Action of Ascorbic Acid on a Myosin Molecule Derived from Carp

Ikeuci, Sayaka; Miyamoto, Yuka; Katoh, Tsuyoshi; Nishimura, Kimio

doi:10.1271/bbb.70205

Cited by 8 publications

(4 citation statements)

References 15 publications

(19 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, they suggested a metal ion-free mechanism for generation of the semiquinone radical 16 , consisting of an initiation step involving a noncatalyzed oxidation of the phenolic substance 15 by oxygen to form superoxide anion, followed by a propagation stage involving oxidation of the phenolic substance by superoxide anion as illustrated in Figure 6 . The generation of superoxide anion and hydrogen peroxide is not unique to polyphenols, since even ascorbic acid undergoes such a reaction [ 54 ]. Tyihák et al [ 6 ] reported that the antimicrobial activity of phenolic substances such as cinnamic acid and transresveratrol depends on their generation of singlet oxygen, and this may involve reactions as depicted in Figure 6 .…”

Section: Singlet Oxygen Formation Via the Oxidation Of Phenolic Sumentioning

confidence: 99%

Endogenous Generation of Singlet Oxygen and Ozone in Human and Animal Tissues: Mechanisms, Biological Significance, and Influence of Dietary Components

Onyango

2016

Oxidative Medicine and Cellular Longevity

View full text Add to dashboard Cite

Recent studies have shown that exposing antibodies or amino acids to singlet oxygen results in the formation of ozone (or an ozone-like oxidant) and hydrogen peroxide and that human neutrophils produce both singlet oxygen and ozone during bacterial killing. There is also mounting evidence that endogenous singlet oxygen production may be a common occurrence in cells through various mechanisms. Thus, the ozone-producing combination of singlet oxygen and amino acids might be a common cellular occurrence. This paper reviews the potential pathways of formation of singlet oxygen and ozone in vivo and also proposes some new pathways for singlet oxygen formation. Physiological consequences of the endogenous formation of these oxidants in human tissues are discussed, as well as examples of how dietary factors may promote or inhibit their generation and activity.

show abstract

Section: Singlet Oxygen Formation Via the Oxidation Of Phenolic Sumentioning

confidence: 99%

Endogenous Generation of Singlet Oxygen and Ozone in Human and Animal Tissues: Mechanisms, Biological Significance, and Influence of Dietary Components

Onyango

2016

Oxidative Medicine and Cellular Longevity

View full text Add to dashboard Cite

show abstract

“…Transition metal traces such as Fe 3+ can also be reduced to Fe 2+ and further react with H 2 O 2 through a Fenton mechanism . The resulting radicals may oxidize the sulfhydryl side chains into thiyl radicals(S • ), promoting myosin II aggregation through S–S bonding. , In the presence of excessive V C , the oxidative radicals could be scavenged by V C , and interprotein S–S bonds are reductively cleaved as well, so dissociation of myosin II aggregates is observed in the high-V C regime. In addition, our work shows a V C -induced reversive structural transition in myosin II between α-helices and β-sheets.…”

Section: Discussionmentioning

confidence: 99%

Vitamin C Drives Reentrant Actin Phase Transition: Biphasic Exocytosis Regulation Revealed by Single-Vesicle Electrochemistry

Liu,

Jiang,

Liu

et al. 2024

J. Am. Chem. Soc.

View full text Add to dashboard Cite

Unveiling molecular mechanisms that dominate protein phase dynamics has been a pressing need for deciphering the intricate intracellular modulation machinery. While ions and biomacromolecules have been widely recognized for modulating protein phase separations, effects of small molecules that essentially constitute the cytosolic chemical atmosphere on the protein phase behaviors are rarely understood. Herein, we report that vitamin C (V C ), a key small molecule for maintaining a reductive intracellular atmosphere, drives reentrant phase transitions of myosin II/F-actin (actomyosin) cytoskeletons. The actomyosin bundle condensates dissemble in the low-V C regime and assemble in the high-V C regime in vitro or inside neuronal cells, through a concurrent myosin II protein aggregation−dissociation process with monotonic V C concentration increase. Based on this finding, we employ in situ single-cell and single-vesicle electrochemistry to demonstrate the quantitative modulation of catecholamine transmitter vesicle exocytosis by intracellular V C atmosphere, i.e., exocytotic release amount increases in the low-V C regime and decreases in the high-V C regime. Furthermore, we show how V C regulates cytomembrane-vesicle fusion pore dynamics through counteractive or synergistic effects of actomyosin phase transitions and the intracellular free calcium level on membrane tensions. Our work uncovers the small molecule-based reversive protein phase regulatory mechanism, paving a new way to chemical neuromodulation and therapeutic repertoire expansion.

show abstract

“…Artificially reared Cyprinus carpio and Carassius auratus must be supplemented with VC to grow well. The GULO enzymatic activity in their livers is only 5%–10% that in Oreochroms mossambcus and Gadus morrhua , and 30% that in the mouse liver (Dabrowski, 1991; Ikeuci et al, 2007; Menezes et al, 2016). Our study showed that silkworm eggs, and fat bodies of larva and pupae show activity of the key enzyme GULO in the l ‐gulose pathway for synthesis of AsA, which catalyzes AsA production from l ‐gulonic acid‐γ‐lactone, thus further confirming that silkworms can synthesize AsA.…”

Section: Discussionmentioning

confidence: 99%

Bombyx mori can synthesize ascorbic acid through the l‐gulose pathway to varying degrees depending on developmental stage

Hou

Dai

Liang

et al. 2021

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

Vitamin C (VC) is an essential nutrient for many animals. However, whether insects, including Bombyx mori, can synthesize VC remains unclear. In this article, the optimized HPLC method was used to determine the content of l‐ascorbic acid (AsA) in silkworm eggs, larvae and pupae, and the activity of l‐gulono‐1,4‐lactone oxidase (GULO), a key enzyme in VC synthesis. The RNA interference method was used to determine the effect of the BmGulo‐like gene on embryonic development and GULO activity in the pupal fat body. The AsA content increased significantly during E144 h–E168 h in the late embryonic stage and P48 h–P144 h in the middle‐late pupal stage, in which exogenous VC was not ingested. Furthermore, the body AsA content in larvae fed VC‐free feed also increased with larval stage. The GULO enzymatic activity was present in eggs and the fat bodies of larvae and pupae, even when the larvae were reared with fresh mulberry leaves. Moreover, the activity was higher in the later embryonic stages (E144 h–E168 h) and the early pupal stage (before P24 h). The GULO activity in the pupal fat body dramatically decreased when the screened BmGulo‐like gene (BGIBMGA005735) was knocked down with small interfering RNA; in addition, the survival rate and hatching rate of eggs significantly decreased 21% and 44%, respectively, and embryonic development was delayed. Thus, Bombyx mori can synthesize AsA through the l‐gulose pathway, albeit with low activity, and this synthesis ability varies with developmental stages.

show abstract

Action of Ascorbic Acid on a Myosin Molecule Derived from Carp

Cited by 8 publications

References 15 publications

Endogenous Generation of Singlet Oxygen and Ozone in Human and Animal Tissues: Mechanisms, Biological Significance, and Influence of Dietary Components

Endogenous Generation of Singlet Oxygen and Ozone in Human and Animal Tissues: Mechanisms, Biological Significance, and Influence of Dietary Components

Vitamin C Drives Reentrant Actin Phase Transition: Biphasic Exocytosis Regulation Revealed by Single-Vesicle Electrochemistry

Bombyx mori can synthesize ascorbic acid through the l‐gulose pathway to varying degrees depending on developmental stage

Contact Info

Product

Resources

About