RGD Reference Report - Expression of galectin-1, a new component of slit diaphragm, is altered in minimal change nephrotic syndrome. - Rat Genome Database

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Expression of galectin-1, a new component of slit diaphragm, is altered in minimal change nephrotic syndrome.

Authors: Shimizu, M  Khoshnoodi, J  Akimoto, Y  Kawakami, H  Hirano, H  Higashihara, E  Hosoyamada, M  Sekine, Y  Kurayama, R  Kurayama, H  Joh, K  Hirabayashi, J  Kasai, K  Tryggvason, K  Ito, N  Yan, K 
Citation: Shimizu M, etal., Lab Invest. 2009 Feb;89(2):178-95. Epub 2008 Dec 15.
RGD ID: 2316526
Pubmed: PMID:19079321   (View Abstract at PubMed)
DOI: DOI:10.1038/labinvest.2008.125   (Journal Full-text)

Nephrin is an essential structural component of the glomerular slit diaphragm (SD), a highly organized intercellular junction that constitutes the ultrafiltration barrier of the kidney. Recent studies have identified two additional nephrin-interacting SD proteins (NEPH1 and NEPH2), suggesting that the zipper-like pattern of the SD is formed through complex intra- and intermolecular interactions of these proteins. However, the complexity of the SD structure suggests that additional SD components remain to be discovered. In this study, we identified galectin-1 (Gal-1) as a new component of the SD, binding to the ectodomain of nephrin. Using dual-immunofluorescence and confocal microscopy and dual-immunoelectron microscopy, we found Gal-1 co-localizing with the ectodomain of nephrin at the SD in normal human kidney. By immunoprecipitation and surface plasmon resonance, we confirmed a direct molecular interaction between Gal-1 and nephrin. Moreover, recombinant Gal-1 induced tyrosine phosphorylation of the cytoplasmic domain of nephrin and activation of the extracellular signal-regulated kinase 1/2 in podocytes. We also showed that podocytes are a major site of biosynthesis of Gal-1 in the glomerulus and that the normal expression patterns and levels of Gal-1 are altered in patients with minimal change nephrotic syndrome. Finally, in puromycin aminonucleoside-induced rat nephrosis, an apparent reduction in the levels of Gal-1 and nephrin around the onset of heavy proteinuria was also revealed. Our data present Gal-1 as a new extracellular ligand of nephrin localized at the glomerular SD, and provide further insight into the complex molecular organization, interaction, and structure of the SD, which is an active site of intracellular signaling necessary for podocyte function.



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Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
LGALS1Humanlipoid nephrosis  ISOLgals1 (Rattus norvegicus)protein:decreased expression:glomerulus, podocytes (rat)RGD 
Lgals1Ratlipoid nephrosis  IEP protein:decreased expression:glomerulus, podocytes (rat)RGD 
Lgals1Mouselipoid nephrosis  ISOLgals1 (Rattus norvegicus)protein:decreased expression:glomerulus, podocytes (rat)RGD 

Objects Annotated

Genes (Rattus norvegicus)
Lgals1  (galectin 1)

Genes (Mus musculus)
Lgals1  (lectin, galactose binding, soluble 1)

Genes (Homo sapiens)
LGALS1  (galectin 1)


Additional Information