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1.
Cell Death Dis ; 5: e1002, 2014 Jan 16.
Article in English | MEDLINE | ID: mdl-24434510

ABSTRACT

Adaptive responses of skeletal muscle regulate the nuclear shuttling of the sarcomeric protein Ankrd2 that can transduce different stimuli into specific adaptations by interacting with both structural and regulatory proteins. In a genome-wide expression study on Ankrd2-knockout or -overexpressing primary proliferating or differentiating myoblasts, we found an inverse correlation between Ankrd2 levels and the expression of proinflammatory genes and identified Ankrd2 as a potent repressor of inflammatory responses through direct interaction with the NF-κB repressor subunit p50. In particular, we identified Gsk3ß as a novel direct target of the p50/Ankrd2 repressosome dimer and found that the recruitment of p50 by Ankrd2 is dependent on Akt2-mediated phosphorylation of Ankrd2 upon oxidative stress during myogenic differentiation. Surprisingly, the absence of Ankrd2 in slow muscle negatively affected the expression of cytokines and key calcineurin-dependent genes associated with the slow-twitch muscle program. Thus, our findings support a model in which alterations in Ankrd2 protein and phosphorylation levels modulate the balance between physiological and pathological inflammatory responses in muscle.


Subject(s)
Cell Differentiation , Muscle Cells/cytology , Muscle Proteins/immunology , Muscle, Skeletal/cytology , NF-kappa B/immunology , Nuclear Proteins/immunology , Repressor Proteins/immunology , Animals , Glycogen Synthase Kinase 3/genetics , Glycogen Synthase Kinase 3/immunology , Humans , Mice , Mice, Inbred C57BL , Mice, Knockout , Muscle Cells/immunology , Muscle Proteins/genetics , Muscle, Skeletal/immunology , NF-kappa B/genetics , Nuclear Proteins/genetics , Protein Binding , Repressor Proteins/genetics
2.
J Agric Food Chem ; 50(8): 2318-23, 2002 Apr 10.
Article in English | MEDLINE | ID: mdl-11929291

ABSTRACT

Two Gram-negative bacterial strains capable of using lupanine, the predominant quinolizidine alkaloid in Lupinus albus, as a sole carbon source were isolated from soil in which L. albus and L. luteus had been grown [Santana, F. M. et al. J. Ind. Microbiol. 1996, 17, 110-115]. In the present study, we present results suggesting that these isolates are of potential interest for removing lupanine and other quinolizidine alkaloids (QA) from the effluent resulting from the wet processing of Lupinus seeds, at temperatures within the range 20-34 degrees C. Growth in L. albus aqueous extract was diauxic, with a first period of rapid growth leading to the simultaneous consumption of a significant part of the initial concentration of QA (3 g L(-1), being 2 g L(-1) lupanine) and amino acids (1.5 g L(-1)). This period was followed by a second period of slower growth corresponding to the subsequent partial utilization (25%) of the carbohydrates (initial concentration of 20 g L(-1)) together with further removal of QA and amino acids. Despite the differences detected in the susceptibility of the two strains to lupanine toxicity, in particular at supraoptimal temperatures, and in the efficiency of lupanine catabolism, their performance on L. albus extract did not vary significantly.


Subject(s)
Alkaloids/metabolism , Carbon/metabolism , Fabaceae/chemistry , Gram-Negative Bacteria/metabolism , Plant Extracts/chemistry , Quinolizines/metabolism , Sparteine/analogs & derivatives
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