Allosteric Inhibition of Rat Liver Fructose 1,6-Diphosphatase by Adenosine 5'-Monophosphate

Taketa, Kazuhisa; Pogell, Burton M.

doi:10.1016/s0021-9258(17)45224-0

Cited by 500 publications

(58 citation statements)

References 27 publications

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“…Lactate dehydrogenase was estimated by measuring the reduction of NADH into NAD + according to the protocol of King ( King, 1965 ). The activity of fructose-1,6-bisphosphatase (FBPase) was measured according to the method of Taketa and Pogell and 6-phosphogluconate dehydrogenase (6PGD) was measured spectrophotometrically according to the method given by Ben-Bassat and Goldberg ( Taketa and Pogell, 1965 ; Ben-Bassat and Goldberg, 1980 ).…”

Section: Methodsmentioning

confidence: 99%

Modulatory Effect of 4-(methylthio)butyl Isothiocyanate Isolated From Eruca Sativa Thell. on DMBA Induced Overexpression of Hypoxia and Glycolytic Pathway in Sprague-Dawley Female Rats

et al. 2021

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4-(methylthio)butyl isothiocyanate (4-MTBITC) is a hydrolytic product from the plant Eruca sativa Thell. In the present study, we explored the anti-cancer effect of 4-MTBITC against 7,12-dimethylbenz [a] anthracene (DMBA) induced breast cancer. Hypoxic conditions were developed using a single dose of 60 mg/kg DMBA. Hepatic and renal parameters were increased along with antioxidants in cancer-bearing rats which were lowered with the treatment of 4-MTBITC. Further, it inhibited the up-regulation of glycolytic enzymes caused by DMBA. The hypoxia pathway was evaluated using RT-PCR and it was found that the 40 mg/kg doses of 4-MTBITC statistically lowered the expression of HIF-1α. Akt/mTOR signaling pathway was one of the major pathways involved in 4-MTBITC-induced cell growth arrest by western blotting. Amino acid profiling serum-free plasma revealed the downregulation of specific amino acids required for vital components of fast-growing cancer cells. 4-MTBITC reduced the levels of serine, arginine, alanine, asparagines, and glutamic acid. Histological examination also showed neoplastic growth following DMBA doses. 4-MTBITC treated rats showed less infiltration and normal physiology. Our findings for the first time demonstrated the potential therapeutic significance of 4-MTBITC on modulation of glycolytic enzymes and hypoxia pathway in female rats.

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Section: Methodsmentioning

confidence: 99%

Modulatory Effect of 4-(methylthio)butyl Isothiocyanate Isolated From Eruca Sativa Thell. on DMBA Induced Overexpression of Hypoxia and Glycolytic Pathway in Sprague-Dawley Female Rats

et al. 2021

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“…(B) The Hill plot for the data in A (TFP, @; CPZ, O). This form of the Hill equation is derived elsewhere by Taketa and Pogel (43). (C) Reaction progress curves (continuous tracings) demonstrating the effects of TFP on the O2--dependent reduction of ferricytochrome c by neutrophils stimulated with PMA, which was added last to initiate the reactions.…”

Section: Effects Of Phenothiazines and Naphthalene Sulfonamides On 02-releasementioning

confidence: 99%

Release of superoxide and change in morphology by neutrophils in response to phorbol esters: antagonism by inhibitors of calcium-binding proteins.

Robinson¹,

Badwey²,

Karnovsky³

1985

The Journal of Cell Biology

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The ability of phorbol derivatives to function as stimulating agents for superoxide (02-) release by guinea pig neutrophils has been evaluated and compared to the known ability of each compound to activate protein kinase C. Those that activate the kinase also stimulate 02-release, while those that are inactive with respect to the kinase have no effect on 02-release. The same correlation was observed with respect to the ability of phorbol esters to induce morphological changes in neutrophils, i.e., vesiculation and reduction in granule content. Certain phenothiazines and naphthalene sulfonamides that are known antagonists of calcium-binding proteins blocked both phorbol ester-induced O~-release and morphological changes in these cells.

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“…Phosphofructokinase and phosphorylase are catabolic enzymes that are activated by decreased cellular energy status, while FBPase is an anabolic enzyme that is inhibited by decreased cellular energy status. It is interesting that, like AMPK, all three of these energy-sensing metabolic enzymes respond primarily to AMP and ATP, rather than to ADP and ATP [5][6][7].…”

mentioning

confidence: 99%

Keeping the home fires burning: AMP-activated protein kinase

Hardie¹

2018

J. R. Soc. Interface.

152

130

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Living cells obtain energy either by oxidizing reduced compounds of organic or mineral origin or by absorbing light. Whichever energy source is used, some of the energy released is conserved by converting adenosine diphosphate (ADP) to adenosine triphosphate (ATP), which are analogous to the chemicals in a rechargeable battery. The energy released by the conversion of ATP back to ADP is used to drive most energy-requiring processes, including cell growth, cell division, communication and movement. It is clearly essential to life that the production and consumption of ATP are always maintained in balance, and the AMP-activated protein kinase (AMPK) is one of the key cellular regulatory systems that ensures this. In eukaryotic cells (cells with nuclei and other internal membrane-bound structures, including human cells), most ATP is produced in mitochondria, which are thought to have been derived by the engulfment of oxidative bacteria by a host cell not previously able to use molecular oxygen. AMPK is activated by increasing AMP or ADP (AMP being generated from ADP whenever ADP rises) coupled with falling ATP. Relatives of AMPK are found in essentially all eukaryotes, and it may have evolved to allow the host cell to monitor the output of the newly acquired mitochondria and step their ATP production up or down according to the demand. Structural studies have illuminated how AMPK achieves the task of detecting small changes in AMP and ADP, despite the presence of much higher concentrations of ATP. Recently, it has been shown that AMPK can also sense the availability of glucose, the primary carbon source for most eukaryotic cells, via a mechanism independent of changes in AMP or ADP. Once activated by energy imbalance or glucose lack, AMPK modifies many target proteins by transferring phosphate groups to them from ATP. By this means, numerous ATP-producing processes are switched on (including the production of new mitochondria) and ATP-consuming processes are switched off, thus restoring energy homeostasis. Drugs that modulate AMPK have great potential in the treatment of metabolic disorders such as obesity and Type 2 diabetes, and even cancer. Indeed, some existing drugs such as metformin and aspirin, which were derived from traditional herbal remedies, appear to work, in part, by activating AMPK.

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Allosteric Inhibition of Rat Liver Fructose 1,6-Diphosphatase by Adenosine 5'-Monophosphate

Cited by 500 publications

References 27 publications

Modulatory Effect of 4-(methylthio)butyl Isothiocyanate Isolated From Eruca Sativa Thell. on DMBA Induced Overexpression of Hypoxia and Glycolytic Pathway in Sprague-Dawley Female Rats

Modulatory Effect of 4-(methylthio)butyl Isothiocyanate Isolated From Eruca Sativa Thell. on DMBA Induced Overexpression of Hypoxia and Glycolytic Pathway in Sprague-Dawley Female Rats

Release of superoxide and change in morphology by neutrophils in response to phorbol esters: antagonism by inhibitors of calcium-binding proteins.

Keeping the home fires burning: AMP-activated protein kinase

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