Abstract
Protein glycosylation is a post-translational modification that impacts on protein activity, stability, and interactions. It was sensitively altered by the cellular state and, therefore, is now used for a diagnostic or prognostic indicator of various human diseases such as cancer. To evaluate the clinical feasibility in the veterinary area, the N-glycan biomarkers were discovered from canine serum for the diagnosis of osteoarthritis (OA), which is one of the most common diseases of dogs. N-glycome was obtained from 20 μL of canine serum by the enzymatic cleavage followed by the purification and enrichment using solid-phase extraction. Independent compositions of 163 and 463 N-glycans were found from healthy control (n = 41) and osteoarthritis patients (n = 92), respectively. Initially, 31 of the potential biomarkers were screened by the p-values below 1.0 × 10−10 from ANOVA. Then, the area under the curve (AUC) and the intensity ratio between OA patient and healthy control (P/C ratio) were calculated. Considering the diagnostic efficacy, the AUC bigger than 0.9 and the P/C ratio larger than 3.0 were used to discover 16 N-glycans as diagnostic biomarkers. Particularly, five of the diagnostic biomarkers were AUC above 0.99 and three of N-glycans had AUC 1.0. The results suggest a clear possibility for N-glycan biomarkers to be used as a clinical tool in the veterinary medical area enabling to provide objective and non-invasive diagnostic information.
Highlights
Glycosylation is a post-translational modification (PTM) of proteins that occurs during the translocation and trafficking of protein through ER and Golgi [1,2]
To evaluate the feasibility and the applicability of glycomics in the veterinary clinic area, we discovered the N-glycan biomarkers from canine serum
140~160 of N-glycans extracted by the MFE software from each serum sample in the healthy control group and 180~240 of N-glycans from the osteoarthritis (OA) patient group
Summary
Glycosylation is a post-translational modification (PTM) of proteins that occurs during the translocation and trafficking of protein through ER and Golgi [1,2]. As most PTM does, it intervenes in the mode of or the degree of protein functionality that influences the stability and activity of an innate protein, and the recognizability and interaction of ligands [2,5,6,7]. The global profile of serum N-glycome is sensitively changed by the cellular state [8]. With the change of specific protein expression, the profile of N-glycan expression can be affected. Without alteration of protein expression, the change of the cellular environments such as the onset of or the response to the disease readily impacts on the protein glycosylation [9,10]
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