Mechanisms Involved in the Progression to Glomerular Sclerosis Induced by Systemic Hypertension During Mild Puromycin Aminonucleoside Nephrosis

1992 ◽  
Vol 5 (9) ◽  
pp. 629-636 ◽  
Author(s):  
D. Amato ◽  
E. Tapia ◽  
N. A. Bobadilla ◽  
M. Franco ◽  
C. Calleja ◽  
...  
1993 ◽  
Vol 84 (3) ◽  
pp. 349-356 ◽  
Author(s):  
Tsukasa Nakamura ◽  
Isao Ebihara ◽  
Mitsumine Fukui ◽  
Toshimasa Takahashi ◽  
Yasuhiko Tomino ◽  
...  

1. We determined glomerular and medullary tumour necrosis factor-α mRNA levels in acute puromycin aminonucleoside nephrosis on days 0, 8 and 20. 2. Tumour necrosis factor-α mRNA levels were increased fourfold in glomeruli and twofold in the medulla during the nephrotic stage of acute puromycin aminonucleoside nephrosis (day 8). 3. The high tumour necrosis factor-α mRNA levels in both glomeruli and the medulla were ameliorated significantly by methylprednisolone administration. 4. Focal glomerular sclerosis was induced in rats by injection of puromycin aminonucleoside on days 0, 27, 34 and 41 and by unilateral nephrectomy on day 22. 5. The percentage of sclerosing glomeruli was 16.6% on day 48 and had increased significantly to 72.8% on day 80. 6. During the sclerotic phase of puromycin amino-nucleoside nephrosis, glomerular tumour necrosis factor-α mRNA levels increased as glomerular sclerosis progressed. On day 80, glomerular tumour necrosis factor-α mRNA levels were 13-fold higher than levels in control rats. 7. These data suggest that glomerular tumour necrosis factor-α mRNA expression is associated with the development of puromycin aminonucleoside-induced glomerular sclerosis.


2004 ◽  
Vol 19 (4) ◽  
pp. 817-822 ◽  
Author(s):  
Y. Watanabe ◽  
T. Kobayashi ◽  
E. Yaoita ◽  
H. Kawachi ◽  
A. Yamauchi ◽  
...  

1995 ◽  
Vol 89 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Tsukasa Nakamura ◽  
Kenjiro Kimura ◽  
Isao Ebihara ◽  
Toshimasa Takahashi ◽  
Yasuhiko Tomino ◽  
...  

1. We investigated the glomerular expression of three types of myosin heavy-chain isoforms, including S-myosin heavy-chain 40 (SM1), S-myosin heavy-chain 29 (SM2) and FS-myosin heavy-chain 34 (SMemb) in puromycin aminonucleoside nephrosis. 2. There was little change in SM1 and SM2 mRNA levels throughout the experiment. In contrast, glomerular SMemb mRNA increased on days 2 and 4 (before and soon after the onset of proteinuria, respectively), but declined on day 8 (the peak of proteinuria). 3. Histological myosin heavy-chain expression was examined using three antibodies against SM1, SM2 and SMemb. Immunohistochemically, SM1 and SM2 were absent in the glomeruli associated with puromycin aminonucleoside nephrosis until day 20. The SMemb isoform was barely detectable in normal glomeruli, but substantial amounts of SMemb were demonstrated in the glomeruli of rats with puromycin aminonucleoside nephrosis. In the puromycin aminonucleoside-treated rats, the number of SMemb-positive glomerular cells increased on days 2 and 4. 4. We examined whether levels of α-smooth-muscle actin or proliferating cell nuclear antigen correlated with myosin heavy-chain levels in the glomeruli of rats with puromycin aminonucleoside nephrosis. None of the cellular components in the glomeruli was positive for either α-smooth-muscle actin or proliferating cell nuclear antigen in puromycin aminonucleoside nephrosis. 5. Administration of methylprednisolone to puromycin aminonucleoside-treated rats resulted in the rapid disappearance of proteinuria. However, methylprednisolone did not affect SMemb mRNA or immunostaining in the glomeruli of rats with puromycin aminonucleoside nephrosis. 6. These data suggest that SMemb may be a molecular marker for phenotypic change in early glomerular injury, and demonstrate that SMemb regulation differs from that of SM1, SM2, α-smooth-muscle actin and proliferating cell nuclear antigen in the glomeruli of rats with puromycin aminonucleoside nephrosis.


2015 ◽  
Vol 95 (9) ◽  
pp. 1019-1028 ◽  
Author(s):  
Izabella Z A Pawluczyk ◽  
Maryam G Najafabadi ◽  
Jeremy R Brown ◽  
Alan Bevington ◽  
Peter S Topham

2005 ◽  
Vol 68 (2) ◽  
pp. 542-551 ◽  
Author(s):  
Eishin Yaoita ◽  
Hidetake Kurihara ◽  
Yutaka Yoshida ◽  
Tsutomu Inoue ◽  
Asako Matsuki ◽  
...  

2004 ◽  
Vol 54 (9) ◽  
pp. 703-711 ◽  
Author(s):  
Na Guan ◽  
Jie Ding ◽  
Jianghong Deng ◽  
Jingjing Zhang ◽  
Jiyun Yang

2011 ◽  
Vol 2011 ◽  
pp. 1-10 ◽  
Author(s):  
Lamine Aoudjit ◽  
Ruihua Jiang ◽  
Tae Hoon Lee ◽  
Laura A. New ◽  
Nina Jones ◽  
...  

Glomerular podocytes are critical for the barrier function of the glomerulus in the kidney and their dysfunction causes protein leakage into the urine (proteinuria). Nephrin is a key podocyte protein, which regulates the actin cytoskeleton via tyrosine phosphorylation of its cytoplasmic domain. Here we report that two protein tyrosine phosphatases, PTP1B and PTP-PEST negatively regulate nephrin tyrosine phosphorylation. PTP1B directly binds to and dephosphorylates nephrin, while the action of PTP-PEST is indirect. The two phosphatases are also upregulated in the glomerulus in the rat model of puromycin aminonucleoside nephrosis. Both overexpression and inhibition of PTP1B deranged the actin cytoskeleton in cultured mouse podocytes. Thus, protein tyrosine phosphatases may affect podocyte function via regulating nephrin tyrosine phosphorylation.


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