Abstract |
For more than three decades, the molecular composition of the interpodocyte slit diaphragm of the glomerular filtration barrier has remained elusive. The first electron microscopic studies described the slit diaphragm as a porous, 'zipper-like' structure, but it was not until 1998 that the first transmembrane molecule of the slit diaphragm was identified: nephrin is a cell surface receptor of the immunoglobulin superfamily participating in cell-cell adhesion and signaling functions. Mutations in nephrin lead to the congenital nephrotic syndrome of the Finnish type, suggesting that nephrin is of pivotal importance for maintaining the filtration barrier. In recent years, the mapping of the genetic background of other inherited and acquired nephropathies and generation of transgenic animal models have led to a beginning of a new era in nephrology, possibly promising new targeted therapies and advanced diagnostics. This review article will briefly summarize the main findings that explain the molecular architecture of the glomerular filter itself and causes of some glomerular diseases that lead to proteinuria and, eventually, to renal failure.
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Authors | Anu Pätäri-Sampo, Pekka Ihalmo, Harry Holthöfer |
Journal | Annals of medicine
(Ann Med)
Vol. 38
Issue 7
Pg. 483-92
( 2006)
ISSN: 0785-3890 [Print] England |
PMID | 17101539
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)
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Chemical References |
- Adaptor Proteins, Signal Transducing
- Cadherins
- Carrier Proteins
- FAT1 protein, human
- KIRREL1 protein, human
- KIRREL3 protein, human
- LRRC7 protein, human
- Membrane Proteins
- Nuclear Matrix-Associated Proteins
- Sialoglycoproteins
- nephrin
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Topics |
- Adaptor Proteins, Signal Transducing
(physiology)
- Cadherins
(physiology)
- Carrier Proteins
(physiology)
- Finland
- Humans
- Kidney Glomerulus
(physiology, ultrastructure)
- Membrane Proteins
(genetics, physiology)
- Microscopy, Electron
- Nephrotic Syndrome
(congenital, genetics)
- Nuclear Matrix-Associated Proteins
(physiology)
- Podocytes
(physiology, ultrastructure)
- Sialoglycoproteins
(physiology)
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