Diethylglyoxal bis(guanylhydrazone), a potent inhibitor of mammalian S-adenosylmethionine decarboxylase. Effects on cell proliferation and polyamine metabolism in L1210 leukemia cells

1993 ◽  
Vol 124 (2) ◽  
pp. 141-147 ◽  
Author(s):  
Fredrik Svensson ◽  
Inger Kockum ◽  
Lo Persson
Keyword(s):  
Cell Proliferation ◽  
Potent Inhibitor ◽  
Leukemia Cells ◽  
Polyamine Metabolism ◽  
L1210 Leukemia ◽  
Adenosylmethionine Decarboxylase

scholarly journals Regulation of S-adenosylmethionine decarboxylase in L1210 leukemia cells. Studies using an irreversible inhibitor of the enzyme

1991 ◽  
Vol 196 (3) ◽  
pp. 551-556 ◽  
Author(s):  
Riccardo AUTELLI ◽  
Louise STJERNBORG ◽  
Alex R. KHOMUTOV ◽  
Radii M. KHOMUTOV ◽  
Lo PERSSON
Keyword(s):  
Leukemia Cells ◽  
L1210 Leukemia ◽  
Irreversible Inhibitor ◽  
Adenosylmethionine Decarboxylase

scholarly journals CGP 48664, a potent and specific S-adenosylmethionine decarboxylase inhibitor: effects on regulation and stability of the enzyme

1997 ◽  
Vol 322 (1) ◽  
pp. 297-302 ◽  
Author(s):  
Fredrik SVENSSON ◽  
Helmut METT ◽  
Lo PERSSON
Keyword(s):  
Potent Inhibitor ◽  
Therapeutic Agents ◽  
Cellular Systems ◽  
Polyamine Metabolism ◽  
Mrna Levels ◽  
Leukaemia Cell Line ◽  
Adenosylmethionine Decarboxylase ◽  
L1210 Cells ◽  
Polyamine Transport ◽  
Mouse Leukaemia

Mammalian S-adenosylmethionine decarboxylase (AdoMetDC) catalyses a regulatory important step in the biosynthesis of polyamines and is a potential target for therapeutic agents against various parasitic diseases and proliferative disorders. In the present study we examined the effects of a newly synthesized AdoMetDC inhibitor, 4-amidinoindan-1-one 2ƀ-amidinohydrazone (CGP 48664), on polyamine metabolism in the mouse leukaemia cell line L1210. Treatment of the cells with 2 ƁM CGP 48664 led to a depletion of cellular spermidine and spermine. The putrescine content, in contrast, was markedly increased. Cells seeded in the presence of the inhibitor showed a significant decrease in growth rate, which was fully reversed by the addition of 2 ƁM spermidine or 1 ƁM spermine. The syntheses of ornithine decarboxylase and AdoMetDC were greatly increased in cells treated with CGP 48664. These increases were not correlated with similar changes in the mRNA levels, indicating the involvement of a translational mechanism. CGP 48664 was demonstrated to be a very poor competitor of spermidine uptake in the L1210 cells. L1210 cells deficient in polyamine transport were as sensitive to the antiproliferative effect of the inhibitor as were the parental cells, indicating that CGP 48664 did not enter the cells by the polyamine transport system. In addition to inhibiting AdoMetDC, CGP 48664 stabilized the enzyme against degradation. In the present study we also demonstrated that aminoguanidine (AMG), which is frequently used in cellular systems to inhibit any action of serum polyamine oxidase, apparently inhibits AdoMetDC by an irreversible mechanism that markedly stabilizes the enzyme against proteolytic degradation. CGP 48664 and the parental compound methylglyoxal bis(guanylhydrazone), which is also a potent inhibitor of AdoMetDC, contain one or two AMG-like moieties; the importance of these residues in the inhibition of AdoMetDC is discussed.

scholarly journals Overexpression of arginine decarboxylase in transgenic plants

1997 ◽  
Vol 325 (2) ◽  
pp. 331-337 ◽  
Author(s):  
Daniel BURTIN ◽  
Anthony J. MICHAEL
Keyword(s):  
Transgenic Plants ◽  
Arginine Decarboxylase ◽  
Polyamine Metabolism ◽  
Morphological Development ◽  
Polyamine Biosynthesis ◽  
Adenosylmethionine Decarboxylase ◽  
Two Generations ◽  
Key Enzyme ◽  
Polyamine Conjugate ◽  
And Control

The activity of arginine decarboxylase (ADC), a key enzyme in plant polyamine biosynthesis, was manipulated in two generations of transgenic tobacco plants. Second-generation transgenic plants overexpressing an oat ADC cDNA contained high levels of oat ADC transcript relative to tobacco ADC, possessed elevated ADC enzyme activity and accumulated 10–20-fold more agmatine, the direct product of ADC. In the presence of high levels of the precursor agmatine, no increase in the levels of the polyamines putrescine, spermidine and spermine was detected in the transgenic plants. Similarly, the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase were unchanged. No diversion of polyamine metabolism into the hydroxycinnamic acid–polyamine conjugate pool or into the tobacco alkaloid nicotine was detected. Activity of the catabolic enzyme diamine oxidase was the same in transgenic and control plants. The elevated ADC activity and agmatine production were subjected to a metabolic/physical block preventing increased, i.e. deregulated, polyamine accumulation. Overaccumulation of agmatine in the transgenic plants did not affect morphological development.

scholarly journals Inhibition of S-adenosylmethionine decarboxylase by inhibitor SAM486A connects polyamine metabolism with p53-Mdm2-Akt/protein kinase B regulation and apoptosis in neuroblastoma

2009 ◽  
Vol 8 (7) ◽  
pp. 2067-2075 ◽  
Author(s):  
Dana-Lynn T. Koomoa ◽  
Tamas Borsics ◽  
David J. Feith ◽  
Craig C. Coleman ◽  
Christopher J. Wallick ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Protein Kinase B ◽  
Polyamine Metabolism ◽  
Adenosylmethionine Decarboxylase

Dieckol attenuates cell proliferation in Molt-4 leukemia cells via modulation of JAK/STAT3 signaling pathway

2021 ◽  
Vol 17 (73) ◽  
pp. 45
Author(s):  
Juandong Wang ◽  
Ai Li ◽  
Li Zhang ◽  
VishnuPriya Veeraraghavan ◽  
SurapaneniKrishna Mohan
Keyword(s):  
Cell Proliferation ◽  
Signaling Pathway ◽  
Leukemia Cells ◽  
Stat3 Signaling ◽  
Stat3 Signaling Pathway
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