Amino acid differences in cat adrenocorticotropin account for the inability of a human-based immunoradiometric assay to detect the molecule in cat plasma.

J Vet Diagn Invest

Department of Anatomy, Physiology, and Pharmacology, College of Veterinary Medicine, Auburn University, Auburn, AL

Published: May 2014

A commercial immunoradiometric assay kit designed for the measurement of endogenous adrenocorticotropin (ACTH) concentrations in human plasma does not detect the molecule in plasma samples from cats. It was hypothesized that the inability of the assay to detect the molecule was related to variation(s) in the amino acid sequence of cat ACTH, compared with human ACTH. Cat ACTH complementary DNA was cloned from pituitary tissue and sequenced. The deduced structure showed amino acid differences from the human molecule with cat ACTH having a valine instead of alanine at amino acid 32 and a threonine instead of alanine at amino acid 34. Cat and human ACTH were synthesized along with 2 modified peptides containing alanine substitutions at cat ACTH 32 and 34. Only the human ACTH was detected using the commercial kit, indicating that an epitope recognized by one of the antibodies in the assay requires the presence of 2 alanines near the C-terminus of the molecule.

Download full-text PDF

Source
http://dx.doi.org/10.1177/1040638714528501DOI Listing

Publication Analysis

Top Keywords

amino acid
20
cat acth
16
detect molecule
12
human acth
12
acid differences
8
immunoradiometric assay
8
assay detect
8
molecule cat
8
acth
8
alanine amino
8

Similar Publications

Unlabelled: This study investigated the anticancer phytocompounds in leaf extracts of Kunth. Quantitative analysis of the phytochemical composition showed high levels of primary metabolites: carbohydrates (45.11 ± 2.

View Article and Find Full Text PDF

Unlabelled: Variably protease-sensitive prionopathy (VPSPr) is a rare, atypical subtype of prion disease in which many patients exhibit a family history of dementia. Rare protein-coding variants in , which are causal for all known forms of genetic prion disease, have been ruled out in all VPSPr cases to date, leading to suspicion that VPSPr could be caused by variants in other genes or by non-coding variation in or near . We performed exome sequencing and targeted sequencing of non-coding regions on genomic DNA from autopsy-confirmed VPSPr patients (N=67) in order to search for a possible genetic cause.

View Article and Find Full Text PDF

Cross-reactivity of anti-modified protein antibodies in rheumatoid arthritis.

Clin Exp Rheumatol

December 2024

Department of Rheumatology and Immunology, West China Hospital, Sichuan University, Chengdu, and Clinical Institute of Inflammation and Immunology (CIII), Frontiers Science Centre for Disease-related Molecular Network, West China Hospital, Sichuan University, Chengdu, Sichuan, China.

This review comprehensively discusses the cross-reactivity of autoantibodies against modified proteins (AMPAs), the hallmark of rheumatoid arthritis (RA). We found that regardless of tissue sources, subtypes, or isotypes of B cells, AMPAs show high cross-reactivity within and across antigens undergoing citrullination, carbamylation, lysine-acetylation or ornithine-acetylation. The cross-reactive patterns of AMPAs display clonal and individual heterogeneity.

View Article and Find Full Text PDF

Food allergies are pathological adverse reactions against harmless dietary proteins. While studies have shown the involvement of host metabolic changes (, lipid metabolism and amino acid metabolism) in the development of food allergy (FA), the adaptive changes in glucose metabolism induced by food allergen exposure remain largely unclear. In this study, BALB/c mice were sensitized intraperitoneally with an ovalbumin (OVA)/aluminum adjuvant, followed by oral OVA challenges to induce anaphylaxis.

View Article and Find Full Text PDF

AlphaFold-guided molecular replacement for solving challenging crystal structures.

Acta Crystallogr D Struct Biol

January 2025

Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA.

Molecular replacement (MR) is highly effective for biomolecular crystal structure determination, increasingly so as the database of known structures has increased. For candidates without recognizable similarity to known structures, however, crystal structure analyses have nearly always required experiments for de novo phase evaluation. Now, with the unprecedented accuracy of AlphaFold predictions of protein structures from amino-acid sequences, an appreciable expansion of the reach of MR for proteins is realized.

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!