Disease relevance of AMD1

• The effect of hypoxia on the activity of another rate-limiting enzyme in polyamine synthesis, S-adenosylmethionine decarboxylase (AdoMet-DC), also was examined [1].

High impact information on AMD1

• The anti-leukemic agent methylglyoxal bis(guanylhydrazone) (MGBG) blocks synthesis of these polyamines by inhibiting S-adenosylmethionine decarboxylase [2].
• The mRNA encoding S-adenosylmethionine decarboxylase (AdoMetDC) has an unusual distribution in polysomes from cells of T lymphocyte origin [3].
• Isolation of a cDNA clone encoding S-adenosylmethionine decarboxylase. Expression of the gene in mitogen-activated lymphocytes [4].
• In resting lymphocytes, the average size of polysomes containing mRNA coding for S-adenosylmethionine decarboxylase was 1.4 ribosomes per mRNA, and this value increased to 2.7 in stimulated cells [4].
• This insert contained nucleotide sequences coding for amino acid sequences of two of the peptides that were analyzed, thus proving that this cDNA clone codes for S-adenosylmethionine decarboxylase [4].

Biological context of AMD1

• This increase was fully explained by a stabilization of the enzyme, probably caused by the binding of aminoguanidine to the active site of AdoMetDC [5].
• These changes in the rates of SDC synthesis and degradation fully account for the observed biphasic enzyme induction curve [6].
• A second elevation of SDC activity coincided with the entry of the cells into S phase at 24 hours [6].
• Our findings suggest that RA treatment increases the intracellular polyamine concentration of RPE cells via activation of ODC, SAMDC and SAT and that this results in the promotion of RPE cell growth until the cells reach full confluency [7].

Associations of AMD1 with chemical compounds

• Several congeners of methylglyoxal bis(guanylhydrazone) were tested for their ability to inhibit eukaryotic putrescine-activated S-adenosylmethionine decarboxylase (EC 4.1.1.50) and intestinal diamine oxidase (EC 1.4.3.6) [8].
• DNA synthesis was determined by [3H]thymidine incorporation into the acid-insoluble fraction after the addition of an inhibitor of ODC (alpha-difluoromethylornithine [DFMO]) or SAMDC (methylglyoxal bis[guanylhydrazone] [MGBG]) [9].
• Stabilization of S-adenosylmethionine decarboxylase by aminoguanidine [5].
• The enzyme preparation was free from S-adenosylmethionine decarboxylase and spermidine synthase activities [10].

Other interactions of AMD1

• The enzyme preparation was free from S-adenosylmethionine decarboxylase (EC 4.1.1.50) and spermine synthase (EC 2.5.1.22) activities [11].

References