| Podocyte alpha-actinin induction precedes foot process effacement in experimental nephrotic syndrome. | |
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MedLine Citation:
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PMID: 9249603 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Attachment of podocytes to the glomerular basement membrane is thought to be mediated primarily by alpha 3/beta 1-integrins and by cytoskeletal proteins including actin, talin, vinculin, and alpha-actinin. We analyzed the expression of those molecules in rat glomeruli at several time points during induction of podocyte foot process effacement and nephrotic syndrome with puromycin aminonucleoside (PAN). PAN injection resulted in marked induction of glomerular alpha-actinin (40% increase vs. paired controls, P < 0.01), which clearly preceded development of podocyte foot process effacement and proteinuria and localized almost exclusively to podocytes. Delayed induction of glomerular alpha 3-integrin (44% increase vs. paired controls, P < 0.01) following foot process effacement was also observed but was not restricted to podocytes. No significant changes in glomerular vinculin, talin, beta 1-integrin, or total actin expression occurred at any time point during disease development. We conclude that foot process effacement is preceded by induction of alpha-actinin in podocytes in experimental nephrotic syndrome. Altered expression of this actin cross-linking protein in podocytes may have a pathogenic role in foot process effacement in nephrotic syndrome. |
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Authors:
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W E Smoyer; P Mundel; A Gupta; M J Welsh |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: The American journal of physiology Volume: 273 ISSN: 0002-9513 ISO Abbreviation: Am. J. Physiol. Publication Date: 1997 Jul |
Date Detail:
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Created Date: 1997-09-03 Completed Date: 1997-09-03 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 0370511 Medline TA: Am J Physiol Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: F150-7 Citation Subset: IM |
Affiliation:
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Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Actinin
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analysis,
biosynthesis* Actins / biosynthesis Animals Antigens, CD / biosynthesis Antigens, CD29 / biosynthesis Epithelium / pathology, physiopathology, ultrastructure Integrin alpha3 Integrins / biosynthesis Kidney / pathology, physiology, physiopathology Kidney Glomerulus / pathology, physiology, physiopathology* Male Nephrotic Syndrome / chemically induced, pathology, physiopathology* Puromycin Aminonucleoside / toxicity Rats Rats, Sprague-Dawley Talin / biosynthesis Time Factors |
| Grant Support | |
ID/Acronym/Agency:
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ES-07006/ES/NIEHS NIH HHS; P30-HD-18258/HD/NICHD NIH HHS; R01-ES-06265/ES/NIEHS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Actins; 0/Antigens, CD; 0/Antigens, CD29; 0/Integrin alpha3; 0/Integrins; 0/Talin; 11003-00-2/Actinin; 58-60-6/Puromycin Aminonucleoside |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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