Disease relevance of Amd1

• The results suggest that sepsis increases ODC and SAMDC activities and putrescine concentrations in enterocytes of the small intestine [1].
• We now show that unlike serum, adenovirus type 5 fails to induce S-adenosylmethionine decarboxylase or polyamine accumulation [2].
• Uptake characteristics and growth-inhibitory effects of methylglyoxal bis(guanylhydrazone) (MGBG), a competitive inhibitor of S-adenosylmethionine decarboxylase, were investigated in 9L rat brain tumor cells and in V79 hamster lung cells [3].
• S-adenosylmethionine decarboxylase activity is decreased in the rat cortex after traumatic brain injury [4].
• The activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase increase in the livers of rats during the acute-phase response to inflammation [5].

High impact information on Amd1

• Ornithine decarboxylase and S-adenosylmethionine decarboxylase activities were measured as the release of 14CO2 from L-[1-14C]ornithine and S-adenosyl-L-[carboxyl-14C]methionine, respectively [6].
• Increases in the activity of S-adenosylmethionine decarboxylase and the content of spermidine were observed 33-37 hr after administration of galactosamine [7].
• Because the subversion of normal cell cycle control is thought to be a crucial event in cancer development, we examined ODC- and AdoMetDC-transformed fibroblasts for alterations in the cell cycle components [8].
• No change in the invasive capacity was observed when the CPAE cells were treated with DFMO and the LC-AH cells with methylglyoxal-bis(guanylhydrazone), an inhibitor of S-adenosylmethionine decarboxylase, which depressed the spermidine and spermine levels but increased the putrescine level in the LC-AH cells [9].
• Pretreatment of 9L cells for 48 hr with 40 microM methylglyoxal bis(guanylhydrazone), a polyamine biosynthesis inhibitor that competitively inhibits S-adenosylmethionine decarboxylase, caused a decrease in the cytotoxicity of AZQ administered without microsomal activation [10].

Chemical compound and disease context of Amd1

• Sepsis stimulated ODC and SAMDC activities and increased putrescine and spermidine concentrations in jejunal mucosa [11].
• Consistent with these results are our findings that S-neplanocylmethionine does not significantly inhibit purified rat prostate or Escherichia coli S-adenosylmethionine decarboxylase and that [carboxy-14C]S-neplanocylmethionine exhibits no substrate activity with either enzyme [12].

Biological context of Amd1

• Two forms of S-adenosylmethionine decarboxylase mRNA (2.1 and about 3.4-3.6 kilobases) are present in human and rodent tissues and may originate from the utilization of two different polyadenylation signals [13].
• Southern blots of rat genomic DNA indicated that the S-adenosylmethionine decarboxylase gene belongs to a multigene family [13].
• In order to understand the structure and regulation of S-adenosylmethionine decarboxylase, cDNA clones encoding this enzyme have been isolated from rat prostate and human fibroblast cDNA libraries [13].
• Comparison of androgen regulation of ornithine decarboxylase and S-adenosylmethionine decarboxylase gene expression in rodent kidney and accessory sex organs [14].
• Now we have isolated another, slightly different AdoMetDC gene from a rat genomic library [15].

Anatomical context of Amd1

• We have shown previously that overexpression of ODC or AdoMetDC alone can induce tumorigenic transformation of rodent fibroblasts [8].
• ODC and AdoMetDC mRNAs were regulated in prostate and seminal vesicles in a coordinate fashion, with the maximal levels reached within 24-48 h of steroid exposure [14].
• The extent of induction was similar for the two gene products, and ODC and AdoMetDC mRNA accumulation occurred primarily in epithelial cells of accessory sex organs, as shown by in situ hybridization studies [14].
• Rats were killed at specific time intervals, over a 12-hour period, and the activities of ODC and SAMDC were measured in the following tissues: liver, kidney, small intestine, brain and skeletal muscle [16].
• S-Adenosylmethionine decarboxylase (AdoMetDC) is a ubiquitous enzyme in eukaryotic cells and responds to a wide variety of stimuli affecting growth [15].

Associations of Amd1 with chemical compounds

• 4. S-Adenosylmethionine decarboxylase activities were increased by administration of methylglyoxal bis(guanylhydrazone) (1,1'-[(methylethanediylidine)dinitrilo]diguanidine) to similar extents in both control and vitamin B-6-deficient animals [17].
• 3. In contrast, the activity of S-adenosylmethionine decarboxylase was not enhanced by pyridoxal phosphate addition even when dialysed extracts were prepared from tissues of young rats suckled by mothers fed on the vitamin B-6-deficient diet [17].
• Studies with actinomycin D showed that SAMDC and ODC activities are regulated at transcription [16].
• Rats fed the diet supplemented with cysteine had increased ODC activity and decreased SAMD activity when compared to rats fed diets supplemented with methionine [18].
• Polyamines were subsequently accumulated in both skeletal muscle fibres, with a rise in putrescine concentration after 2 h, and a fall corresponding to conversion of putrescine to spermidine and spermine by SAMDC [19].

Regulatory relationships of Amd1

• The results contrast with those observed in other rat tissues where SAM-DC is generally induced by treatments that induce ornithine decarboxylase [20].

Other interactions of Amd1

• The findings suggest that the early depletion of hepatic GSH content is prerequisite for and plays a role in the induction of heme oxygenase, ODC and SAMDC [21].
• Regulation of the activity of ornithine decarboxylase and S-adenosylmethionine decarboxylase in mammary gland and liver of lactating rats. Effects of starvation, prolactin and insulin deficiency [22].
• These organisms also had less than 10% of control AdoMetDC activity, and had elevated decarboxy AdoMet (greater than 4000-fold) and AdoMet (up to 50-fold) levels [23].
• So, 1-aminooxy-3-aminopropane is a very weak inhibitor of S-adenosylmethionine decarboxylase and the cellular effects can be correlated primarily with its inhibitory effects on ornithine decarboxylase and spermidine synthase [24].
• Both compounds were good competitive inhibitors and poor substrates of spermine synthase, good substrates of cytosolic polyamine acetyltransferase, inactivators of S-adenosylmethionine decarboxylase and inhibitors of ornithine decarboxylase [25].

Analytical, diagnostic and therapeutic context of Amd1

• Southern blot analyses reveal a complex hybridization pattern suggesting that there are multiple copies of the AdoMetDC gene in the rat genome [26].
• Soleus muscle (consisting mainly of slow-twitching oxidative fibres-STO) and extensor digitorum longus (mainly fast-twitching glycolytic muscle fibres-FTG) were analysed for polyamine content by HPLC, and ODC and SAMDC activity [19].
• ODC and S-adenosylmethionine decarboxylase (SAMDC) activities and putrescine concentrations were increased in isolated jejunal enterocytes 16 h after induction of sepsis by cecal ligation and puncture [1].
• Translation of the mRNA for S-adenosylmethionine decarboxylase was maximal in a lysate which had been substantially freed from polyamines by gel filtration [27].
• The activity of S-adenosylmethionine decarboxylase shows little change following hepatectomy [28].

References