The alpha 1-alpha 6 subunits of integrins are characteristically expressed in distinct segments of developing and adult human nephron.
Open Access
- 31 August 1990
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 111 (3) , 1245-1254
- https://doi.org/10.1083/jcb.111.3.1245
Abstract
We studied the distribution of the alpha 1-alpha 6 subunits of beta 1 integrins in developing and adult human kidney using a panel of mAbs in indirect immunofluorescence microscopy. Uninduced mesenchyme displayed a diffuse immunoreactivity for only the alpha 1 integrin subunit. At the S-shaped body stage of nephron development, several of the alpha subunits were characteristically expressed in distinct fetal nephron segments, and the pattern was retained also in the adult nephron. Thus, the alpha 1 subunit was characteristically expressed in mesangial and endothelial cells, the alpha 2 in glomerular endothelium and distal tubules, the alpha 3 in podocytes, Bowman's capsule, and distal tubules, and the alpha 6 subunit basally in all tubules, and only transiently in podocytes during development. Unlike the alpha 3 and alpha 6 subunits, the alpha 2 subunit displayed an overall cell surface distribution in distal tubules. It was also distinctly expressed in glomerular endothelia during glomerulogenesis. The beta 4 subunit was expressed only in fetal collecting ducts, and hence the alpha 6 subunit seems to be complexed with the beta 1 rather than beta 4 subunit in human kidney. Of the two fibronectin receptor alpha subunits, alpha 4 and alpha 5, only the latter was expressed, confined to endothelia of developing and adult blood vessels, suggesting that these receptor complexes play a minor role during nephrogenesis. The present results suggest that distinct integrins play a role during differentiation of specific nephron segments. They also indicate that alpha 3 beta 1 and alpha 6 beta 1 integrin complexes may function as basement membrane receptors in podocytes and tubular epithelial cells.This publication has 77 references indexed in Scilit:
- Antibody to integrin α6 subunit specifically inhibits cell-binding to laminin fragment 8Experimental Cell Research, 1990
- Epithelial-mesenchymal interactions regulate the stage-specific expression of a cell surface proteoglycan, syndecan, in the developing kidneyDevelopmental Biology, 1989
- Integrin heterodimer and receptor complexity in avian and mammalian cells.The Journal of cell biology, 1989
- A substrate of the cell-attachment sequence of fibronectin (Arg-Gly-Asp-Ser) is sufficient to promote transition of arterial smooth muscle cells from a contractile to a synthetic phenotypeDevelopmental Biology, 1989
- High resolution immunoelectron microscopic localization of functional domains of laminin, nidogen, and heparan sulfate proteoglycan in epithelial basement membrane of mouse cornea reveals different topological orientations.The Journal of cell biology, 1988
- FIBRONECTIN AND ITS RECEPTORSAnnual Review of Biochemistry, 1988
- An antibody to a receptor for fibronectin and laminin perturbs cranial neural crest development in vivoDevelopmental Biology, 1986
- Cell-adhesion molecule uvomorulin during kidney developmentDevelopmental Biology, 1985
- Shift in collagen type as an early response to induction of the metanephric mesenchyme.The Journal of cell biology, 1981
- In vitro segregation of the metanephric nephronDevelopmental Biology, 1981