FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2514992716> ?p ?o ?g. }

• W2514992716 endingPage "e2317" @default.
• W2514992716 startingPage "e2317" @default.
• W2514992716 abstract "Background. Mammalian hibernation in thirteen-lined ground squirrels ( Ictidomys tridecemlineatus ) is characterized by dramatic changes on a physiological and molecular level. During hibernation, mammalian hearts show a propensity to hypertrophy due to the need for increasing contractility to pump colder and more viscous blood. While cardiac hypertrophy is quite often a process characterized by decompensation, the ground squirrel studied is an excellent model of cardiac plasticity and cardioprotection under conditions of hypothermia and ischemia. The forkhead box O (Foxo) family of proteins and myogenin (MyoG) are transcription factors that control protein degradation and muscle atrophy by regulating the expression of the E3 ubiquitin ligases, MAFbx and MuRF1. These ligases are part of the ubiquitin proteasome system by transferring ubiquitin to proteins and targeting these proteins for degradation. Regulation of Foxo1 and 3a occurs through phosphorylation at different residues. The threonine-24 (Thr-24) and serine-319 (Ser-319) residues on Foxo1, and the Thr-32 residue on Foxo3a are phosphorylated by Akt, leading to cytoplasmic localization of Foxo. We propose that the described mechanism contributes to the changes taking place in cardiac muscle throughout hibernation. Methods. Total and phosphorylated protein levels of Foxo1 and Foxo3a, as well as total protein levels of MyoG, MAFbx, and MuRF1, were studied using immunoblotting. Results. Immunoblotting results demonstrated upregulations in Foxo1 and Foxo3a total protein levels (1.3- and 4.5-fold increases relative to euthermic control, for Foxo1 and 3a respectively) during late torpor, and protein levels remained elevated throughout the rest of torpor and at interbout arousal. We also observed decreases in inactive, phosphorylated Foxo1 and 3a proteins during throughout torpor, where levels of p-Foxo1 Ser 319 and Thr 24 , as well as p-Foxo3a Thr 32 decreased by at least 45% throughout torpor. MyoG was upregulated only during late torpor by 2.4-fold. Protein levels of MAFbx and MuRF1 increased in late torpor as well as during early arousal by as much as 2.8-fold, and MAFbx levels remained elevated during interbout arousal, whereas MuRF1 levels returned to control levels. Discussion. The present results indicate that upregulation and activation of Foxo1 and 3a, in addition to the increase in MyoG levels at late torpor, may be upregulating the expression of MAFbx and MuRF1. These findings suggest that there is activation of the ubiquitin proteasome system (UPS) as ground squirrels arouse from torpor. Therefore, the signalling pathway involving MyoG, and the E3 ligases MAFbx and MuRF1, plays a significant role in cardiac muscle remodelling during hibernation. These findings provide insights into the regulation of protein degradation and turnover in the cardiac muscle of a hibernator model." @default.
• W2514992716 created "2016-09-16" @default.
• W2514992716 creator A5000605316 @default.
• W2514992716 creator A5078699661 @default.
• W2514992716 date "2016-08-11" @default.
• W2514992716 modified "2023-10-12" @default.
• W2514992716 title "Transcriptional activation of muscle atrophy promotes cardiac muscle remodeling during mammalian hibernation" @default.
• W2514992716 cites W1506256990 @default.
• W2514992716 cites W1870982485 @default.
• W2514992716 cites W1969528211 @default.
• W2514992716 cites W1971857747 @default.
• W2514992716 cites W1972239225 @default.
• W2514992716 cites W1982977354 @default.
• W2514992716 cites W1987501637 @default.
• W2514992716 cites W1991634033 @default.
• W2514992716 cites W1993722975 @default.
• W2514992716 cites W2000873756 @default.
• W2514992716 cites W2002060477 @default.
• W2514992716 cites W2005510844 @default.
• W2514992716 cites W2006796385 @default.
• W2514992716 cites W2008020112 @default.
• W2514992716 cites W2014942570 @default.
• W2514992716 cites W2014964156 @default.
• W2514992716 cites W2017856783 @default.
• W2514992716 cites W2024921031 @default.
• W2514992716 cites W2029013337 @default.
• W2514992716 cites W2032035791 @default.
• W2514992716 cites W2032189098 @default.
• W2514992716 cites W2033797333 @default.
• W2514992716 cites W2036837630 @default.
• W2514992716 cites W2038005840 @default.
• W2514992716 cites W2038699613 @default.
• W2514992716 cites W2041043528 @default.
• W2514992716 cites W2055082208 @default.
• W2514992716 cites W2056677650 @default.
• W2514992716 cites W2059635626 @default.
• W2514992716 cites W2062163499 @default.
• W2514992716 cites W2065025470 @default.
• W2514992716 cites W2065056367 @default.
• W2514992716 cites W2070345867 @default.
• W2514992716 cites W2082852887 @default.
• W2514992716 cites W2089856287 @default.
• W2514992716 cites W2096980800 @default.
• W2514992716 cites W2102038264 @default.
• W2514992716 cites W2107664641 @default.
• W2514992716 cites W2109686686 @default.
• W2514992716 cites W2121016855 @default.
• W2514992716 cites W2121181558 @default.
• W2514992716 cites W2123509574 @default.
• W2514992716 cites W2123922689 @default.
• W2514992716 cites W2128676235 @default.
• W2514992716 cites W2129328548 @default.
• W2514992716 cites W2129439677 @default.
• W2514992716 cites W2137035181 @default.
• W2514992716 cites W2138639799 @default.
• W2514992716 cites W2143587276 @default.
• W2514992716 cites W2150318663 @default.
• W2514992716 cites W2155581711 @default.
• W2514992716 cites W2162063376 @default.
• W2514992716 cites W2162857699 @default.
• W2514992716 cites W2165718181 @default.
• W2514992716 cites W2167033587 @default.
• W2514992716 cites W2167763573 @default.
• W2514992716 cites W2223675028 @default.
• W2514992716 cites W2258710488 @default.
• W2514992716 cites W2283844314 @default.
• W2514992716 cites W2289914077 @default.
• W2514992716 cites W2299105000 @default.
• W2514992716 cites W2465487218 @default.
• W2514992716 cites W4231442978 @default.
• W2514992716 cites W4232767515 @default.
• W2514992716 doi "https://doi.org/10.7717/peerj.2317" @default.
• W2514992716 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4991874" @default.
• W2514992716 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/27602284" @default.
• W2514992716 hasPublicationYear "2016" @default.
• W2514992716 type Work @default.
• W2514992716 sameAs 2514992716 @default.
• W2514992716 citedByCount "22" @default.
• W2514992716 countsByYear W25149927162016 @default.
• W2514992716 countsByYear W25149927162017 @default.
• W2514992716 countsByYear W25149927162018 @default.
• W2514992716 countsByYear W25149927162019 @default.
• W2514992716 countsByYear W25149927162020 @default.
• W2514992716 countsByYear W25149927162021 @default.
• W2514992716 countsByYear W25149927162022 @default.
• W2514992716 countsByYear W25149927162023 @default.
• W2514992716 crossrefType "journal-article" @default.
• W2514992716 hasAuthorship W2514992716A5000605316 @default.
• W2514992716 hasAuthorship W2514992716A5078699661 @default.
• W2514992716 hasBestOaLocation W25149927161 @default.
• W2514992716 hasConcept C100564792 @default.
• W2514992716 hasConcept C104317684 @default.
• W2514992716 hasConcept C11413529 @default.
• W2514992716 hasConcept C11960822 @default.
• W2514992716 hasConcept C119865680 @default.
• W2514992716 hasConcept C126322002 @default.
• W2514992716 hasConcept C134018914 @default.
• W2514992716 hasConcept C134459356 @default.

• next