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Low protein
About: Low protein is a research topic. Over the lifetime, 8139 publications have been published within this topic receiving 213225 citations.
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TL;DR: Results implicate arginine as a key component in the beneficial effects of low protein diet after induction of glomerulonephritis by injection of an antibody reactive to glomerular mesangial cells.
Abstract: We have previously shown beneficial effects of dietary protein restriction on transforming growth factor beta (TGF-beta) expression and glomerular matrix accumulation in experimental glomerulonephritis. We hypothesized that these effects result from restriction of dietary L-arginine intake. Arginine is a precursor for three pathways, the products of which are involved in tissue injury and repair: nitric oxide, an effector molecule in inflammatory and immunological tissue injury; polyamines, which are required for DNA synthesis and cell growth; and proline, which is required for collagen production. Rats were fed six isocaloric diets differing in L-arginine and/or total protein content, starting immediately after induction of glomerulonephritis by injection of an antibody reactive to glomerular mesangial cells. Mesangial cell lysis and monocyte/macrophage infiltration did not differ with diet. However, restriction of dietary L-arginine intake, even when total protein intake was normal, resulted in decreased proteinuria, decreased expression of TGF-beta 1 mRNA and TGF-beta 1 protein, and decreased production and deposition of matrix components. L-Arginine, but not D-arginine, supplementation to low protein diets reversed these effects. These results implicate arginine as a key component in the beneficial effects of low protein diet.
73 citations
TL;DR: The results indicate that the protection from chemotoxicity and retardation of the progression of certain tumors achieved with fasting is not obtained with short-term calorie and/or macronutrient restriction.
73 citations
TL;DR: The results provide further support for a condensation mode of low protein chromatins that involves a liquid-crystalline organization of the DNA filaments in terms of intracellular packing densities.
73 citations
TL;DR: Evidence suggests that the phosphorylated form of enzyme I is more stable, and kinetics that are consistent with a bi bi Ping-Pong mechanism are suggested.
Abstract: Enzyme I of the phosphoenolpyruvate - sugar phosphotransferase system (PTS) has been purified to homogeneity from Escherichia coli. A merodiploid strain P650 which had an extra copy of the gene for enzyme I resulting in a twofold increase in the amount of activity was used. The enzyme is a dimer of 67 000 +/- 5000 molecular weight subunits. At low protein concentration and 4 degrees C the monomer predominates, while at room temperature the dimer predominates. At higher protein concentrations (2 to 10 mg) this reversible temperature-dependent association-dissociation is not found. Enzyme I has a pH optimum of pH 7.2, a Km for HPr of 9 +/- 3 microM, a Km for phosphoenolpyruvate of 0.18 +/- 0.04 mM, and kinetics that are consistent with a bi bi Ping-Pong mechanism. No allosteric regulation of kinetic activity has been found. The amino acid composition has been determined and the epsilon 1% 280 nm is 4.4. Evidence suggests that the phosphorylated form of enzyme I is more stable.
73 citations
TL;DR: A new concentration-shift method was proposed to cultivate heterotrophic Chlorella vulgaris, aiming to increase protein content, with a prior starvation period, whereby microalgae utilized more nitrate and accumulated more proteins compared to one-stage cultivation.
73 citations