A screening procedure for primary aldosteronism based on the Diasorin Liaison automated chemiluminescent immunoassay for direct renin.

BACKGROUND: Primary aldosteronism (PA), the most common secondary cause of hypertension, can be screened for using the aldosterone/renin ratio. This ratio is raised in PA and its accuracy depends on the ability to measure plasma renin at extremely low concentrations. METHODS: We compared two different procedures for assessing plasma renin. The conventional method, which measures plasma renin activity (PRA), is technically demanding and laborious, and the Diasorin Liaison method, which measures plasma renin concentration (PRC), is an automated immunoassay. Results from each method were used to calculate the aldosterone/renin ratio (ARR) and the performance of the Diasorin Liaison method compared with that of the conventional assay using receiver operator characteristic curves. RESULTS: The analytical and functional sensitivity of the PRC method were 2.1 and 5 microIU/mL, respectively. Intra- and inter-assay precision were <7.2% and 10.4%, respectively. There was significant (9%) prorenin interference. Samples with PRA > 1.0 ng/mL/h showed significant correlation with PRC (r = 0.93; P < 0.05; n = 146); however, with PRA < 1.0 ng/mL/h, no significant correlation occurred (r = 0.14; P < 0.05; n = 79). An aldosterone (pmol/L)/PRC(microIU/mL) ratio of >35, in patients with aldosterone >300 pmol/L, resulted in 100% sensitivity and 93% specificity, when compared with the commonly accepted aldosterone (pmol/L)/PRA (ng/mL/h) ratio of >750, in identifying patients who may suffer from PA. CONCLUSION: This study indicates the feasibility of using the automated PRC assay as a replacement for the conventional manual PRA assay in calculating the ARR as a first-line screen for PA.

Regulation of glycogen synthesis by amino acids in cultured human muscle cells.

Insulin and a number of metabolic factors stimulate glycogen synthesis and the enzyme glycogen synthase. Using human muscle cells we find that glycogen synthesis is stimulated by treatment of the cells with lithium ions, which inhibit glycogen synthase kinase 3. Insulin further stimulates glycogen synthesis in the presence of lithium ions, an effect abolished by wortmannin and rapamycin. We report also that amino acids stimulate glycogen synthesis and glycogen synthase, these effects also being blocked by rapamycin and wortmannin. Amino acids stimulate p70(s6k) and transiently inhibit glycogen synthase kinase 3 without effects on the activity of protein kinase B or the mitogen-activated protein kinase pathway. Thus, the work reported here demonstrates that amino acid availability can regulate glycogen synthesis. Furthermore, it demonstrates that glycogen synthase kinase 3 can be inactivated within cells independent of activation of protein kinase B and p90(rsk).