The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Properties of the Glomerular Barrier and Mechanisms of Proteinuria
Abstract
This review focuses on the intricate properties of the glomerular barrier. Other reviews have focused on podocyte biology, mesangial cells, and the glomerular basement membrane (GBM). However, since all components of the glomerular membrane are important for its function, proteinuria will occur regardless of which layer is affected by disease. We review the properties of endothelial cells and their surface layer, the GBM, and podocytes, discuss various methods of studying glomerular permeability, and analyze data concerning the restriction of solutes by size, charge, and shape. We also review the physical principles of transport across biological or artificial membranes and various theoretical models used to predict the fluxes of solutes and water. The glomerular barrier is highly size and charge selective, in qualitative agreement with the classical studies performed 30 years ago. The small amounts of albumin filtered will be reabsorbed by the megalin-cubulin complex and degraded by the proximal tubular cells. At present, there is no unequivocal evidence for reuptake of intact albumin from urine. The cellular components are the key players in restricting solute transport, while the GBM is responsible for most of the resistance to water flow across the glomerular barrier.
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Maynard, S. E., Min, J.-Y., Merchan, J., Lim, K.-H., Li, J., Mondal, S., Libermann, T. A., Morgan, J. P., Sellke, F. W., Stillman, I. E., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci17189 · Cited by 4,101
Circulating angiogenic factors and the risk of preeclampsia
Levine, R. J., Maynard, S. E., Qian, C., Lim, K.-H., England, L. J., Yu, K. F., Schisterman, E. F., Thadhani, R., Sachs, B. P., Epstein, F. H., et al. (2004) · New England Journal of Medicine · doi:10.1056/nejmoa031884 · Cited by 3,720
Cell biology of the glomerular podocyte
Pavenstädt, H., Kriz, W., & Kretzler, M. (2003) · Physiological Reviews · doi:10.1152/physrev.00020.2002 · Cited by 1,499
Boute, N., Gribouval, O., Roselli, S., Benessy, F., Lee, H., Fuchshuber, A., Dahan, K., Gubler, M.-C., Niaudet, P., & Antignac, C. (2000) · Nature Genetics · doi:10.1038/74166 · Cited by 1,444
Giddings, J. C., Kucera, E., Russell, C. P., & Myers, M. N. (1968) · The Journal of Physical Chemistry · doi:10.1021/j100859a008 · Cited by 476
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Eckardt, K.-U., Coresh, J., Devuyst, O., Johnson, R. J., Köttgen, A., Levey, A. S., & Levin, A. (2013) · The Lancet · doi:10.1016/s0140-6736(13)60439-0 · Cited by 1,159
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Metadata
- Authors
- Haraldsson, B., Nyström, J., & Deen, W. M.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2008-04
- Volume
- 88
- Issue
- 2
- Pages
- 451-487
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2128545033
- Cited by
- 909
- References
- 5
- FWCI
- 5.89
- Type
- journal article
- Language
- en
- Open access
- closed
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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