scholarly journals Effects of Dietary Salt Restriction on Puromycin Aminonucleoside Nephrosis: Preliminary Data

2011 ◽  
Vol 9 (2) ◽  
pp. 55 ◽  
Author(s):  
Chor Ho Jo ◽  
Sua Kim ◽  
Joon-Sung Park ◽  
Gheun-Ho Kim
Keyword(s):  
Preliminary Data ◽  
Dietary Salt ◽  
Puromycin Aminonucleoside ◽  
Salt Restriction ◽  
Dietary Salt Restriction ◽  
Aminonucleoside Nephrosis ◽  
Puromycin Aminonucleoside Nephrosis

scholarly journals Novel expression of sodium/myo-inositol co-transporter in podocytes in puromycin aminonucleoside nephrosis

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

Dietary salt restriction accelerates atherosclerosis in apolipoprotein E-deficient mice

2005 ◽  
Vol 180 (2) ◽  
pp. 271-276 ◽  
Author(s):  
Ognen Ivanovski ◽  
Dorota Szumilak ◽  
Thao Nguyen-Khoa ◽  
Michele Dechaux ◽  
Ziad A. Massy ◽  
...  
Keyword(s):  
Apolipoprotein E ◽  
Dietary Salt ◽  
Salt Restriction ◽  
Dietary Salt Restriction ◽  
Deficient Mice

Glomerular Expression of Smooth-Muscle Myosin Heavy-Chain Isoforms in Aminonucleoside Nephrosis in Rats

1995 ◽  
Vol 89 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Tsukasa Nakamura ◽  
Kenjiro Kimura ◽  
Isao Ebihara ◽  
Toshimasa Takahashi ◽  
Yasuhiko Tomino ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Proliferating Cell Nuclear Antigen ◽  
Smooth Muscle Actin ◽  
Nuclear Antigen ◽  
Puromycin Aminonucleoside ◽  
Proliferating Cell ◽  
Aminonucleoside Nephrosis ◽  
Puromycin Aminonucleoside Nephrosis

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.

Differential Regulation of the Epithelial Sodium Channel (ENaC) in Rat Kidney, Lung and Distal Colon in Response to Aldosterone.

Hypertension ◽  
2000 ◽  
Vol 36 (suppl_1) ◽  
pp. 724-724
Author(s):  
Shyama M E Masilamani ◽  
Gheun-Ho Kim ◽  
Mark A Knepper
Keyword(s):  
Sodium Channel ◽  
Epithelial Sodium Channel ◽  
Distal Colon ◽  
Β Subunit ◽  
Dietary Salt ◽  
Α Subunit ◽  
Salt Restriction ◽  
Γ Subunit ◽  
Dietary Salt Restriction ◽  
Epithelial Sodium Channel Enac

P170 The mineralocorticoid hormone, aldosterone increases renal tubule Na absorption via increases in the protein abundances of the α-subunit of the epithelial sodium channel (ENaC) and the 70 kDa form of the γ- subunit of ENaC (JCI 104:R19-R23). This study assesses the affect of dietary salt restriction on the regulation of the epithelial sodium channel (ENaC) in the lung and distal colon, in addition to kidney, using semiquantitative immunoblotting. Rats were placed initially on either a control Na intake (0.02 meq/day), or a low Na intake (0.2 meq/day) for 10 days. The low salt treated rats demonstrated an increase in plasma aldosterone levels at day 10 (control = 0.78 + 0.32 nM; Na restricted = 3.50 + 1.30 nM). In kidney homogenates, there were marked increases in the band density of the α-subunit of ENaC (286 % of control) and the 70 kDa form of γ-subunit of ENaC (262 % of control), but no increase in the abundance of the β-subunit of ENaC. In lung homogenates, there was no significant change in the band densities of the α, β, or γ subunits of ENaC. In distal colon, there was an increase in the band density of the β-subunit of ENaC (311 % of control) and an increase in both the 85 kDa (2355% of control) and 70 kDa (843 % of control) form of the γ subunit of ENaC in response to dietary Na restriction. However, there was no significant difference in the band density of the α-subunit of ENaC. These findings demonstrate tissue specific regulation of the three subunits of ENaC in response to dietary salt restriction.

Mobilization of osmotically inactive Na+ by growth and by dietary salt restriction in rats

2007 ◽  
Vol 292 (5) ◽  
pp. F1490-F1500 ◽  
Author(s):  
Markus Schafflhuber ◽  
Nicola Volpi ◽  
Anke Dahlmann ◽  
Karl F. Hilgers ◽  
Francesca Maccari ◽  
...  
Keyword(s):  
Binding Capacity ◽  
Dry Weight ◽  
Sprague Dawley ◽  
Dietary Salt ◽  
Salt Restriction ◽  
Sprague Dawley Rats ◽  
Low Salt ◽  
Total Body ◽  
Dietary Salt Restriction

The idea that an osmotically inactive Na+ storage pool exists that can be varied to accommodate states of Na+ retention and/or Na+ loss is controversial. We speculated that considerable amounts of osmotically inactive Na+ are lost with growth and that additional dietary salt excess or salt deficit alters the polyanionic character of extracellular glycosaminoglycans in osmotically inactive Na+ reservoirs. Six-week-old Sprague-Dawley rats were fed low-salt (0.1%; LS) or high-salt (8%; HS) diets for 1 or 4 wk. At their death, we separated the tissues and determined their Na+, K+, and water content. Three weeks of growth reduced the total body Na+ content relative to dry weight (rTBNa+) by 23%. This “growth-programmed” Na+ loss originated from the bone and the completely skinned and bone-removed carcasses. The Na+ loss was osmotically inactive (45–50%) or osmotically active (50–55%). In rats aged 10 wk, compared with HS, 4 wk of LS reduced rTBNa+ by 9%. This dietary-induced Na+ loss was osmotically inactive (≈50%) and originated largely from the skin, while ≈50% was osmotically active. LS for 1 wk did not reduce skin Na+ content. The mobilization of osmotically inactive skin Na+ with long-term salt deprivation was associated with decreased negatively charged skin glycosaminoglycan content and thereby a decreased water-free Na+ binding capacity in the extracellular matrix. Our data not only serve to explain discrepant results in salt balance studies but also show that glycosaminoglycans may provide an actively regulated interstitial cation exchange mechanism that participates in volume and blood pressure homeostasis.

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