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| Domitrovic,Tatiana; Fausto,Anna K.; Silva,Tatiane da F.; Romanel,Elisson; Vaslin,Maite F. S.. |
| Abstract Regulation of protein stability and/or degradation of misfolded and damaged proteins are essential cellular processes. A part of this regulation is mediated by the so-called N-end rule proteolytic pathway, which, in concert with the ubiquitin proteasome system (UPS), drives protein degradation depending on the N-terminal amino acid sequence. One important enzyme involved in this process is arginyl-t-RNA transferase, known as ATE. This enzyme acts post-translationally by introducing an arginine residue at the N-terminus of specific protein targets to signal degradation via the UPS. However, the function of ATEs has only recently begun to be revealed. Nonetheless, the few studies to date investigating ATE activity in plants points to the great... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: ATE; N-end rule; Plant; Argyniltransferase; Protein degradation. |
| Ano: 2017 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572017000200253 |
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| Barchiesi-Ferrari,Claudia; Anrique,René. |
| The flow of ruminal undegradable protein (RUP) to the small intestine can be increased if ruminal degradation of dietary protein is reduced. The objective of this study was to evaluate the effect of extrusion on ruminal degradability of dry matter (DM) and crude protein (CP) from dehulled lupin (Lupinus albus L.) (DL) and rapeseed (Brassica napus L.) meal (RM). Unextruded soybean (Glicine max L.) meal (SBM) was used as a control. The DL was extruded at 130 ºC with 20% moisture and RM was extruded at 120 ºC with 20% moisture. Ruminal degradability was evaluated in situ by incubating feed samples for 2, 4, 8, 12, 24, and 48 h of fermentation in the rumen using three rumen-fistulated dairy cows. Values of CP soluble fraction (a) in SBM, DL, extruded... |
| Tipo: Journal article |
Palavras-chave: Extrusion; Protein supplements; Protein degradation; Soybean meal; Cattle. |
| Ano: 2011 |
URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0718-58392011000300014 |
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| Marzuca-Nassr,G.N.; Fortes,M.A.S.; Guimarães-Ferreira,L.; Murata,G.M.; Vitzel,K.F.; Vasconcelos,D.A.A.; Bassit,R.A.; Curi,R.. |
| The effect of a short-term creatine supplementation on hindlimb suspension (HS)-induced muscle atrophy was investigated. Creatine monohydrate (5 g/kg b.w. per day) or placebo, divided in 2 daily doses, was given by oral gavage for 5 days. Rats were maintained in HS with dietary supplementation concomitantly for 5 days. Body weight, soleus and EDL muscle masses, and cross-sectional areas (CSA) of the muscle fibers were measured. Signaling pathways associated with skeletal muscle mass regulation (FST, MSTN, FAK, IGF-1, MGF, Akt, mTOR, atrogin-1, and MuRF1 expressions, and Akt, S6, GSK3B, and 4EBP1 proteins) were evaluated in the muscles. Soleus muscle exhibited more atrophy than the EDL muscle due to HS. Creatine supplementation attenuated the decrease of... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Creatine supplementation; Hindlimb suspension; Muscle disuse atrophy; Protein synthesis; Protein degradation. |
| Ano: 2019 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2019001000606 |
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