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Characterization of the canine urinary proteome

Authors

  • Laura E. Brandt,

    1. Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO, USA
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  • E. J. Ehrhart,

    1. Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO, USA
    2. Animal Cancer Center, Colorado State University, Fort Collins, CO, USA
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  • Hataichanok Scherman,

    1. Proteomics and Metabolomics Facility, Colorado State University, Fort Collins, CO, USA
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  • Christine S. Olver,

    1. Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO, USA
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  • Andrea A. Bohn,

    1. Department of Microbiology, Immunology and Pathology, Colorado State University, Fort Collins, CO, USA
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  • Jessica E. Prenni

    Corresponding author
    1. Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA
    2. Proteomics and Metabolomics Facility, Colorado State University, Fort Collins, CO, USA
    • Correspondence

      Jessica E. Prenni, Department of Biochemistry and Molecular Biology, and Proteomics and Metabolomics Facility, 2021 Campus Delivery, Colorado State University, Fort Collins, CO 80523, USA

      E-mail: jprenni@colostate.edu

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Abstract

Background

Urine is an attractive biofluid for biomarker discovery as it is easy and minimally invasive to obtain. While numerous studies have focused on the characterization of human urine, much less research has focused on canine urine.

Objectives

The objectives of this study were to characterize the universal canine urinary proteome (both soluble and exosomal), to determine the overlap between the canine proteome and a representative human urinary proteome study, to generate a resource for future canine studies, and to determine the suitability of the dog as a large animal model for human diseases.

Methods

The soluble and exosomal fractions of normal canine urine were characterized using liquid chromatography tandem mass spectrometry (LC-MS/MS). Biological Networks Gene Ontology (BiNGO) software was utilized to assign the canine urinary proteome to respective Gene Ontology categories, such as Cellular Component, Molecular Function, and Biological Process.

Results

Over 500 proteins were confidently identified in normal canine urine. Gene Ontology analysis revealed that exosomal proteins were largely derived from an intracellular location, while soluble proteins included both extracellular and membrane proteins. Exosome proteins were assigned to metabolic processes and localization, while soluble proteins were primarily annotated to specific localization processes. Several proteins identified in normal canine urine have previously been identified in human urine where these proteins are related to various extrarenal and renal diseases.

Conclusions

The results of this study illustrate the potential of the dog as an animal model for human disease states and provide the framework for future studies of canine renal diseases.

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