S-100 proteins: basics and applications as biomarkers in animals with special focus on calgranulins (S100A8, A9, and A12)

Ceron Madrigal, J. J., Ortín-Bustillo, A., López-Martínez, M. J., Martínez-Subiela, S., Eckersall, P. D. , Tecles, F., Tvarijonaviciute, A. and Muñoz-Prieto, A. (2023) S-100 proteins: basics and applications as biomarkers in animals with special focus on calgranulins (S100A8, A9, and A12). Biology, 12(6), 881. (doi: 10.3390/biology12060881) (PMID:37372165) (PMCID:PMC10295460)

Abstract

S100 proteins are a group of calcium-binding proteins which received this name because of their solubility in a 100% saturated solution of ammonium sulphate. They have a similar molecular mass of 10–12 KDa and share 25–65% similarity in their amino acid sequence. They are expressed in many tissues, and to date 25 different types of S100 proteins have been identified. This review aims to provide updated information about S100 proteins and their use as biomarkers in veterinary science, with special emphasis on the family of calgranulins that includes S100A8 (calgranulin A; myeloid-related protein 8, MRP8), S100A9 (calgranulin B; MRP14), and S100A12 (calgranulin C). The proteins SA100A8 and S100A9 can be linked, forming a heterodimer which is known as calprotectin. Calgranulins are related to the activation of inflammation and the immune system and increase in gastrointestinal diseases, inflammation and sepsis, immunomediated diseases, and obesity and endocrine disorders in different animal species. This review reflects the current knowledge about calgranulins in veterinary science, which should increase in the future to clarify their role in different diseases and potential as biomarkers and therapeutic targets, as well as the practical use of their measurement in non-invasive samples such as saliva or feces.

• Item Type: Articles
• Additional Information: This study was supported by a Grant Reference PID2019-105950RB-100 funded by MCIN/AEI/10.13039/501100011033. It was also supported by a Grant Reference PCI2020-120712-2 from MCIN/AEI/10.13039/501100011033 and European Union “NextGenerationEU”/PRTR (1st ICRAD Joint Cofund Call). M.J.L.-M. was funded by 21293/FPI/19, Fundación Séneca, Región de Murcia (Spain). A.O.-B. was funded by a pre-doctoral grant from the Seneca Foundation of Murcia Regional Government, Spain (21603/FPI/21). A.M.-P. has a post-doctoral fellowship “Ramón y Cajal” supported by the Ministerio de Ciencia e Innovación, Agencia Estatal de Investigación (AEI), Spain, and The European Next Generation Funds (NextgenerationEU) (RYC2021-033660-I).
• Status: Published
• Refereed: Yes
• Glasgow Author(s) Enlighten ID: Ceron Madrigal, Professor Jose and Eckersall, Professor David
• Authors: Ceron Madrigal, J. J., Ortín-Bustillo, A., López-Martínez, M. J., Martínez-Subiela, S., Eckersall, P. D., Tecles, F., Tvarijonaviciute, A., and Muñoz-Prieto, A.
• College/School: College of Medical Veterinary and Life Sciences > School of Biodiversity, One Health & Veterinary Medicine
• Journal Name: Biology
• Publisher: MDPI
• ISSN: 2079-7737
• ISSN (Online): 2079-7737
• Published Online: 19 June 2023
• Copyright Holders: Copyright © 2023 The Authors
• First Published: First published in Biology 12(6): 881
• Publisher Policy: Reproduced under a Creative Commons License