Organ specific underexpression renal of Na+-dependent B0AT1 in the SHR correlates positively with overexpression of NHE3 and salt intake |
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Authors: | Maria João Pinho Maria Paula Serrão Pedro A José Patrício Soares-da-Silva |
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Institution: | (1) Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland;(2) Department of Anatomy, University of Greifswald, Greifswald, Germany |
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Abstract: | Densin is a member of LAP (leucine-rich repeat and PDZ domain) protein family that localizes in kidney to slit diaphragms,
which are essential components of the glomerular filtration barrier. We have previously shown that densin interacts with a
crucial slit diaphragm protein, nephrin. Here, we searched for novel binding partners of densin by yeast-two hybrid assay
and identified beta-catenin. The interaction was confirmed by reciprocal co-immunoprecipitation assay and the binding site
in densin was determined by GST-pull down assays. The GST-tagged densin was also able to pull down P-cadherin together with
beta-catenin from human kidney glomerular lysates. Furthermore, densin co-localized with beta-catenin and F-actin in cell–cell
contacts in cultured mouse podocytes. During cell–cell contact disruption and reformation densin and beta-catenin were dislocated
from and relocated back to plasma membrane in a similar fashion. These and our previous findings suggest that densin may associate
with the cadherin-catenin and nephrin complex(es), and may be involved in the formation of the cell–cell contacts including
the slit diaphragm. |
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Keywords: | Densin Cell– cell contact Catenin/cadherin complex Nephrin |
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