Threonine-deficient diets induced changes in hepatic bioenergetics

Ross-Inta, Catherine; Zhang, Yi Fan; Almendares, Andrew; Giulivi, Cecilia R

doi:10.1152/ajpgi.90545.2008

Cited by 33 publications

(25 citation statements)

References 53 publications

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“…Male, 4-wks old Sprague-Dawley rats were fed with an amino-acid based diet containing all nutrients for adequate growth (diet with 0.87% Thr as described in [11]). To determine the amino acid levels present in liver mitochondria, and considering that these concentrations fluctuate significantly after or before a meal [12, 13], it is important to indicate that the rats used in this study were euthanized between 9 and 10 am, about 2–3 hours after their first meal, thus, the amino acid pool reported in this study should be taken as representative of a postprandial period.…”

Section: Resultsmentioning

confidence: 99%

The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: indication of a post- translational quality control for protein synthesis

2008

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Mitochondria can synthesize a limited number of proteins encoded by mtDNA by using its own biosynthetic machinery, whereas most of the proteins are imported from the cytosol. It could be hypothesized that the mitochondrial pool of amino acids follows the frequency of amino acids in mtDNA-encoded proteins or alternatively, the profile is the result of the participation of amino acids in pathways other than protein synthesis (e.g. heme biosynthesis, aminotransferase reactions). These hypotheses were tested by evaluating the pool of free amino acids and derivatives in highly-coupled, purified liver mitochondria obtained from rats fed a nutritionally adequate diet for growth. Our results indicated that the pool mainly reflects the amino acid composition of mtDNA-encoded proteins suggesting that there is a posttranslational control of protein synthesis. This conclusion was supported by the following findings: one, correlation between the concentration of free amino acids in the matrix and the frequency of abundance of amino acids in mtDNA-encoded proteins; two, the similar ratios of essential-to-nonessential amino acids in mtDNA-encoded proteins and mitochondrial pool of amino acids; three, lack of a correlation between codon usage or tRNA levels and amino acid concentrations. Quantitative information on the mammalian mitochondrial content of amino acids, such as that presented in this report, along with functional studies will help us better understand the pathogenesis of mitochondrial diseases or the biochemical implications in mitochondrial metabolism.

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Section: Resultsmentioning

confidence: 99%

The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: indication of a post- translational quality control for protein synthesis

2008

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“…In a similar way, as a result of casein supplemented with the amino acid mixture, casein+ provided 23% and 20% less methionine and threonine than cod protein (Table 1), respectively. Therefore casein+ supplied lower amounts of methionine and threonine than cod protein, resulting likely in reduced anabolic and/or anti-catabolic potential [52-54] and slower muscle mass during the recovery period. Further research is needed to study the influence of a supplementation of casein with sulfur amino acids and threonine in addition to arginine, glycine, taurine and lysine on muscle mass regeneration.…”

Section: Discussionmentioning

confidence: 99%

Beneficial Effects of Cod Protein on Inflammatory Cell Accumulation in Rat Skeletal Muscle after Injury Are Driven by Its High Levels of Arginine, Glycine, Taurine and Lysine

et al. 2013

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We have shown that feeding cod protein, which is rich in anti-inflammatory arginine, glycine, and taurine, may beneficially modulate the inflammatory response during recovery following skeletal muscle injury; however it is unknown if these amino acids are responsible for this effect. This study was designed to assess whether supplementing casein with an amino acid mixture composed of arginine, glycine, taurine and lysine, matching their respective levels in cod protein, may account for the anti-inflammatory effect of cod protein. Male Wistar rats were fed isoenergetic diets containing either casein, cod protein, or casein supplemented with L-arginine (0.45%), glycine (0.43%), L-taurine (0.17%) and L-lysine (0.44%) (casein+). After 21 days of ad libitum feeding, one tibialis anterior muscle was injured with 200 µl bupivacaine while the saline-injected contra-lateral tibialis anterior was served as sham. Cod protein and casein+ similarly modulated the inflammation as they decreased COX-2 level at day 2 post-injury (cod protein, p=0.014; casein+, p=0.029) and ED1+ macrophage density at days 2 (cod protein, p=0.012; casein+, p<0.0001), 5 (cod protein, p=0.001; casein+, p<0.0001) and 14 (cod protein, p<0.0001; casein+, p<0.0001) post-injury, and increased ED2+ macrophage density at days 5 (cod protein, p<0.0001; casein+, p=0.006), 14 (cod protein, p=0.001; casein+, p<0.002) and 28 (cod protein, p<0.009; casein+, p<0.005) post-injury compared with casein. Furthermore, cod protein up-regulated (p=0.037) whereas casein+ tended to up-regulate (p=0.062) myogenin expression at day 5 post-injury compared with casein. In the cod protein-fed group, these changes resulted in greater muscle mass at days 14 (p=0.002), and 28 (p=0.001) post-injury and larger myofiber cross-sectional area at day 28 post-injury compared with casein (p=0.012). No such effects were observed with casein+. These data indicate that anti-inflammatory actions of cod protein, contrary to its effect on muscle mass recovery, are driven by its high levels of arginine, glycine, taurine and lysine.

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“…Samples were processed as described in Supplementary Methods. Fat from mosquitoes (30–200/treatment) was determined using Folch extraction, drying the extracted organic layer under nitrogen, and weighing the final dry pellets as described [75]. Data were normalized per mosquito.…”

Section: Methodsmentioning

confidence: 99%

Two insulin-like peptides differentially regulate malaria parasite infection in the mosquito through effects on intermediary metabolism

Pietri

Pakpour

Napoli

et al. 2016

Biochemical Journal

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Insulin-like peptides (ILPs) play important roles in growth and metabolic homeostasis, but have also emerged as key regulators of stress responses and immunity in a variety of vertebrates and invertebrates. Furthermore, a growing literature suggests that insulin signaling-dependent metabolic provisioning can influence host responses to infection and affect infection outcomes. In line with these studies, we previously showed that knockdown of either of two closely related, infection-induced ILPs, ILP3 and ILP4, in the mosquito Anopheles stephensi decreased infection with the human malaria parasite Plasmodium falciparum through kinetically distinct effects on parasite death. However, the precise mechanisms by which ILP3 and ILP4 control the response to infection remained unknown. To address this knowledge gap, we used a complementary approach of direct ILP supplementation into the blood meal to further define ILP-specific effects on mosquito biology and parasite infection. Notably, we observed that feeding resulted in differential effects of ILP3 and ILP4 on blood-feeding behavior and P. falciparum development. These effects depended on ILP-specific regulation of intermediary metabolism in the mosquito midgut, suggesting a major contribution of ILP-dependent metabolic shifts to the regulation of infection resistance and parasite transmission. Accordingly, our data implicate endogenous ILP signaling in balancing intermediary metabolism for the host response to infection, affirming this emerging tenet in host–pathogen interactions with novel insights from a system of significant public health importance.

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Threonine-deficient diets induced changes in hepatic bioenergetics

Abstract: Ross-Inta CM, Zhang Y-F, Almendares A, Giulivi C. Threonine-deficient diets induced changes in hepatic bioenergetics.

Cited by 33 publications

References 53 publications

The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: indication of a post- translational quality control for protein synthesis

The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: indication of a post- translational quality control for protein synthesis

Beneficial Effects of Cod Protein on Inflammatory Cell Accumulation in Rat Skeletal Muscle after Injury Are Driven by Its High Levels of Arginine, Glycine, Taurine and Lysine

Two insulin-like peptides differentially regulate malaria parasite infection in the mosquito through effects on intermediary metabolism

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