Role of integrins in the assembly and function of hensin in intercalated cells Journal Article


Authors: Vijayakumar, S.; Erdjument-Bromage, H.; Tempst, P.; Al-Awqati, Q.
Article Title: Role of integrins in the assembly and function of hensin in intercalated cells
Abstract: Epithelial differentiation proceeds in at least two steps: Conversion of a nonepithelial cell into an epithelial sheet followed by terminal differentiation into the mature epithelial phenotype. It was recently discovered that the extracellular matrix (ECM) protein hensin is able to convert a renal intercalated cell line from a flat, squamous shape into a cuboidal or columnar epithelium. Global knockout of hensin in mice results in embryonic lethality at the time that the first columnar cells appear. Here, antibodies that either activate or block integrin ß1 were used to demonstrate that activation of integrin αvβ1 causes deposition of hensin in the ECM. Once hensin polymerizes and deposits into the ECM, it binds to integrin α6 and mediates the conversion of epithelial cells to a cuboidal phenotype capable of apical endocytosis; therefore, multiple integrins play a role in the terminal differentiation of the intercalated cell: αvβ1 generates polymerized hensin, and another set of integrins (containing α6) mediates signals between hensin and the interior of the cells. Copyright © 2008 by the American Society of Nephrology.
Keywords: controlled study; nonhuman; protein function; animal cell; mouse; phenotype; animal; cytology; animals; mice; protein assembly; protein binding; cell differentiation; physiology; scleroprotein; extracellular matrix; kidney; amino acid sequence; nucleotide sequence; epithelium cell; epithelial cells; alpha6 integrin; endocytosis; antibody; integrin; protein polymerization; integrins; mucin; mucins; kidney cell; beta1 integrin; hensin; integrin alphav beta1; dmbt1 protein, mouse
Journal Title: Journal of the American Society of Nephrology
Volume: 19
Issue: 6
ISSN: 1046-6673
Publisher: American Society of Nephrology  
Date Published: 2008-06-01
Start Page: 1076
End Page: 1091
Language: English
DOI: 10.1681/ASN.2007070737
PUBMED: 18337486
PROVIDER: scopus
PMCID: PMC2396932
DOI/URL:
Notes: --- - "Cited By (since 1996): 5" - "Export Date: 17 November 2011" - "CODEN: JASNE" - "Molecular Sequence Numbers: GENBANK: AF192528, AF468058, FCU27351, AY195896, GI28565527; SWISSPROT: P26008, P90055;" - "Source: Scopus"
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  1. Paul J Tempst
    324 Tempst