Changes in S100A8/A9 and S100A12 and Their Comparison with Other Analytes in the Saliva of Pigs with Diarrhea Due to E. coli

Author:

Ortín-Bustillo Alba1,Botía María1ORCID,López-Martínez María José1ORCID,Martínez-Subiela Silvia1ORCID,Cerón José Joaquín1,González-Bulnes Antonio23,Manzanilla Edgar García45ORCID,Goyena Elena6,Tecles Fernando1,Muñoz-Prieto Alberto1ORCID

Affiliation:

1. Interdisciplinary Laboratory of Clinical Analysis of the University of Murcia (INTERLAB-UMU), Department of Animal Medicine and Surgery, Veterinary School, Regional Campus of International Excellence Mare Nostrum, University of Murcia, Espinardo, 30100 Murcia, Spain

2. Departamento de Producción y Sanidad Animal, Facultad de Veterinaria, Universidad Cardenal Herrera-CEU, CEU Universities, C/Tirant lo Blanc, 7, Alfara del Patriarca, 46115 Valencia, Spain

3. Cuarte S.L. Grupo Jorge, Ctra. De Logroño, Km 9,2., Monzalbarba, 50120 Zaragoza, Spain

4. Pig Development Department, The Irish Food and Agriculture Authority, Teagasc, Moorepark, P61 C996 Fermoy, Ireland

5. School of Veterinary Medicine, University College Dublin, Belfield, D04 W6F6 Dublin, Ireland

6. Department of Animal Health, Faculty of Veterinary Medicine, University of Murcia, 30100 Murcia, Spain

Abstract

The family of calgranulins includes S100A8 (calgranulin A), S100A9 (calgranulin B), which can appear as a heterodimer known as S100A8/A9 or calprotectin, and S100A12 (calgranulin C). These proteins are related to different inflammatory conditions, immune-mediated diseases, and sepsis and are considered biomarkers of potential interest. This study aims to evaluate if S100A8/A9 and A12 could change in pigs with diarrhea due to E. coli and to compare the changes of S100A8/A9 and A12 with other analytes in order to explore the possible causes or mechanisms involved. For this purpose, a panel integrated by analytes related to inflammation (haptoglobin, inter-alpha trypsin inhibitor 4 (ITIH4), and total protein); immune system (adenosine deaminase, ADA); stress (alpha-amylase); tissue damage (lactate and lactate dehydrogenase (LDH)); sepsis (aldolase) and redox status (ferric-reducing ability of saliva (FRAS) and advanced oxidation protein products (AOPP)) was evaluated. S100A8/A9 and A12 and the other analytes measured in this study showed increases in the saliva of pigs with diarrhea due to E. coli. S100A8/A9 and/or A12 showed a significant correlation of different magnitude with some of the other analytes evaluated. Further studies should be conducted to gain knowledge about the possible practical applications as biomarkers of the measurements of S100A8/A9 and A12 in the saliva of pigs.

Publisher

MDPI AG

Subject

General Veterinary,Animal Science and Zoology

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