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NDT Advance Access published online on January 21, 2009
Nephrology Dialysis Transplantation, doi:10.1093/ndt/gfn743
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© The Author [2009].
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org


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

Jenny Nyström1, Kjell Hultenby2, Sara Ek3, Jonas Sjölund4, Håkan Axelson4, Karin Jirström4, Moin A. Saleem5, Kristina Nilsson4 and Martin E. Johansson4

1 Department of Nephrology, Göteborg University, Gothenburg 2 Division of Electron Microscopy, Karolinska University Hospital, Huddinge, Karolinska Institutet, Stockholm 3 Lund University, Department of Immunotechnology, CREATE Health, BioMedical Center 4 Department of Laboratory Medicine, Center for Molecular Pathology, Lund University, University Hospital MAS, Malmö, Sweden 5 Academic Renal Unit, University of Bristol, Bristol, UK

Correspondence and offprint requests to: Martin E. Johansson, Department of Laboratory Medicine, Center for Molecular Pathology, University Hospital MAS, Entrance 78, S-205 02 Malmö, Sweden. Tel: +46-40-337387; Fax +46-40-337322; E-mail: martin.johansson{at}med.lu.se



  Abstract

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.

Keywords: bone morphogenic protein; filtration slit membrane; immunoelectron microscopy; podocyte

Received for publication: 14. 5.08
Accepted in revised form: 11.12.08


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