scholarly journals Leukotriene C4 binds to human glomerular epithelial cells and promotes their proliferation in vitro.

1985 ◽  
Vol 76 (1) ◽  
pp. 374-377 ◽  
Author(s):  
L Baud ◽  
J Sraer ◽  
J Perez ◽  
M P Nivez ◽  
R Ardaillou
1979 ◽  
Vol 15 (1) ◽  
pp. 80-87 ◽  
Author(s):  
Peter M. Andrews ◽  
Marguerite Stauver

1999 ◽  
Vol 2 (2) ◽  
pp. 170-175 ◽  
Author(s):  
Pi-Chao Wang ◽  
Kenichi Horisawa ◽  
Masatoshi Matsumura

1994 ◽  
Vol 45 (1) ◽  
pp. 43-47 ◽  
Author(s):  
Paul A.J. Brown ◽  
Heather M. Wilson ◽  
Fiona J. Reid ◽  
Nuala A. Booth ◽  
John G. Simpson ◽  
...  

2003 ◽  
Vol 285 (4) ◽  
pp. F765-F774 ◽  
Author(s):  
Lamine Aoudjit ◽  
Monica Stanciu ◽  
Hongping Li ◽  
Serge Lemay ◽  
Tomoko Takano

In the passive Heymann nephritis (PHN) model of rat membranous nephropathy, complement C5b-9 causes sublytic injury of glomerular epithelial cells (GEC). We previously showed that sublytic concentration of C5b-9 triggers a variety of biological events in GEC. In the current study, we demonstrate that complement activates p38 MAPK in GEC and address the role of p38 in complement-mediated cell injury. When cultured rat GEC were stimulated with complement, p38 kinase activity and phosphorylation were increased by ∼2.4-fold, compared with control. Treatment with p38 inhibitors significantly augmented complement-mediated cytotoxicity. In contrast, when the constitutively active mutant of transforming growth factor-β-activated kinase 1 (TAK1), a kinase upstream of p38, was expressed in GEC in an inducible manner, cytotoxicity was significantly reduced, compared with uninduced cells. p38 inhibitors abolished the protective effect of TAK1 expression. By analogy to cultured cells, p38 activity was also increased in glomeruli from rats with PHN and treatment with the p38 inhibitor FR-167653 increased proteinuria. Complement induced phosphorylation of MAPK-associated protein kinase-2 (MAPKAPK-2), a kinase downstream of p38 in GEC. Heat shock protein (HSP27) is a cytoskeleton-interacting substrate of MAPKAPK-2. Overexpression of the wild-type HSP27, but not a non-phosphorylatable mutant, markedly reduced complement-mediated GEC injury. In summary, complement activates p38 MAPK in GEC in vitro and in glomeruli from rats with PHN. The activation of p38 MAPK appears to be cytoprotective for GEC against complement-mediated GEC injury. Phosphorylation of HSP27 may mediate this cytoprotection.


2001 ◽  
Vol 101 (4) ◽  
pp. 439-446 ◽  
Author(s):  
Steven J. HARPER ◽  
Chang Ying XING ◽  
Cathy WHITTLE ◽  
Robin PARRY ◽  
David GILLATT ◽  
...  

Vascular endothelial growth factor (VEGF) is a potent promoter of endothelial mitogenesis and of endothelial permeability. Within the kidney it is synthesized primarily in the visceral glomerular epithelial cells (vGECs); however, the role of VEGF in the glomerulus remains unknown, as does the target cell upon which it acts. Although the target cells may be those of the glomerular endothelium, there are micro-anatomical reasons why this might not be the case. This, therefore, led us to consider the possibility that glomerular VEGF may bind to the vGECs themselves. Since it has been shown that vGECs do not express the main tyrosine kinase VEGF receptors, we chose to study vGEC expression of the more recently described VEGF isoform-specific receptors, the neuropilins. The expression of mRNAs for neuropilin-1, neuropilin-2 and soluble neuropilin was studied in whole kidney, sieved glomeruli and cultured podocytes by reverse transcription-PCR, and neuropilin-1 mRNA expression in isolated single glomeruli was analysed by nested reverse transcription-PCR. The expression of neuropilin-1 protein was investigated in cultured vGECs by Western blotting and immunocytochemistry, and in normal kidney sections by immunohistochemistry. Neuropilin-1 mRNA was detected in whole kidney, single and sieved glomeruli and cultured vGECs. Neuropilin-1 protein was detected in cultured vGECs and in vGECs in normal kidney sections by immunohistochemistry. Thus the present study suggests that vGECs may have the potential to bind the VEGF that they secrete. Functional studies will be required to address the potential significance of this finding in terms of an autocrine loop or VEGF sequestration.


Nephron ◽  
1994 ◽  
Vol 68 (1) ◽  
pp. 97-103 ◽  
Author(s):  
Makoto Kawaguchi ◽  
Fumie Kawashima ◽  
Keisuke Ohshima ◽  
Satoru Kawaguchi ◽  
Hiroyoshi Wada

1990 ◽  
Vol 3 (3) ◽  
pp. 245-251
Author(s):  
Masayasu Yamada ◽  
Chiharu Moritoh ◽  
Tohru Okigaki

2001 ◽  
Vol 101 (4) ◽  
pp. 439 ◽  
Author(s):  
Steven J. HARPER ◽  
Chang Ying XING ◽  
Cathy WHITTLE ◽  
Robin PARRY ◽  
David GILLATT ◽  
...  

Author(s):  
Gian Marco Ghiggeri ◽  
Roberta Bertelli ◽  
Fabrizio Ginevri ◽  
Roberta Oleggini ◽  
Paola Altieri ◽  
...  

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