Document Detail


Slit diaphragm dysfunction in proteinuric states: identification of novel therapeutic targets for nephrotic syndrome.
MedLine Citation:
PMID:  19266252     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Several recent studies have demonstrated that the slit diaphragm of the glomerular epithelial cell (podocyte) is the structure likely to be the principal barrier in the glomerular capillary wall. Nephrin identified as a gene product mutated in congenital nephrotic syndrome located at the outer leaflet of plasma membranes of the slit diaphragm. The anti-nephrin antibody is capable of inducing massive proteinuria, which indicates that nephrin is a key functional molecule in the slit diaphragm. Expression of nephrin was reduced in glomeruli of minimal change nephrotic syndrome. Some recent studies demonstrated that podocin, CD2-associated protein and NEPH1 are also functional molecules in the slit diaphragm, and their expressions are altered in membranous nephropathy and also in focal glomerulosclerosis. These observations suggested that the alteration of the molecular arrangement in the slit diaphragm is involved in the development of proteinuria in several kinds of glomerular diseases. Recent studies of our group have demonstrated that type 1 receptor-mediated angiotensin II action reduced the expression of the slit diaphragm-associated molecules and that type 1 receptor blockade ameliorated proteinuria by preventing the function of angiotensin II on the slit diaphragm. By the subtraction hybridization techniques using glomerular cDNA of normal and proteinuric rats, we detected that synaptic vesicle protein 2B and ephrin B1 are involved in the maintenance of the barrier function of the slit diaphragm.
Authors:
Hiroshi Kawachi; Koichi Suzuki; Naoko Miyauchi; Taeko Hashimoto; Yasuhiro Otaki; Fujio Shimizu
Publication Detail:
Type:  Journal Article; Review     Date:  2009-03-07
Journal Detail:
Title:  Clinical and experimental nephrology     Volume:  13     ISSN:  1437-7799     ISO Abbreviation:  Clin. Exp. Nephrol.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-08-06     Completed Date:  2009-10-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9709923     Medline TA:  Clin Exp Nephrol     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  275-80     Citation Subset:  IM    
Affiliation:
Department of Cell Biology, Institute of Nephrology, Niigata University Graduate School of Medical and Dental Sciences, 1-757 Asahimachi-dori, Niigata 951-8510, Japan. kawachi@med.niigata-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Adaptor Proteins, Signal Transducing / metabolism
Angiotensin II / metabolism
Angiotensin II Type 1 Receptor Blockers / pharmacology
Animals
Cytoskeletal Proteins / metabolism
Ephrin-B1 / metabolism
Glomerular Filtration Rate* / drug effects
Humans
Intracellular Signaling Peptides and Proteins / metabolism
Membrane Glycoproteins / metabolism
Membrane Proteins / metabolism
Nephrotic Syndrome / drug therapy,  metabolism*,  physiopathology
Nerve Tissue Proteins / metabolism
Podocytes / drug effects,  metabolism*
Proteinuria / drug therapy,  metabolism*,  physiopathology
Receptor, Angiotensin, Type 1 / drug effects,  metabolism
Chemical
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Angiotensin II Type 1 Receptor Blockers; 0/CD2-associated protein; 0/Cytoskeletal Proteins; 0/Ephrin-B1; 0/Intracellular Signaling Peptides and Proteins; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/NPHS2 protein; 0/Nerve Tissue Proteins; 0/Receptor, Angiotensin, Type 1; 0/Sv2b protein, rat; 0/nephrin; 11128-99-7/Angiotensin II

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