Quality control serum samples and postdexamethasone plasma pools were used to compare 16 commercial cortisol radioimmunoassay kits with the competitive protein-binding assay for plasma glucocorticoids that we used to standardize the dexamethasone suppression test (DST). Thirteen radioimmunoassays gave higher criterion values for the DST than those established using the competitive protein-binding assay. The range of radioimmunoassay criterion values was 4.34 to 8.70 mu mg/dL. Possible explanations are given for these findings, and their importance to the clinical utility of the DST are emphasized. Each laboratory should validate its own criterion cortisol value for depression based on local data, including appropriate control groups.

Download full-text PDF

Source
http://dx.doi.org/10.1001/archpsyc.1985.01790280075007DOI Listing

Publication Analysis

Top Keywords

competitive protein-binding
12
dexamethasone suppression
8
suppression test
8
protein-binding assay
8
criterion values
8
plasma cortisol
4
cortisol determination
4
determination dexamethasone
4
test comparison
4
comparison competitive
4

Similar Publications

Alzheimer's disease (AD) is a neurodegenerative disease that primarily affects the elderly population and is the leading cause of dementia. Meanwhile, the vascular hypothesis suggests that vascular damage occurs in the early stages of the disease, leading to neurodegeneration and hindered waste clearance, which in turn triggers a series of events including the accumulation of amyloid plaques and Tau protein tangles. Non-coding RNAs (ncRNAs), including long noncoding RNAs (lncRNAs), microRNAs (miRNAs), and circular RNAs (circRNAs), have been found to be involved in the regulation of AD.

View Article and Find Full Text PDF

Each human genome has approximately 5 million DNA variants. Even for complete loss-of-function variants causing inherited, monogenic diseases, current understanding based on gene-specific molecular function does not adequately predict variability observed between people with identical mutations or fluctuating disease trajectories. We present a parallel paradigm for loss-of-function variants based on broader consequences to the cell when aberrant polypeptide chains of amino acids are translated from mutant RNA to generate mutated proteins.

View Article and Find Full Text PDF
Article Synopsis
  • The TRAMP complex is crucial for RNA processing and features two key enzymatic activities that involve both polyadenylation and unwinding of RNA.
  • New research using hydrogen-deuterium exchange data reveals insights into how TRAMP assembles and shuffles RNA between its catalytic sites, which are not fully understood.
  • Findings indicate that peripheral RNA-recognition motifs affect TRAMP assembly and that different active-site subunits interact with tRNA in ways that influence RNA transfer between TRAMP components.
View Article and Find Full Text PDF

Small molecules targeting the eubacterial β-sliding clamp discovered by combined and screening approaches.

J Enzyme Inhib Med Chem

December 2025

Laboratory of Biochemistry and Molecular Biology, Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, Parma, Italy.

Antibiotic resistance stands as the foremost post-pandemic threat to public health. The urgent need for new, effective antibacterial treatments is evident. Protein-protein interactions (PPIs), owing to their pivotal role in microbial physiology, emerge as novel and attractive targets.

View Article and Find Full Text PDF

Structural and kinetic characterization of DUSP5 with a Di-phosphorylated tripeptide substrate from the ERK activation loop.

Front Chem Biol

August 2024

Center for Structure-based Drug Design and Development, Department of Pharmaceutical Sciences, Concordia University Wisconsin, Mequon, WI, United States.

Introduction: Dual specific phosphatases (DUSPs) are mitogen-activated protein kinase (MAPK) regulators, which also serve as drug targets for treating various vascular diseases. Previously, we have presented mechanistic characterizations of DUSP5 and its interaction with pERK, proposing a dual active site.

Methods: Herein, we characterize the interactions between the DUSP5 phosphatase domain and the pT-E-pY activation loop of ERK2, with specific active site assignments.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!