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胚胎期鸡的骨骼肌、心肌和平滑肌表达一种共同的胚胎特异性肌球蛋白轻链。

Embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain.

作者信息

Takano-Ohmuro H, Obinata T, Kawashima M, Masaki T, Tanaka T

出版信息

J Cell Biol. 1985 Jun;100(6):2025-30. doi: 10.1083/jcb.100.6.2025.

DOI:10.1083/jcb.100.6.2025
PMID:3889018
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2113588/
Abstract

It has been demonstrated that embryonic chicken gizzard smooth muscle contains a unique embryonic myosin light chain of 23,000 mol wt, called L23 (Katoh, N., and S. Kubo, 1978, Biochem. Biophys. Acta, 535:401-411; Takano-Ohmuro, H., T. Obinata, T. Mikawa, and T. Masaki, 1983, J. Biochem. (Tokyo), 93:903-908). When we examined myosins in developing chicken ventricular and pectoralis muscles by two-dimensional gel electrophoresis, the myosin light chain (Le) that completely comigrates with L23 was detected in both striated muscles at early developmental stages. Two monoclonal antibodies, MT-53f and MT-185d, were applied to characterize the embryonic light chain Le of striated muscles. Both monoclonal antibodies were raised to fast skeletal muscle myosin light chains; the former antibody is specific to fast muscle myosin light chains 1 and 3, whereas the latter recognizes not only fast muscle myosin light chains but also the embryonic smooth muscle light chain L23. The immunoblots combined with both one- and two-dimensional gel electrophoresis showed that Le reacts with MT-185d but not with MT-53f. These results strongly indicate that Le is identical to L23 and that embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain.

摘要

已经证明,鸡胚砂囊平滑肌含有一种独特的分子量为23,000的胚胎肌球蛋白轻链,称为L23(加藤,N.,和S.久保,1978,生物化学与生物物理学报,535:401 - 411;高野-大室,H.,T.小畑,T.三川,和T.正木,1983,生物化学杂志(东京),93:903 - 908)。当我们通过二维凝胶电泳检测发育中的鸡心室肌和胸肌中的肌球蛋白时,在早期发育阶段的两种横纹肌中都检测到了与L23完全共迁移的肌球蛋白轻链(Le)。应用两种单克隆抗体MT - 53f和MT - 185d来表征横纹肌的胚胎轻链Le。这两种单克隆抗体都是针对快肌骨骼肌肌球蛋白轻链产生的;前一种抗体对快肌肌球蛋白轻链1和3具有特异性,而后一种抗体不仅识别快肌肌球蛋白轻链,还识别胚胎平滑肌轻链L23。结合一维和二维凝胶电泳的免疫印迹表明,Le与MT - 185d反应,但不与MT - 53f反应。这些结果有力地表明,Le与L23相同,并且鸡胚骨骼肌、心肌和平滑肌表达一种共同的胚胎特异性肌球蛋白轻链。

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1
Embryonic chicken skeletal, cardiac, and smooth muscles express a common embryo-specific myosin light chain.胚胎期鸡的骨骼肌、心肌和平滑肌表达一种共同的胚胎特异性肌球蛋白轻链。
J Cell Biol. 1985 Jun;100(6):2025-30. doi: 10.1083/jcb.100.6.2025.
2
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J Biochem. 1987 Nov;102(5):1321-7. doi: 10.1093/oxfordjournals.jbchem.a122170.
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A common myosin light chain is expressed in chicken embryonic skeletal, cardiac, and smooth muscles and in brain continuously from embryo to adult.一种常见的肌球蛋白轻链在鸡胚胎期的骨骼肌、心肌和平滑肌以及大脑中持续表达,从胚胎期直至成年期。
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Nature. 1980 Aug 14;286(5774):731-3. doi: 10.1038/286731a0.

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本文引用的文献

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A MICRO-BIURET METHOD FOR ESTIMATING PROTEINS.一种用于蛋白质定量的微量双缩脲法。
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Myosin from fetal hearts contains the skeletal muscle embryonic light chain.来自胎儿心脏的肌球蛋白含有骨骼肌胚胎轻链。
Nature. 1980 Aug 14;286(5774):731-3. doi: 10.1038/286731a0.
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Types of myosin light chains present during the development of fast skeletal muscle in chick embryo.鸡胚快速骨骼肌发育过程中存在的肌球蛋白轻链类型。
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Myosin light chains and the developmental origin of fast muscle.肌球蛋白轻链与快肌的发育起源
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Synthesis of adult myosin light chains by embryonic muscle cultures.胚胎肌肉培养物合成成人肌球蛋白轻链。
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9
Changes in myosin isozymes during development of chicken gizzard muscle.鸡砂囊肌肉发育过程中肌球蛋白同工酶的变化。
J Biochem. 1983 Mar;93(3):903-8. doi: 10.1093/jb/93.3.903.
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Changes in myosin isozymes during development of chicken breast muscle.鸡胸肌发育过程中肌球蛋白同工酶的变化。
J Biochem. 1982 Apr;91(4):1305-11. doi: 10.1093/oxfordjournals.jbchem.a133816.