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In vivo and in vitro characterization of the canine nephron and urinary proteome

dc.contributor.authorBrandt, Laura Elizabeth, author
dc.contributor.authorBohn, Andrea A., advisor
dc.contributor.authorEhrhart, Eugene J., committee member
dc.contributor.authorOlver, Christine S., committee member
dc.contributor.authorPrenni, Jessica E., committee member
dc.date.accessioned2007-01-03T05:13:56Z
dc.date.available2007-01-03T05:13:56Z
dc.date.issued2011
dc.description.abstractImmunohistochemistry allows the localization of proteins to specific regions of the nephron. This study reports the identification and localization of proteins in situ within normal canine, feline and mouse kidney by immunohistochemistry, maps their distribution and compares results to previously reported findings in other species. The proteins investigated are aquaporin-1, aquaporin-2, calbindin-d28k, glutathione S-transferase-α and Tamm-Horsfall protein. Our findings in the dog are similar to that in other species, and localize aquaporin-1 to the proximal convoluted tubule epithelium, vasa recta endothelium and descending thin limbs, aquaporin-2 to collecting duct epithelium and calbindin-d28k is found within distal convoluted tubule epithelium. Glutathione S-transferase-α has variable expression and is found in renal transitional epithelium only in some individuals, the proximal straight tubules only in some individuals or in both locations in others. Tamm-Horsfall protein localizes to thick ascending limb epithelium. These findings are similar in the cat, with the exception that aquaporin-1 is located in glomerular podocytes, in addition to proximal convoluted tubule epithelium, and glutathione S-transferase-α is found solely within the proximal convoluted tubule within all kidney samples examined. The mouse kidney is almost identical to the dog, but expresses glutathione S-transferase-α in the glomeruli only. Additionally, we successfully adapted techniques employed in human studies to characterize the normal canine urinary proteome. Both soluble proteins and the exosomal fraction of urine were examined. Greater than 500 proteins were identified in this initial study. Many of these proteins are also found in human urine, but large numbers of proteins also appear to be unique to the canine. Software entitled Biological Networks Gene Ontology (BiNGO) was utilized to characterize canine urinary proteins into respective Gene Ontology categories of Cellular Component, Molecular Function and Biological Process. Exosomal proteins are largely derived from an intracellular location, while soluble proteins are comprised of extracellular and membrane proteins. The majority of proteins in both canine urinary fractions are involved in protein binding. Exosomal proteins are also involved in metabolic process and localization, while soluble proteins are linked to specific localization processes. The distribution of canine urinary proteins within GO functional categories is very similar to that of human urine. Known markers of renal disease, such as aquaporin-1, gamma-glutamyl transferase and retinal binding protein were identified via proteomic techniques in the urine of healthy dogs, as were novel biomarkers like fetuin-A and ubiquitin A-52.
dc.format.mediumborn digital
dc.format.mediummasters theses
dc.identifierBrandt_colostate_0053N_10435.pdf
dc.identifier.urihttp://hdl.handle.net/10217/47306
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.subjectbiomarkers
dc.subjectcanine
dc.subjectimmunohistochemistry
dc.subjectnephron
dc.subjectrenal failure
dc.subjecturinary proteome
dc.titleIn vivo and in vitro characterization of the canine nephron and urinary proteome
dc.typeText
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineMicrobiology, Immunology, and Pathology
thesis.degree.grantorColorado State University
thesis.degree.levelMasters
thesis.degree.nameMaster of Science (M.S.)

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