Document Detail


Podocyte alpha-actinin induction precedes foot process effacement in experimental nephrotic syndrome.
MedLine Citation:
PMID:  9249603     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
W E Smoyer; P Mundel; A Gupta; M J Welsh
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The American journal of physiology     Volume:  273     ISSN:  0002-9513     ISO Abbreviation:  Am. J. Physiol.     Publication Date:  1997 Jul 
Date Detail:
Created Date:  1997-09-03     Completed Date:  1997-09-03     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0370511     Medline TA:  Am J Physiol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  F150-7     Citation Subset:  IM    
Affiliation:
Department of Pediatrics, University of Michigan, Ann Arbor 48109, USA.
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MeSH Terms
Descriptor/Qualifier:
Actinin / 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:
ES-07006/ES/NIEHS NIH HHS; P30-HD-18258/HD/NICHD NIH HHS; R01-ES-06265/ES/NIEHS NIH HHS
Chemical
Reg. No./Substance:
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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