scholarly journals Effect of a low-protein diet on expression of non-muscle type myosin heavy-chain isoforms in glomeruli of rats with puromycin aminonucleoside nephrosis

1996 ◽  
Vol 11 (9) ◽  
pp. 1769-1774
Author(s):  
H. Koide ◽  
T. Nakamura ◽  
K. Kimura ◽  
I. Ebihara ◽  
R. Nagai ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Muscle Type ◽  
Puromycin Aminonucleoside ◽  
Low Protein ◽  
Aminonucleoside Nephrosis ◽  
Puromycin Aminonucleoside Nephrosis

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.

Effects of a Low-Protein Diet on Glomerular Endothelin Family Gene Expression in Experimental Focal Glomerular Sclerosis

1995 ◽  
Vol 88 (1) ◽  
pp. 29-37 ◽  
Author(s):  
Tsukasa Nakamura ◽  
Mitsumine Fukui ◽  
Isao Ebihara ◽  
Shiori Osada ◽  
Toshimasa Takahashi ◽  
...  
Keyword(s):  
Protein Diet ◽  
Low Protein Diet ◽  
Endothelin Receptors ◽  
Glomerular Sclerosis ◽  
Standard Diet ◽  
Mrna Levels ◽  
Puromycin Aminonucleoside ◽  
Endothelin 1 ◽  
Low Protein ◽  
Focal Glomerular Sclerosis

1. The present study was designed to assess whether glomerular expression of mRNAs for endothelin-1 and endothelin-3, as well as endothelin receptors A and B is affected by a low-protein diet during the course of focal glomerular sclerosis. 2. Focal glomerular sclerosis was induced in rats by injection of puromycin aminonucleoside on days 0, 27, 34 and 41 in conjunction with unilateral nephrectomy on day 22. Control rats were subjected to nephrectomy or sham operation on day 22. 3. Animals were divided into six groups. In group 1, the puromycin aminonucleoside-injected rats were fed a standard diet containing 22% protein. In group 2, the puromycin aminonucleoside-injected rats were fed a low-protein diet containing 6% protein, which was initiated on the day of the first puromycin aminonucleoside injection. In group 3, the nephrectomized rats without puromycin aminonucleoside were fed a standard diet. In group 4, the nephrectomized rats without puromycin aminonucleoside were fed a low-protein diet. In group 5, the sham-operated rats were fed a standard diet. In group 6, the sham-operated rats were fed a low-protein diet. 4. The percentage of sclerotic glomeruli in group 1 rats increased markedly with time, reaching 77% on day 80. 5. The glomerular mRNA levels for endothelin-1 and endothelin receptors A and B increased significantly as glomerular sclerosis progressed, whereas no endothelin-3 mRNA was detected in the glomeruli of any group. 6. The endothelin-1 production in isolated glomeruli from group 1 increased significantly as glomerular sclerosis progressed. 7. In group 2, the low-protein diet reduced the prevalence of glomerular sclerosis, attenuated the rise in mRNA levels for endothelin-1 and endothelin receptors A and B and reduced endothelin-1 production in glomeruli from rats with focal glomerular sclerosis. 8. These data indicate that increases in glomerular endothelin-1 and endothelin receptor mRNA levels are associated with the development of puromycin aminonucleoside-induced glomerular sclerosis. These effects are blunted by administration of a low-protein diet.

Smooth muscle-type myosin heavy chain isoforms in bovine smooth muscle and non-muscle tissues

1996 ◽  
Vol 86 (1) ◽  
pp. 27-38 ◽  
Author(s):  
Angela Chiavegato ◽  
Paolo Pauletto ◽  
Saverio Sartore
Keyword(s):  
Smooth Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Type ◽  
Muscle Tissues

scholarly journals Expression of SERCA2a is independent of innervation in regenerating soleus muscle

2003 ◽  
Vol 285 (4) ◽  
pp. C853-C861 ◽  
Author(s):  
Ernő Zádor ◽  
Frank Wuytack
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Mrna Level ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Type ◽  
Protein Levels ◽  
Constitutively Active Mutants ◽  
Slow Type

The speed of contraction of a skeletal muscle largely depends on the myosin heavy chain isoforms (MyHC), whereas the relaxation is initiated and maintained by the sarcoplasmic reticulum Ca2+-ATPases (SERCA). The expression of the slow muscle-type myosin heavy chain I (MyHCI) is entirely dependent on innervation, but, as we show here, innervation is not required for the expression of the slow-type sarcoplasmic reticulum Ca2+-ATPase (SERCA2a) in regenerating soleus muscles of the rat, although it can play a modulator role. Remarkably, the SERCA2a level is even higher in denervated than in innervated regenerating soleus muscles on day 7 when innervation is expected to resume. Later, the level of SERCA2a protein declines in denervated regenerated muscles but it remains expressed, whereas the corresponding mRNA level is still increasing. SERCA1 (i.e., the fast muscle-type isoform) expression shows only minor changes in denervated regenerating soleus muscles compared with innervated regenerating controls. When the soleus nerve was transected instead of the sciatic nerve, SERCA2a and MyHCI expressions were found to be even more uncoupled because the MyHCI nearly completely disappeared, whereas the SERCA2a mRNA and protein levels decreased much less. The transfection of regenerating muscles with constitutively active mutants of the Ras oncogene, known to mimic the effect of innervation on the expression of MyHCI, did not affect SERCA2a expression. These results demonstrate that the regulation of SERCA2a expression is clearly distinct from that of the slow myosin in the regenerating soleus muscle and that SERCA2a expression is modulated by neuronal activity but is not entirely dependent on it.

Hepatic Ultrastructure Changes Induced by Lithocholic Acid

1967 ◽  
Vol 25 ◽  
pp. 162-163 ◽  
Author(s):  
F. G. Zaki
Keyword(s):  
Endoplasmic Reticulum ◽  
Lithocholic Acid ◽  
Smooth Endoplasmic Reticulum ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Electron Microscopic ◽  
Hydropic Degeneration ◽  
Hepatic Cells ◽  
Low Protein ◽  
Microscopic Studies

Addition of lithocholic acid (LCA), a naturally occurring bile acid in mammals, to a low protein diet fed to rats induced marked inflammatory reaction in the hepatic cells followed by hydropic degeneration and ductular cell proliferation. These changes were accompanied by dilatation and hyperplasia of the common bile duct and formation of “gallstones”. All these changes were reversible when LCA was withdrawn from the low protein diet except for the hardened gallstones which persisted.Electron microscopic studies revealed marked alterations in the hepatic cells. Early changes included disorganization, fragmentation of the rough endoplasmic reticulum and detachment of its ribosomes. Free ribosomes, either singly or arranged in small clusters were frequently seen in most of the hepatic cells. Vesiculation of the smooth endoplasmic reticulum was often encountered as early as one week after the administration of LCA (Fig. 1).

Economic Effects of Treatment of Chronic Kidney Disease with Low-Protein Diet

2013 ◽  
Author(s):  
Francesco Saverio Mennini ◽  
Simone Russo ◽  
Andrea Marcellusi ◽  
Giuseppe Quintaliani ◽  
Denis Fouque
Keyword(s):  
Chronic Kidney Disease ◽  
Kidney Disease ◽  
Economic Effects ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Low Protein

scholarly journals PSIV-6 Effect of a Phytogenic Water Additive on Growth Performance, Blood Metabolites and Gene Expression of Amino Acids Transporters in Nursery Pigs Fed with Low Protein Diets

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 281-282
Author(s):  
Cedrick N Shili ◽  
Mohammad Habibi ◽  
Julia Sutton ◽  
Jessie Barnes ◽  
Jacob Burchkonda ◽  
...  
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Growth Performance ◽  
Mrna Abundance ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Blood Calcium ◽  
Low Protein ◽  
Protein Diets ◽  
Standard Protein

Abstract Moderately low protein (MLP) diets can help decrease nutrient excretion from the swine production. However, MLP diets negatively impact growth performance. We hypothesized that supplementing MLP diets with phytogenics may reduce the negative effects of these diets on growth. The objective of this study was to investigate the effect of a phytogenic water additive (PWA; Herbanimal®) on growth performance, blood metabolite and gene expression of amino acids transporters in pigs fed with MLP diets. Forty-eight weaned barrows were allotted to six dietary treatments (n = 8) for 4 weeks: >CON-NS: standard protein diet-no PWA; CON-LS: standard protein diet-low PWA dose (4 ml/L); CON-HS: standard protein diet-high PWA dose (8 ml/L); LP-NS: low protein diet-no PWA; LP-LS: low protein diet-low PWA dose (4 ml/L); LP-HS: low protein diet- high PWA dose (8 ml/L). Feed intake and body weight were recorded daily and weekly, respectively. At week 4, blood and tissue samples were collected and analyzed for metabolites using a chemistry analyzer and amino acid transporters using qPCR, respectively. The data were analyzed by univariate GLM (SPSS®) and the means were separated using paired Student’s t-test corrected by Benjamini-Hochberg. Pigs fed CON-HS improved the average daily gain and serum calcium and phosphorus concentrations compared to CON-NS. Pigs fed LP-LS had higher serum phosphorus and blood urea nitrogen compared to the pigs fed with LP-NS. The mRNA abundance of SLC7A11 in the jejunum was lower in CON-LS and CON-HS compared to CON-NS. Additionally, mRNA abundance of SLC6A19 in the jejunum of pigs fed with LP-LS was higher compared to LP-NS and lower in CON-HS relative to pigs fed with CON-LS. In conclusion, PWA improved the growth performance of pigs fed standard protein diets but not low protein diets. Further, the PWA improved the concentrations of blood calcium and phosphorous in pigs fed MLP diets. Funding: Agrivida and Animal Health and Production and Animal Products: Improved Nutritional Performance, Growth, and Lactation of Animals from the USDA-NIFA.

Sign in / Sign up

Export Citation Format

Share Document