The isolation and purification of a specific “protector” protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system.

Kim, Kanghwa; Kim, Il Han; Lee, Ki-Young; Rhee, Sue Goo; Stadtman, Earl R.

doi:10.1016/s0021-9258(18)68840-4

Cited by 435 publications

(41 citation statements)

References 28 publications

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“…Peroxiredoxins are a class of peroxidase antioxidant enzymes [46,47]. Six members of peroxiredoxins have been identified [46][47][48][49], with Prx1 to Prx5 containing two catalytic cysteines that perform the two-electron reduction of hydrogen peroxide to water [46,47]. Prx6, however, is a unique peroxiredoxin that possesses only one catalytic cysteine and presumably utilizes glutathione to receive the second electron for the two-electron reduction [50,51].…”

Section: Discussionmentioning

confidence: 99%

Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease

Ding

Shults

Gychka

et al. 2021

IJMS

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Alzheimer’s disease is a chronic neurodegenerative disorder and represents the main cause of dementia globally. Currently, the world is suffering from the coronavirus disease 2019 (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), a virus that uses angiotensin-converting enzyme 2 (ACE2) as a receptor to enter the host cells. In COVID-19, neurological manifestations have been reported to occur. The present study demonstrates that the protein expression level of ACE2 is upregulated in the brain of patients with Alzheimer’s disease. The increased ACE2 expression is not age-dependent, suggesting the direct relationship between Alzheimer’s disease and ACE2 expression. Oxidative stress has been implicated in the pathogenesis of Alzheimer’s disease, and brains with the disease examined in this study also exhibited higher carbonylated proteins, as well as an increased thiol oxidation state of peroxiredoxin 6 (Prx6). A moderate positive correlation was found between the increased ACE2 protein expression and oxidative stress in brains with Alzheimer’s disease. In summary, the present study reveals the relationships between Alzheimer’s disease and ACE2, the receptor for SARS-CoV-2. These results suggest the importance of carefully monitoring patients with both Alzheimer’s disease and COVID-19 in order to identify higher viral loads in the brain and long-term adverse neurological consequences.

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Section: Discussionmentioning

confidence: 99%

Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease

Ding

Shults

Gychka

et al. 2021

IJMS

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“…The first Prx was discovered by Kim et al in late 1980s in yeast, in which it protected the enzyme glutamine synthase from oxidation in a system that serendipitously included thiol compounds to generate hydrogen peroxide. 2 The enzyme was first named thiol-specific antioxidant due to its dependence on thiols. 2 The name was then changed to thioredoxin peroxidase as the protein was found to be oxidized by hydrogen peroxide and reduced back by thioredoxin.…”

Section: Introductionmentioning

confidence: 99%

“…2 The enzyme was first named thiol-specific antioxidant due to its dependence on thiols. 2 The name was then changed to thioredoxin peroxidase as the protein was found to be oxidized by hydrogen peroxide and reduced back by thioredoxin. Subsequent studies demonstrated homologous proteins in other species that shared the peroxidase activity, and the term Prx was introduced, which has been widely adopted in the literature.…”

Section: Introductionmentioning

confidence: 99%

The antioxidant enzyme peroxiredoxin and its protective role in neurological disorders

Zhu

Santo

2012

Exp Biol Med (Maywood)

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Peroxiredoxin (Prx) represents a family of sulfhydryl-dependent peroxidases that reduce hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. There are six known mammalian isozymes (Prx1-6), classified as typical 2-Cys, atypical 2-Cys, or 1-Cys Prxs. In addition to their well-established peroxide-scavenging activity, Prxs also participate in the regulation of various cell signaling pathways. Experimental studies provide substantial evidence for a protective role of Prxs in various neurological disorders involving oxidative and inflammatory stress. There is also evidence suggesting a potential benefit of Prxs in certain neurological diseases in human subjects. This review first describes the biochemical properties and molecular regulation of Prxs, then summarizes the major findings on the neuroprotective functions of Prxs and finally discusses the feasibility of using natural compounds, including those from herbal remedies to augment Prx expression to counteract oxidative neurological disorders.

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“…Initially, Prxs were identified according to its ability to protect cells especially proteins from abiotic stress particularly oxidative damage that leads to an increase of ROS 20 . Previously, Prxs was termed as the "protector protein" or "thiol-specific antioxidant" before being name again as Prxs [21][22][23][24] . Five different Prxs genes including sll1621 were found in the genome of Synechocystis PCC 68036.…”

Section: Synechocystis Pcc 6803 Prxii Protein Is Necessary For Improve Growth Of E Coli Under Salt Stressmentioning

confidence: 99%

Molecular Cloning, Expression, and Function of Synechocystis PCC6803 Type II Peroxiredoxin (sll1621) Gene in Escherichia coli Cells under Salinity Stress Conditions

Gaber¹,

Farag²,

Ismail³

et al. 2020

J Pure Appl Microbiol

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Microorganism's cycle exposure to reactive oxidants from internal metabolism and abiotic stress conditions, e.g. oxidative stress, salinity, drought, low temperature, high temperature, and high light. Synechocystis PCC6803 genomes typically encode different types of antioxidant scavenging enzymes including Peroxiredoxins (Prxs). There are five genes similar to Prxs were found inthe Synechocystis PCC 6803 genome. Based on sequence homology analysis of Synechocystis PCC 6803sll1621 gene, it is categorized into type II Prx (PrxII). The presumed amino acid sequence of Synechocystis PCC6803 Prxii protein exhibited identity about 44%-99% to other PrxII proteins from human, plants, algae, and other different cyanobacterial cells. In the last decade, the genetically controllable model organism E. coli has been introduced as a viable biotechnological model for genetically modified microorganisms. The Synechocystis PCC6803 sll1621 gene was overexpressed in pTYB21 expression vector and the resulting was named as pTYB21/sll1621. The pTYB21/sll1621 was overexpressed in Escherichia coli BL21 (DE3) host cell. The overexpressed protein of PrxII gave the recombinant E. coli cells the ability to survive under high concentrations of salinity stress, whereas the viability of wild type cells was completely inhibited at the same high concentrations of salinity stress. In conclusion, the present research documented the expressing of the sll1621 gene into E. coli cells. This result approved the absence of species barrier in relations to the function of Synechocystis PCC 6803 PrxII protein in different microorganism.

show abstract

The isolation and purification of a specific “protector” protein which inhibits enzyme inactivation by a thiol/Fe(III)/O2 mixed-function oxidation system.

Cited by 435 publications

References 28 publications

Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease

Protein Expression of Angiotensin-Converting Enzyme 2 (ACE2) is Upregulated in Brains with Alzheimer’s Disease

The antioxidant enzyme peroxiredoxin and its protective role in neurological disorders

Molecular Cloning, Expression, and Function of Synechocystis PCC6803 Type II Peroxiredoxin (sll1621) Gene in Escherichia coli Cells under Salinity Stress Conditions

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