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CRIM1 is localized to the podocyte filtration slit diaphragm of the adult human kidney

Publiceringsår: 2009
Språk: Engelska
Sidor: 2038-2044
Publikation/Tidskrift/Serie: Nephrology Dialysis Transplantation
Volym: 24
Nummer: 7
Dokumenttyp: Artikel
Förlag: Oxford University Press


Background. CRIM1 is a plasma membrane bound protein
containing six cysteine-rich repeats (CRR). Through these,
CRIM1 has been shown to interact with a subgroup of the
TGF-β superfamily, the bone morphogenic proteins (BMP)
isoforms 2, 4 and 7. The probable action is to modulate
the signalling properties of these factors. CRIM1 has also
been shown to regulate the release of VEGFA by podocytes
during renal organogenesis. Knock-out studies in mice have
shown that CRIM1 is critically involved in the development
of the central nervous system, eye and kidney. Replacement
of CRIM1 with a defective version leads to renal dysgenesis
and perinatal death. We have analysed the distribution of
CRIM1 in adult human renal tissue.
Methods. To this end, we have used immunofluorescence,
immunohistochemistry and immunoelectron microscopy.
We performed western blotting for the CRIM1 protein,
using lysates from isolated glomerular podocytes and human
renal tissue homogenate. By using quantitative PCR,
we compared the CRIM1 mRNA levels in podocytes, human
renal tissue homogenate, primary human renal proximal
tubular epithelial cells and primary human pulmonary
artery smooth muscle cells.
Results. The results show that in the human adult kidney,
CRIM1 is mainly expressed in the glomerular podocytes
and is associated with the insertional region of the filtration
slit diaphragm (SD) of the podocyte pedicles.
Conclusions. CRIM1 is a protein that should be added to
the list of proteins associated with the podocyte filtration
SD and with the probable action of modulating BMP and
VEGFA signalling.



  • Urology and Nephrology
  • podocyte
  • immunoelectron microscopy
  • bone morphogenic protein
  • filtration slit membrane


  • ISSN: 0931-0509

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