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Renal catabolism of advanced glycation end products: The fate of pentosidine
Open accessAbstract
Advanced glycation end products (AGEs) generated through the Maillard reaction significantly alter protein characteristics. Their accumulation has been incriminated in tissue injury associated with aging, diabetes, and renal failure. However, little is known about their clearance from the body. The present study delineates the catabolic pathway of a well-defined AGE product, pentosidine. Synthesized pentosidine given intravenously in rats with normal renal function was rapidly eliminated from the circulation through glomerular filtration, but was undetectable in the urine by chemical analysis. Immunohistochemistry with anti-pentosidine antibody disclosed that pentosidine accumulated transiently in the proximal renal tubule one hour after its administration, but had disappeared from the kidney at 24 hours. After an intravenous load of radiolabeled pentosidine, radioactivity peaked in the kidney at one hour and subsequently decreased, whereas it rose progressively in the urine. Over 80% of the radioactivity was recovered in the 72-hour collected urine. However, only 20% of urine radioactivity was associated with intact pentosidine chemically or immunochemically. In gentamicin-treated rats with tubular dysfunction, up to 30% of the pentosidine load was recovered as intact pentosidine in the urine. The present study suggests that free pentosidine (and possibly other AGEs) is filtered by renal glomeruli, reabsorbed in the proximal tubule where it is degraded or modified, and eventually excreted in the urine. Kidney thus plays a key role in pentosidine disposal.
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“The increase in abdominal fat mass is associated with a chronic elevation of the circulating concentrations of inflammatory mediators including several acute-phase inflammatory proteins such as CRP (46,47) , proand anti-inflammatory cytokines, adhesion molecules and pro-thrombotic molecules (22,47 -49) .”
From Dietary factors and low-grade inflammation in relation to overweight and obesity (2011) · cites this paper as [48]
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Citations
Cites
Role of Oxidative Stress in Development of Complications in Diabetes
Baynes, J. (1991) · Diabetes · doi:10.2337/diab.40.4.405 · Cited by 3,791
Advanced Glycosylation End Products in Tissue and the Biochemical Basis of Diabetic Complications
Flier, J. S., Underhill, L. H., Brownlee, M., Cerami, A., & Vlassara, H. (1988) · New England Journal of Medicine · doi:10.1056/nejm198805193182007 · Cited by 2,512
Neeper, M. P., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y., Elliston, K. O., Stern, D., & SHAW, A. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42138-2 · Cited by 1,545
Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y., Pinsky, D. J., & Stern, D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36966-1 · Cited by 1,305
Structure Elucidation of a Senescence Cross-Link from Human Extracellular Matrix
Sell, D. R., & Monnier, V. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88225-8 · Cited by 1,082
Advanced Glycosylation End Products in Patients with Diabetic Nephropathy
Makita, Z., Radoff, S., Rayfield, E. J., Yang, Z. H., Skolnik, E. Y., DELANEY, V. B., Friedman, E. A., Cerami, A., & Vlassara, H. (1991) · New England Journal of Medicine · doi:10.1056/nejm199109193251202 · Cited by 922
Ahmed, M. U., Thorpe, S. R., & Baynes, J. W. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)89188-3 · Cited by 864
Accumulation of Maillard reaction products in skin collagen in diabetes and aging.
Dyer, D. G., Dunn, J. A., Thorpe, S. R., Bailie, K., Lyons, T. J., McCance, D. R., & Baynes, J. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116481 · Cited by 770
Cachectin/TNF and IL-1 Induced by Glucose-Modified Proteins: Role in Normal Tissue Remodeling
Vlassara, H., Brownlee, M., Manogue, K. R., Dinarello, C. A., & Pasagian, A. (1988) · Science · doi:10.1126/science.3259727 · Cited by 597
Wells‐Knecht, K. J., Zyzak, D. V., Litchfield, J., Thorpe, S. R., & Baynes, J. (1995) · Biochemistry · doi:10.1021/bi00011a027 · Cited by 594
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Reis, J. S., Veloso, C. A., de Mattos, R. T., Purisch, S., & Nogueira‐Machado, J. A. (2008) · Arquivos Brasileiros de Endocrinologia & Metabologia · doi:10.1590/s0004-27302008000700005 · Cited by 54
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Coughlan, M. T., Patel, S. K., Jerums, G., Penfold, S. A., Nguyen, T.-V., Sourris, K. C., Panagiotopoulos, S., Srivastava, P., Cooper, M. E., Burrell, L. M., et al. (2011) · American Journal of Nephrology · doi:10.1159/000331064 · Cited by 41
Perkins, R. K., Miranda, E. R., Karstoft, K., Beisswenger, P. J., Solomon, T. P. J., & Haus, J. M. (2019) · Nutrients · doi:10.3390/nu11030532 · Cited by 39
Furuya, R., Kumagai, H., Odamaki, M., Takahashi, M., Miyaki, A., & Hishida, A. (2009) · Nephron Clinical Practice · doi:10.1159/000224792 · Cited by 39
Hartog, J. W. L., Smit, A. J., van Son, W. J., Navis, G., Gans, R. O. B., Wolffenbuttel, B. H. R., & de Jong, P. E. (2004) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2004.02.008 · Cited by 39
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Thomas, M. C., Forbes, J. M., MacIsaac, R. J., Jerums, G., & Cooper, M. E. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.073 · Cited by 39
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Suh, M., Tovchigrechko, A., Thovarai, V., Rolfe, M. A., Torralba, M., Wang, J., Adkins, J., Webb‐Robertson, B., Osborne, W., Cogen, F. R., et al. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00052 · Cited by 36
Sundl, I., Roob, J. M., Meinitzer, A., Tiran, B., Khoschsorur, G., Haditsch, B., Holzer, H., & Winklhofer‐Roob, B. M. (2009) · Peritoneal Dialysis International · doi:10.1177/089686080902900113 · Cited by 35
Forbes, J. M., Sourris, K. C., de Courten, M., Dougherty, S. L., Chand, V., Lyons, J. G., Bertovic, D. A., Coughlan, M. T., Schlaich, M. P., Soldatos, G., et al. (2013) · Amino Acids · doi:10.1007/s00726-013-1542-9 · Cited by 34
Raupbach, J., Ott, C., Koenig, J., & Grune, T. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.11.024 · Cited by 34
Chen, S., Guh, J., Hwang, C., Chiou, S.-J., Lin, T., Ko, Y., Huang, J., Yang, Y., & Chuang, L. (2009) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22376 · Cited by 34
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Leurs, P. B., & Lindholm, B. (2013) · Archives of Medical Research · doi:10.1016/j.arcmed.2013.11.002 · Cited by 29
Waanders, F., van den Berg, E., Nagai, R., van Veen, I., Navis, G. J., & van Goor, H. (2007) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfm589 · Cited by 29
Lee, H.-W., Gu, M. J., Kim, Y., Lee, J., Lee, S., Choi, I., & Ha, S. K. (2021) · Antioxidants · doi:10.3390/antiox10091486 · Cited by 28
Saito, A., Takeda, T., Hama, H., Oyama, Y., Hosaka, K., Tanuma, A., Kaseda, R., Ueno, M., Nishi, S., Ogasawara, S., et al. (2005) · Nephrology · doi:10.1111/j.1440-1797.2005.00453.x · Cited by 27
Circulating advanced glycation end product levels in rats rapidly increase with acute renal failure
Šsebeková, K., Blažíček, P., Syrova, D., Krivošíková, Z., Spustová, V., Heidland, A., & Schinzel, R. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.59780058.x · Cited by 27
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Clark, W. R., & Henderson, L. W. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.59780298.x · Cited by 27
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Kaňková, K., Kalousová, M., Hertlová, M., Krusová, D., Olšovský, J., & Zima, T. (2008) · Archives of Physiology and Biochemistry · doi:10.1080/13813450802033818 · Cited by 27
Perkins, B. A., Rabbani, N., Weston, A. J., Adaikalakoteswari, A., Lee, J. A., Lovblom, L. E., Cardinez, N., & Thornalley, P. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-69350-y · Cited by 25
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Renal accumulation of pentosidine in non-diabetic proteinuria-induced renal damage in rats
Waanders, F., Greven, W. L., Baynes, J., Thorpe, S. R., Kramer, A. B., Nagai, R., Sakata, N., van Goor, H., & Navis, G. J. (2005) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfh939 · Cited by 23
S, C. A. T., Pereira, L. M., dos Santos, L., Fávero, P. P., & Martin, A. A. (2015) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2015.06.110 · Cited by 22
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Bhat, S., Mary, S., Giri, A. P., & Kulkarni, M. J. (2017) · Springer eBooks · doi:10.1007/978-3-319-60324-7_19 · Cited by 21
Ikeda, T., Maruyama, K., Ito, N., Utagawa, A., Nagane, M., & Shiokawa, Y. (2010) · Journal of Stroke and Cerebrovascular Diseases · doi:10.1016/j.jstrokecerebrovasdis.2010.10.004 · Cited by 21
Liu, Y., Huang, H. Y., Gao, R., & Liu, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00172 · Cited by 21
Słowik-Żyłka, D., Safranow, K., Dziedziejko, V., Bukowska, H., Ciechanowski, K., & Chlubek, D. (2004) · Journal of Biochemical and Biophysical Methods · doi:10.1016/j.jbbm.2004.06.002 · Cited by 21
Brown, C. D., Zhao, Z., Thomas, L. L., deGroof, R., & Friedman, E. A. (2001) · American Journal of Kidney Diseases · doi:10.1053/ajkd.2001.29281 · Cited by 20
Szwergold, B. S., & Miller, C. B. (2014) · Rejuvenation Research · doi:10.1089/rej.2014.1561 · Cited by 22
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Jeon, G. Y., Nam, M., & Lee, K. (2021) · Journal of Food Science · doi:10.1111/1750-3841.15588 · Cited by 16
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Lee, J. S., Chung, Y., Chang, S. Y., Jung, Y., & Kim, S. H. (2017) · International Journal of Analytical Chemistry · doi:10.1155/2017/1389807 · Cited by 15
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Aoki, S.-I., Hasegawa, G., Shigeta, H., Obayashi, H., Fujii, M., Kimura, F., Moriwaki, A., Nakamura, N., Ienaga, K., Nakamura, K., et al. (2000) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(99)00148-5 · Cited by 15
Aso, Y., Takanashi, K., Sekine, K., Yoshida, N., Takebayashi, K., Yoshihara, K., & Inukai, T. (2004) · Journal of Laboratory and Clinical Medicine · doi:10.1016/j.lab.2004.03.016 · Cited by 15
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Blumenthal, S. S. (2011) · Postgraduate Medicine · doi:10.3810/pgm.2011.11.2506 · Cited by 12
Zhang, S., Wang, D., Xue, N., Lai, F., Ji, M., Jin, J., & Chen, X. (2017) · PubMed Central · Cited by 12
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Kanaoka, T., Tamura, K., Ohsawa, M., Yanagi, M., Haku, S., Wakui, H., Maeda, A., Dejima, T., Azushima, K., Mitsuhashi, H., et al. (2012) · Clinical and Experimental Hypertension · doi:10.3109/10641963.2012.681082 · Cited by 12
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Liu, Y. A., Zhang, W., & Sayre, L. M. (2011) · Journal of Heterocyclic Chemistry · doi:10.1002/jhet.611 · Cited by 11
Varikasuvu, S. R., Sulekar, H., Aloori, S., & Thangappazham, B. (2020) · International Urology and Nephrology · doi:10.1007/s11255-020-02543-6 · Cited by 11
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Gugliucci, A. (2000) · Cited by 10
Kaburagi, T., Kanaki, K., Otsuka, Y., & Hino, R. (2019) · Nutrients · doi:10.3390/nu11112801 · Cited by 9
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Inagi, R. (2021) · Glycoconjugate Journal · doi:10.1007/s10719-021-09989-5 · Cited by 9
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Andrades, M. É., Lorenzi, R., Nagai, R., Moreira, J. C. F., Ritter, C., & Dal‐Pizzol, F. (2012) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2012.02694.x · Cited by 9
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Hamlett, L., & Haragsim, L. (2007) · Advances in Chronic Kidney Disease · doi:10.1053/j.ackd.2007.03.006 · Cited by 9
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Baumann, M., Caron, M. M. J., Schmaderer, C., Schulte, C., Viklický, O., von Weyhern, C. W. H., Lutz, J., & Heemann, U. W. (2008) · Transplantation · doi:10.1097/tp.0b013e31817ef7a5 · Cited by 9
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Labissiere, X., Zigmond, Z. M., Challa, A. S., Montoya, C., Manzur-Pineda, K., Abraham, A., Tabbara, M., Salama, A., Pan, Y., Salman, L. H., et al. (2022) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2022.1005030 · Cited by 7
Cattaneo, L., Rocchetti, G., Piccioli-Cappelli, F., Zini, S., Trevisi, E., & Minuti, A. (2023) · Scientific Reports · doi:10.1038/s41598-023-31922-z · Cited by 7
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Oyanagi, A., Orikasa, M., Kawachi, H., Ito, Y., Koike, H., Gejo, F., & Shimizu, F. (2001) · The Nephron journals/Nephron journals · doi:10.1159/000046117 · Cited by 7
Huang, N. K., Pai, M.-H., Wu, C.-H., Liu, J., & Yeh, S. L. (2010) · e-SPEN the European e-Journal of Clinical Nutrition and Metabolism · doi:10.1016/j.eclnm.2010.02.001 · Cited by 7
Miyataka, K., Kaneko, Y., Hori, T., Yamaguchi, Y., Tsuji, S., Hara, T., Yamagami, H., Yoshida, S., Otoda, T., Yuasa, T., et al. (2025) · Journal of Diabetes Investigation · doi:10.1111/jdi.70149 · Cited by 8
Tsutsumi, E., Murata, Y., Sakamoto, M., & Horikawa, E. (2015) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2015.03.002 · Cited by 6
Varikasuvu, S. R., Aloori, S., & Bhongir, A. V. (2020) · Journal of Artificial Organs · doi:10.1007/s10047-020-01189-6 · Cited by 6
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Ng, D., Hardy, C. L., Burns, W. C., Muggli, E., Kerr, N. F., McCausland, J., Alcorn, D., Adams, T. E., Zajac, J. D., Larkins, R. G., et al. (2002) · Endocrine · doi:10.1385/endo:18:1:47 · Cited by 5
Azamian, Y., Abdollahzad, H., Rezaeian, S., Rouhani, M. H., & Fatehi, M. H. (2024) · Food Science & Nutrition · doi:10.1002/fsn3.4338 · Cited by 4
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Yamagami, H., Hara, T., Yasui, S., Hosoki, M., Hori, T., Kaneko, Y., Mitsui, Y., Kurahashi, K., Harada, T., Yoshida, S., et al. (2023) · Biomedicines · doi:10.3390/biomedicines11113020 · Cited by 3
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Hu, Y., Yeh, C., Pai, M.-H., Li, C.-C., Liu, J., & Yeh, S. L. (2011) · Journal of Experimental & Clinical Medicine · doi:10.1016/j.jecm.2011.11.004 · Cited by 3
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Silvério, A. D. S. D., Pereira, R. G. F. A., Duarte, S. M. D. S., Figueiredo, S. A., Paula, F. B. D. A., Araújo, T. H., Ferreira, C. D. S., Salles, B. C. C., Viana, A. L. M., Ferreira, E. B., et al. (2021) · Revista de ciencias farmaceuticas · doi:10.4322/2179-443x.0711 · Cited by 2
Hara, T., Watanabe, T., Yamagami, H., Miyataka, K., Yasui, S., Asai, T., Kaneko, Y., Mitsui, Y., Masuda, S., Kurahashi, K., et al. (2024) · Biomedicines · doi:10.3390/biomedicines12081789 · Cited by 2
Inflammation in Chronic Kidney Disease
Kovesdy, C. P., & Kalantar‐Zadeh, K. (2010) · Elsevier eBooks · doi:10.1016/b978-1-4377-0987-2.00013-3 · Cited by 2
Cordeiro, A. C. C., de Castro, I., Pecoits‐Filho, R., Ramasawmy, R., Rodrigues, H., Borba, S. C. P., Pereira, L. M., Romão, J. E., David‐Neto, E., Ianhez, L. E., et al. (2008) · Transplantation Proceedings · doi:10.1016/j.transproceed.2008.04.021 · Cited by 1
Pentosidine: Can Be Related To The Etiology Of Chronic Kidney Disease?
Kerkeni, M., Bouzidi, H., Ahmed, L., & Hammami, M. (2014) · International Journal of Diabetology & Vascular Disease Research · doi:10.19070/2328-353x-140009 · Cited by 1
Characterization of Black Pigmenturia in a Cat with Apocrine Gland Cystadenocarcinoma
Fournier, Q., Höhn, A., Deubel, S., Milne, E., Bavčar, Š., & Morrison, L. R. (2020) · Journal of Comparative Pathology · doi:10.1016/j.jcpa.2020.03.002 · Cited by 1
Miyata, T., & Kurokawa, K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-818540-7.00021-5 · Cited by 1
Advanced Glycation End Products in Diabetes
Mosquera-Sulbarán, J., & Hernández-Fonseca, J. P. (2022) · Biomarkers in disease · doi:10.1007/978-3-031-08014-2_8 · Cited by 1
Kelly, C. B., Karanchi, H., Yu, Y., Leyva, M. J., Jenkins, A. J., Nankervis, A. J., Hanssen, K. F., Garg, S. K., Scardo, J. A., Hammad, S. M., et al. (2023) · Journal of Diabetes Research · doi:10.1155/2023/8537693 · Cited by 1
Protein Oxidation in Some Age‐Related Diseases
Grune, T., Karademir-Yilmaz, B., & Jung, T. (2012) · Wiley eBooks · doi:10.1002/9781118493038.ch4 · Cited by 1
Huang, Z., Gao, D. Y., Ronco, C., & Clark, W. R. (2011) · Springer eBooks · doi:10.1007/978-1-4614-0721-8_2 · Cited by 1
The analysis of advanced glycation endproducts
Scheijen (2017) · Research Publications (Maastricht University) · doi:10.26481/dis.20170621js · Cited by 1
Boojar, F. M. A., Golmohamad, S., & Tafreshi, G. (2019) · doi:10.22186/jyi.36.1.5-10 · Cited by 1
Toxins in Renal Disease and Dialysis Therapy : Genotoxic Potential and Mechanisms
Fink, K. (2008) · Online Publication Service of Würzburg University (Würzburg University) · Cited by 1
Yamada, K. H., Tanimoto, M., Gohda, T., Ohsawa, I., Hamada, C., Ohi, H., Horikoshi, S., & Tomino, Y. (2008) · Juntendō Igaku/Juntendo igaku · doi:10.14789/pjmj.54.67
Metadata
- Authors
- Miyata, T., Ueda, Y., Horie, K., Nangaku, M., Tanaka, S., de Strihou, C. V. Y., & Kurokawa, K.
- Affiliations
- Tokai University (JP)
- Corresponding author
- Miyata, Toshio
- ORCID
- Nangaku, Masaomi
- Venue
- Kidney International
- Publisher
- Elsevier BV
- Published
- 1998-02
- Volume
- 53
- Issue
- 2
- Pages
- 416-422
- ISSN
- 0085-2538 (ISSN-L)
- OpenAlex
- W1998110176
- Cited by
- 227
- References
- 26
- Citations by year
- 2026: 3 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 7 · 2021: 8 · 2020: 12 · 2019: 10 · 2018: 4 · 2017: 12 · 2016: 1 · 2015: 10 · 2014: 5 · 2013: 11 · 2012: 8
- FWCI
- 5.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Kidney International (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Japan Society for the Promotion of Science (96L00303)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
- Health Sciences › Medicine › Nephrology › Dialysis and Renal Disease Management
- Keywords
- advanced glycation end products, pentosidine, Maillard reaction, glomerular filtration, proximal tubule, tubular reabsorption, urinary excretion, renal clearance, protein glycation
- MeSH terms
- Animals, Anti-Bacterial Agents, Arginine, Chromatography, High Pressure Liquid, Gentamicins, Kidney Diseases, Kidney Glomerulus, Kidney Tubules, Proximal, Lysine, Protein Synthesis Inhibitors, Glycation End Products, Advanced, Rats, Wistar, Rats
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