Biochemical and functional evidences for a GLUT-4 homologous protein in avian skeletal muscle.

V Thomas-Delloye, F Marmonier, C Duchamp, B Pichon-Georges, J Lachuer, H Barré, G Crouzoulon
{"title":"Biochemical and functional evidences for a GLUT-4 homologous protein in avian skeletal muscle.","authors":"V Thomas-Delloye,&nbsp;F Marmonier,&nbsp;C Duchamp,&nbsp;B Pichon-Georges,&nbsp;J Lachuer,&nbsp;H Barré,&nbsp;G Crouzoulon","doi":"10.1152/ajpregu.1999.277.6.R1733","DOIUrl":null,"url":null,"abstract":"<p><p>The characteristics and modulation of glucose transport were investigated in skeletal muscles of 5-wk-old Muscovy ducklings (Cairina moschata). Glucose uptake by sarcolemmal vesicles isolated from gastrocnemius muscle followed typical Michaelis-Menten kinetics with a K(m) value (17 mM) similar to that described in equivalent mammalian preparations. Western blot analysis of duckling sarcolemma using antibodies directed against rat GLUT-4 transporter revealed an immunoreactive protein of similar molecular mass (45 kDa) to that present in rats. When ducklings were killed in the postabsorptive state, GLUT-4 homologous protein was located predominantly (80%) in intracellular membranes. Insulin stimulation of a perfused leg muscle preparation in vitro led to the translocation of GLUT-4 homologous proteins from intracellular pools to the sarcolemma, with a subsequent increase in glucose uptake by sarcolemmal vesicles and perfused muscles. Glucose transport was positively controlled by the metabolic needs of skeletal muscle as reflected by the increased glucose uptake of sarcolemmal vesicles isolated from cold-acclimated ducklings. Present results, therefore, demonstrate, for the first time in an avian species, the existence in skeletal muscle of a glucose transporter showing molecular and functional homologies with the mammalian GLUT-4 transporter.</p>","PeriodicalId":7590,"journal":{"name":"American Journal of Physiology","volume":"277 6","pages":"R1733-40"},"PeriodicalIF":0.0000,"publicationDate":"1999-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1152/ajpregu.1999.277.6.R1733","citationCount":"28","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"American Journal of Physiology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1152/ajpregu.1999.277.6.R1733","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 28

Abstract

The characteristics and modulation of glucose transport were investigated in skeletal muscles of 5-wk-old Muscovy ducklings (Cairina moschata). Glucose uptake by sarcolemmal vesicles isolated from gastrocnemius muscle followed typical Michaelis-Menten kinetics with a K(m) value (17 mM) similar to that described in equivalent mammalian preparations. Western blot analysis of duckling sarcolemma using antibodies directed against rat GLUT-4 transporter revealed an immunoreactive protein of similar molecular mass (45 kDa) to that present in rats. When ducklings were killed in the postabsorptive state, GLUT-4 homologous protein was located predominantly (80%) in intracellular membranes. Insulin stimulation of a perfused leg muscle preparation in vitro led to the translocation of GLUT-4 homologous proteins from intracellular pools to the sarcolemma, with a subsequent increase in glucose uptake by sarcolemmal vesicles and perfused muscles. Glucose transport was positively controlled by the metabolic needs of skeletal muscle as reflected by the increased glucose uptake of sarcolemmal vesicles isolated from cold-acclimated ducklings. Present results, therefore, demonstrate, for the first time in an avian species, the existence in skeletal muscle of a glucose transporter showing molecular and functional homologies with the mammalian GLUT-4 transporter.

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
禽骨骼肌中glut4同源蛋白的生物化学和功能证据。
研究了5周龄麝香鸭骨骼肌中葡萄糖转运的特性和调控。从腓肠肌分离的肌上皮囊泡摄取葡萄糖遵循典型的Michaelis-Menten动力学,其K(m)值(17 mM)与等效哺乳动物制剂中描述的相似。利用针对大鼠GLUT-4转运蛋白的抗体对鸭肌膜进行Western blot分析,发现一种分子质量与大鼠相似(45 kDa)的免疫反应蛋白。当雏鸭在吸收后状态下被杀死时,GLUT-4同源蛋白主要位于细胞膜内(80%)。体外灌注腿肌制剂的胰岛素刺激导致GLUT-4同源蛋白从细胞内池转移到肌膜,随后肌膜囊泡和灌注肌肉的葡萄糖摄取增加。葡萄糖运输受到骨骼肌代谢需求的积极控制,这反映在从冷适应鸭中分离的肌上皮囊泡增加的葡萄糖摄取上。因此,本研究结果首次在鸟类中证实骨骼肌中存在与哺乳动物GLUT-4转运蛋白具有分子和功能同源性的葡萄糖转运蛋白。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
自引率
0.00%
发文量
1
期刊最新文献
Case Report: Intraoperative Fascial Traction in Robotic Abdominal Wall Surgery; An Early Experience. Microvessel occlusions alter amyloid-beta plaque morphology in a mouse model of Alzheimer's disease. De virtuele diabeteskliniek in een stroomversnelling? An interventional image-guided microdevice implantation and retrieval method for in-vivo drug response assessment. Methods for Congenital Thumb Hypoplasia Reconstruction. A Review of the Outcomes for Ten Years of Surgical Treatment.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1