

Yanai

Shiotani

Hagiwara

et al. 2008

Bioscience, Biotechnology, and Biochemistry

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“…[122,123] Furthermore, We demonstrated that human, dog and bovine AGPs are able to stabilize the erythrocyte membrane by binding to the surface of the erythrocyte. [124] At physiological concentrations, AGP protects erythrocytes from H 2 O 2 due to its antioxidant activity. [124,125] According to these reports, an increase in the AGP content in serum above the normal value found under pathological conditions facilitates the passage of erythrocytes through capillaries, stabilizes erythrocyte membranes and protects against oxidative stress, all of which are favorable properties for the microcirculation.…”

Section: Biological Functionsmentioning

confidence: 99%

Molecular Aspects of Human Alpha-1 Acid Glycoprotein — Structure and Function

Taguchi¹,

Nishi²,

Chuang³

et al. 2013

Acute Phase Proteins

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“…Indeed, there are reports that AGP interacts with leukocytes and then exhibit various pharmacological actions 11. In addition, AGP binds to the erythrocyte surface, and then stabilizes the membrane 73–75. These findings indicate that interactions of AGP with biomembranes are important for exhibiting its biological functions.…”

Section: Discussionmentioning

confidence: 95%

Involvement of disulfide bonds and histidine 172 in a unique β‐sheet to α‐helix transition of α₁‐acid glycoprotein at the biomembrane interface

et al. 2006

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Human alpha(1)-acid glycoprotein (AGP), which is comprised of 183 amino acid residues and 5 carbohydrate chains, is a major plasma protein that binds to basic and neutral drugs as well as to steroid hormones. It has a beta-sheet-rich structure in aqueous solution. Our previous findings suggest that AGP forms an alpha-helix structure through an interaction with biomembranes. We report herein on a study of the mechanism of alpha-helix formation in AGP using various modified AGPs. The disulfide reduced AGP (R-AGP) was extensively unfolded, whereas asialylated AGP (A-AGP) maintained the native structure. Intriguingly, reduced and asialylated AGP (RA-AGP) increased the alpha-helix content as observed in the presence of biomembrane models, and showed a significant decrease in ligand binding capacity. This suggests that AGP has an innate tendency to form an alpha-helix structure, and disulfide bonds are a key factor in the conformational transition between the beta-sheet and alpha-helix structures. However, RA-AGP with all histidine residues chemically modified (HRA-AGP) was found to lose the intrinsic ability to form an alpha-helix structure. Furthermore, disulfide reduction of the H172A mutant expressed in Pichia pastoris also caused a similar loss of folding ability. The present results indicate that disulfide bonds and the C-terminal region, including H172 of AGP, play important roles in alpha-helix formation in the interaction of the protein with biomembranes.

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Effects of .ALPHA.1-Acid Glycoprotein on Erythrocyte Deformability and Membrane Stabilization.

Cited by 13 publications

References 16 publications

Antioxidant Combination Inhibits Reactive Oxygen Species Mediated Damage

Antioxidant Combination Inhibits Reactive Oxygen Species Mediated Damage

Molecular Aspects of Human Alpha-1 Acid Glycoprotein — Structure and Function

Involvement of disulfide bonds and histidine 172 in a unique β‐sheet to α‐helix transition of α₁‐acid glycoprotein at the biomembrane interface

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Effects of .ALPHA.1-Acid Glycoprotein on Erythrocyte Deformability and Membrane Stabilization.

Cited by 13 publications

References 16 publications

Antioxidant Combination Inhibits Reactive Oxygen Species Mediated Damage

Antioxidant Combination Inhibits Reactive Oxygen Species Mediated Damage

Molecular Aspects of Human Alpha-1 Acid Glycoprotein — Structure and Function

Involvement of disulfide bonds and histidine 172 in a unique β‐sheet to α‐helix transition of α1‐acid glycoprotein at the biomembrane interface

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Product

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Involvement of disulfide bonds and histidine 172 in a unique β‐sheet to α‐helix transition of α₁‐acid glycoprotein at the biomembrane interface