Disease relevance of ADSL

• Cloning of a cDNA encoding adenylosuccinate lyase by functional complementation in Escherichia coli [1].

High impact information on ADSL

• When rats are starved, the rate of de novo synthesis of adenine mononucleotide decreases in spleen and liver but not in kidney, suggesting a regulatory role for adenylosuccinase in purine biosynthesis [2].
• Adenylosuccinase activity of rat liver is depressed by prolonged starvation, cortisol administration, high protein diets, and alloxan diabetes [2].
• The recovery of adenylosuccinase activity is equally rapid after refeeding a balanced diet, or corn oil, or glucose, and is not inhibited by injection of glucagon, in contrast to malic enzyme activity [2].
• The low activity of adenylosuccinase in liver of severely starved rats is inconsistent with the proposal (Moss, K. M., and McGivan, J.D. (1975) Biochem. J. 150, 275-283) that the purine nucleotide cycle plays a major role in ammonia production for urea synthesis, at least under these conditions [2].
• Transfectant L cell lines expressing delta 2 exhibited significantly higher ASL activity than those without [3].

Biological context of ADSL

• To test this possibility, we cloned the delta 2 gene on a plasmid, introduced it into mouse cells, and assessed expression and ASL activity in comparison with delta 1 [3].
• Close similarity of the delta 2 gene to mammalian argininosuccinate lyase (ASL)-encoding genes in organization and deduced amino acid sequence of the encoded protein suggested that this gene may encode chicken ASL [3].
• The 4.6 kbp intergenic spacer in the duck locus is 79% identical to the 4 kbp chicken spacer, except for the existence of a 615 bp CR1 element, highly reiterated in the duck genome, 1.8 kbp upstream of the duck ASL/delta 2 gene [4].

Associations of ADSL with chemical compounds

• In conclusion, ADL, CYP450, ovoinhibitor, and PGDS represent the novel targets of estrogen, which regulates the transcriptional activity of these genes [5].
• Four cDNA fragments that displayed dramatic change after estrogen administration were identified as liver adenylosuccinate lyase (ADL), phenobarbital-inducible cytochrome P-450 (CYP450), ovoinhibitor, and glutathione-dependent prostaglandin D2 synthase (PGDS) [5].

References