Insulin: Know what your immunoassay detects. Evaluation of two new immunoassays.

Cross-reactivity Diabetes Hypoglycemia Immunoassay Insulin Insulin analogues

Journal

Clinica chimica acta; international journal of clinical chemistry
ISSN: 1873-3492
Titre abrégé: Clin Chim Acta
Pays: Netherlands
ID NLM: 1302422

Informations de publication

Date de publication:
01 Aug 2023
Historique:
received: 02 06 2023
revised: 24 07 2023
accepted: 13 08 2023
medline: 11 9 2023
pubmed: 21 8 2023
entrez: 20 8 2023
Statut: ppublish

Résumé

Insulin is essential for glycemic regulation but diseases can cause a default or an excess of insulin secretion leading to dysregulated glycemia. Hence, measurement of insulinemia is useful to investigate hypoglycemia, determine the pathogenesis of diabetes and evaluate β-cell function. Thus, diabetic patients need supplementation with recombinant human insulin and/or insulin analogues. Analogues have primary sequences different from native human insulin and may not be detected by some immunoassays. The objective of our study was to evaluate new insulin immunoassays by determining their ability to detect different types of human insulin or analogues. This study compared the reactivity of two new insulin immunoassays with five well-established immunoassays on ten commercial insulins. We also measured insulin in blood samples from diabetic or pancreas transplant patients with known treatment. Contrary to recombinant human insulin, there were differences in the specificity to insulin analogues. We distinguished three immunoassay categories: those recognizing all types of insulin such as the non-specific BI-INS-IRMA®, Architect® and Access® immunoassays; those recognizing human insulin only (Cobas®); and those recognizing human insulin and analogues in variable proportions (Liaison XL®, iFlash® and Maglumi®). An accurate biological interpretation of insulinemia relies on knowledge of the specificity of the immunoassay used.

Sections du résumé

BACKGROUND BACKGROUND
Insulin is essential for glycemic regulation but diseases can cause a default or an excess of insulin secretion leading to dysregulated glycemia. Hence, measurement of insulinemia is useful to investigate hypoglycemia, determine the pathogenesis of diabetes and evaluate β-cell function. Thus, diabetic patients need supplementation with recombinant human insulin and/or insulin analogues. Analogues have primary sequences different from native human insulin and may not be detected by some immunoassays. The objective of our study was to evaluate new insulin immunoassays by determining their ability to detect different types of human insulin or analogues.
METHODS METHODS
This study compared the reactivity of two new insulin immunoassays with five well-established immunoassays on ten commercial insulins. We also measured insulin in blood samples from diabetic or pancreas transplant patients with known treatment.
RESULTS RESULTS
Contrary to recombinant human insulin, there were differences in the specificity to insulin analogues. We distinguished three immunoassay categories: those recognizing all types of insulin such as the non-specific BI-INS-IRMA®, Architect® and Access® immunoassays; those recognizing human insulin only (Cobas®); and those recognizing human insulin and analogues in variable proportions (Liaison XL®, iFlash® and Maglumi®).
CONCLUSION CONCLUSIONS
An accurate biological interpretation of insulinemia relies on knowledge of the specificity of the immunoassay used.

Identifiants

pubmed: 37598742
pii: S0009-8981(23)00318-2
doi: 10.1016/j.cca.2023.117516
pii:
doi:

Substances chimiques

Insulin 0

Types de publication

Comparative Study Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

117516

Informations de copyright

Copyright © 2023 Elsevier B.V. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.

Auteurs

Alizee Violin (A)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France. Electronic address: alizee.violin@chu-nantes.fr.

Emmanuel Enard (E)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France.

Justine Blin (J)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France; Nantes Université, CHU Nantes, INSERM U1235, The Enteric Nervous System in Gut and Brain Disorders, IMAD, F-44000 Nantes, France.

Dimitri Paillusson (D)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France.

Antoine Collin (A)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France.

David Guénet (D)

Normandie Univ, UNICAEN, CHU of Caen Normandie, Laboratory of Biochemistry, 14000 Caen, France.

Véronique Raverot (V)

Service de Biochimie et Biologie Moléculaire, Laboratoire de Biologie Médicale Multi-Sites (LBMMS), Hospices Civils de Lyon, Lyon, France.

Kalyane Bach-Ngohou (K)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France; Nantes Université, CHU Nantes, INSERM U1235, The Enteric Nervous System in Gut and Brain Disorders, IMAD, F-44000 Nantes, France.

Damien Masson (D)

Nantes Université, CHU Nantes, Department of Biology, Laboratory of Biochemistry, F-44000 Nantes, France; Nantes Université, CHU Nantes, INSERM U1235, The Enteric Nervous System in Gut and Brain Disorders, IMAD, F-44000 Nantes, France.

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Classifications MeSH