Monitoring the Glutathione Redox Reaction in Living Human Cells by Combining Metabolic Labeling with Heteronuclear NMR

2016 ◽  
Vol 128 (28) ◽  
pp. 8071-8074 ◽  
Author(s):  
Xing Jin ◽  
Soeun Kang ◽  
Shinya Tanaka ◽  
Sunghyouk Park
Keyword(s):  
Redox Reaction ◽  
Heteronuclear Nmr ◽  
Human Cells ◽  
Metabolic Labeling ◽  
Glutathione Redox

scholarly journals Metabolic labeling of human cells with tritiated nucleosides results in activation of the ATM-dependent p53 signaling pathway and acceleration of DNA repair

Oncogene ◽  
2003 ◽  
Vol 22 (36) ◽  
pp. 5562-5571 ◽  
Author(s):  
Razmik Mirzayans ◽  
Scott Pollock ◽  
April Scott ◽  
Cindy Q Gao ◽  
David Murray
Keyword(s):  
Dna Repair ◽  
Signaling Pathway ◽  
Human Cells ◽  
Metabolic Labeling ◽  
P53 Signaling ◽  
P53 Signaling Pathway

scholarly journals Characterization of the human c-fms gene product and its expression in cells of the monocyte-macrophage lineage.

1985 ◽  
Vol 5 (12) ◽  
pp. 3458-3466 ◽  
Author(s):  
J Woolford ◽  
V Rothwell ◽  
L Rohrschneider
Keyword(s):  
Rabbit Antiserum ◽  
Growth Factor Receptor ◽  
Protein Product ◽  
Human Cells ◽  
Cell Protein ◽  
Bewo Cell ◽  
Metabolic Labeling ◽  
Bewo Cells ◽  
Human Choriocarcinoma Cells

The McDonough strain of feline sarcoma virus contains an oncogene called v-fms whose ultimate protein product (gp140v-fms) resembles a cell surface growth factor receptor. To identify and characterize the protein product of the proto-oncogene c-fms, antisera were prepared to the viral fms sequences and used to detect specific cross-reacting sequences in human choriocarcinoma cells (BeWo) known to express c-fms mRNA. Both tumor-bearing rat sera and a rabbit antiserum prepared to a segment of v-fms expressed in Escherichia coli detected a 140-kilodalton (kDa) glycoprotein in the BeWo cells. Tryptic fingerprint analysis of [35S]methionine-labeled proteins indicated that the viral fms proteins and the 140-kDa BeWo cell protein were highly related. This 140-kDa glycoprotein contained an associated tyrosine kinase activity in vitro and was labeled principally on serine after 32Pi metabolic labeling. These results suggest that the 140-kDa protein in BeWo cells is the protein product of the human c-fms proto-oncogene. This conclusion is supported by the finding that a similar protein is detectable only in other human cells that express c-fms mRNA. These other human cells include adherent monocytes and the cell line ML-1, which can be induced to differentiate along the monocyte-macrophage pathway. This is in agreement with current thought that the c-fms proto-oncogene product functions as the CSF-1 receptor specific to this pathway.

Switching of fluorescence mediated by a peroxynitrite–glutathione redox reaction in a porous silicon nanoreactor

2012 ◽  
Vol 14 (15) ◽  
pp. 5251 ◽  
Author(s):  
Beniamino Sciacca ◽  
Stephanie Pace ◽  
Paola Rivolo ◽  
Francesco Geobaldo
Keyword(s):  
Porous Silicon ◽  
Redox Reaction ◽  
Glutathione Redox

scholarly journals Deletion of the lactoperoxidase gene causes multisystem inflammation and tumors in mice

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jayden Yamakaze ◽  
Zhe Lu
Keyword(s):  
Redox Reaction ◽  
Human Cells ◽  
Mutant Mice ◽  
Biological Role ◽  
Protective Mechanism ◽  
Enzymatic Mechanism ◽  
High Incidence ◽  
Cultured Human Cells

AbstractStrongly oxidative H2O2 is biologically important, but if uncontrolled, would lead to tissue injuries. Lactoperoxidase (LPO) catalyzes the redox reaction of reducing highly reactive H2O2 to H2O while oxidizing thiocyanate (SCN−) to relatively tissue-innocuous hypothiocyanite (OSCN−). SCN− is the only known natural, effective reducing-substrate of LPO; humans normally derive SCN− solely from food. While its enzymatic mechanism is understood, the actual biological role of the LPO-SCN− system in mammals remains unestablished. Our group previously showed that this system protected cultured human cells from H2O2-caused injuries, a basis for the hypothesis that general deficiency of such an antioxidative mechanism would lead to multisystem inflammation and tumors. To test this hypothesis, we globally deleted the Lpo gene in mice. The mutant mice exhibited inflammation and lesions in the cardiovascular, respiratory, digestive or excretory systems, neuropathology, and tumors, with high incidence. Thus, this understudied LPO-SCN− system is an essential protective mechanism in vivo.

Characterization of the human c-fms gene product and its expression in cells of the monocyte-macrophage lineage

1985 ◽  
Vol 5 (12) ◽  
pp. 3458-3466
Author(s):  
J Woolford ◽  
V Rothwell ◽  
L Rohrschneider
Keyword(s):  
Rabbit Antiserum ◽  
Growth Factor Receptor ◽  
Protein Product ◽  
Human Cells ◽  
Cell Protein ◽  
Bewo Cell ◽  
Metabolic Labeling ◽  
Bewo Cells ◽  
Human Choriocarcinoma Cells

The McDonough strain of feline sarcoma virus contains an oncogene called v-fms whose ultimate protein product (gp140v-fms) resembles a cell surface growth factor receptor. To identify and characterize the protein product of the proto-oncogene c-fms, antisera were prepared to the viral fms sequences and used to detect specific cross-reacting sequences in human choriocarcinoma cells (BeWo) known to express c-fms mRNA. Both tumor-bearing rat sera and a rabbit antiserum prepared to a segment of v-fms expressed in Escherichia coli detected a 140-kilodalton (kDa) glycoprotein in the BeWo cells. Tryptic fingerprint analysis of [35S]methionine-labeled proteins indicated that the viral fms proteins and the 140-kDa BeWo cell protein were highly related. This 140-kDa glycoprotein contained an associated tyrosine kinase activity in vitro and was labeled principally on serine after 32Pi metabolic labeling. These results suggest that the 140-kDa protein in BeWo cells is the protein product of the human c-fms proto-oncogene. This conclusion is supported by the finding that a similar protein is detectable only in other human cells that express c-fms mRNA. These other human cells include adherent monocytes and the cell line ML-1, which can be induced to differentiate along the monocyte-macrophage pathway. This is in agreement with current thought that the c-fms proto-oncogene product functions as the CSF-1 receptor specific to this pathway.

Monitoring dynamic changes of glutathione redox state in subcellular compartments of human cells – an approach based on rxYFP biosensor

2014 ◽  
Vol 75 ◽  
pp. S33 ◽  
Author(s):  
Agata Banach-Latapy ◽  
Tiantian He ◽  
Michèle Dardalhon ◽  
Laurence Vernis ◽  
Roland Chanet ◽  
...  
Keyword(s):  
Redox State ◽  
Human Cells ◽  
Dynamic Changes ◽  
Subcellular Compartments ◽  
Glutathione Redox

Alpha-Tocopherol Protects Cultured Human Cells from the Acute Lethal Cytotoxicity of Dioxin

2002 ◽  
Vol 72 (3) ◽  
pp. 147-153 ◽  
Author(s):  
Kei-Ichi Hirai ◽  
Jie-Hong Pan ◽  
Ying-Bo Shui ◽  
Eriko Simamura ◽  
Hiroki Shimada ◽  
...  
Keyword(s):  
Cell Death ◽  
Cell Damage ◽  
Smooth Endoplasmic Reticulum ◽  
Dehydroascorbic Acid ◽  
Human Cells ◽  
Alpha Tocopherol ◽  
Cervical Cancer Cells ◽  
Cultured Human Cells ◽  
Nuclear Damage ◽  
Conjunctival Epithelial Cells

The possible protection of cultured human cells from acute dioxin injury by antioxidants was investigated. The most potent dioxin, 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), caused vacuolization of the smooth endoplasmic reticulum and Golgi apparatus in cultured human conjunctival epithelial cells and cervical cancer cells. Subsequent nuclear damage included a deep irregular indentation resulting in cell death. A dosage of 30–40 ng/mL TCDD induced maximal intracellular production of H2O2 at 30 minutes and led to severe cell death (0–31% survival) at two hours. A dose of 1.7 mM alpha-tocopherol or 1 mM L-dehydroascorbic acid significantly protected human cells against acute TCDD injuries (78–97% survivals), but vitamin C did not provide this protection. These results indicate that accidental exposure to fatal doses of TCDD causes cytoplasmic free radical production within the smooth endoplasmic reticular systems, resulting in severe cytotoxicity, and that vitamin E and dehydroascorbic acid can protect against TCDD-induced cell damage.

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