Tamm-Horsfall protein and urinary exosome isolation
Open accessAbstract
Urinary exosomes have been proposed as starting material for discovery of protein biomarkers of kidney disease. Current protocols for their isolation use a two-step differential centrifugation process. Due to their low density, exosomes are expected to remain in the low-speed (17,000 x g) supernatant and to sediment only when the sample is spun at high speed (200,000 x g). Analysis using western blot and electron microscopy found that urinary exosomes are also present in the low-speed pellet entrapped by polymeric Tamm-Horsfall protein, thus diminishing the procedure's reproducibility. Here we show that addition of dithiothreitol to the low-speed pellet disrupted the polymeric network, presumably by reduction of disulfide bonds linking the monomers. This modification shifted the exosomal proteins from the low- to the high-speed pellet. Also, by shifting the Tamm-Horsfall protein to the high-speed pellet, the use of dithiothreitol makes it feasible to use Tamm-Horsfall protein to normalize excretion rates of exosomal proteins in spot urines. We tested this by western blot, and found that there was a high degree of correlation between exosomal proteins and Tamm-Horsfall protein in the high-speed pellet. Since the yield of exosomes by differential centrifugation can be increased by chemical reduction, Tamm-Horsfall protein may be a suitable normalizing variable for urinary exosome studies when quantitative urine collections are not practical.
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TSG101 and Alix are two proteins sometimes used as exosome markers.
“TSG101 and Alix are two other proteins sometimes used as exosome markers [38, 46, 47].”
From Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies (2013) · cites this paper as [47]
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- Authors
- Fernández-Llama, P., Khositseth, S., Gonzales, P. A., Star, R. A., Pisitkun, T., & Knepper, M. A.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Knepper, Mark A.
- Venue
- Kidney International
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 77
- Issue
- 8
- Pages
- 736-742
- ISSN
- 0085-2538 (ISSN-L)
- PMC
- PMC3398710
- OpenAlex
- W2038509755
- Cited by
- 290
- References
- 17
- Citations by year
- 2026: 7 · 2025: 10 · 2024: 12 · 2023: 12 · 2022: 23 · 2021: 27 · 2020: 37 · 2019: 18 · 2018: 22 · 2017: 20 · 2016: 18 · 2015: 18 · 2014: 22 · 2013: 18 · 2012: 13
- FWCI
- 5.74
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Kidney International (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Sociedad Española de Nefrología
- National Institutes of Health (Z99 HL999999)
- National Heart, Lung, and Blood Institute (Z01HL001285, ZIAHL001285, Z01-HL001285)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Health Sciences › Medicine › Nephrology › Renal Diseases and Glomerulopathies
- Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Kidney Stones and Urolithiasis Treatments
- Keywords
- uromodulin, urinary exosomes, exosome isolation, differential centrifugation, dithiothreitol, disulfide bond reduction, kidney disease biomarkers, spot urine, urinary protein excretion
- MeSH terms
- Adult, Humans, Male, Microscopy, Electron, Mucoproteins, Urinary Tract, Blotting, Western, Biomarkers, Exosomes, Uromodulin
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