Disease relevance of Asl

• Using antibody and plaque hybridization screening, we isolated rat argininosuccinate lyase (AS lyase) cDNA clones from a liver cDNA library prepared in the phage expression vector lambda gt11 [1].
• Molecular cloning of cDNA for rat argininosuccinate lyase and its expression in rat hepatoma cell lines [1].

High impact information on Asl

• Citrulline, which is the coproduct of NOS-catalyzed metabolism of arginine, can be recycled to arginine by the action of argininosuccinate synthetase and argininosuccinate lyase, which are present at high levels in hepatocytes and renal tubular cells but normally at very low levels in other cell types such as macrophages [2].
• Regional localization of the mouse argininosuccinate lyase gene to chromosome 5 [3].
• However, only argininosuccinate lyase mRNA exhibits any significant change in abundance at birth, resembling postnatal expression of tyrosine aminotransferase mRNA [4].

Associations of Asl with chemical compounds

• Argininosuccinate synthetase and argininosuccinate lyase catalyze the conversion of citrulline to arginine in kidney [5].
• Circulating arginine available for synthesis of protein is produced in the kidney of the adult mammal by the action of the last two enzymes of the urea cycle, argininosuccinate synthase and argininosuccinate lyase [6].
• Mice homozygous for the c3H deletion, shown previously to have drastically reduced mRNA levels for phosphoenolpyruvate carboxykinase in the liver, expressed the same deficiency in the kidney, while mRNA levels for argininosuccinate synthetase and argininosuccinate lyase were reduced in the liver but remained unaffected in the kidney [7].

References