COMPLETE AMINO-ACID SEQUENCE OF ACTINS FROM BOVINE AORTA, BOVINE HEART, BOVINE FAST SKELETAL-MUSCLE, AND RABBIT SLOW SKELETAL-MUSCLE - PROTEIN-CHEMICAL ANALYSIS OF MUSCLE ACTIN DIFFERENTIATION
COMPLETE AMINO-ACID SEQUENCE OF ACTINS FROM BOVINE AORTA, BOVINE HEART, BOVINE FAST SKELETAL-MUSCLE, AND RABBIT SLOW SKELETAL-MUSCLE - PROTEIN-CHEMICAL ANALYSIS OF MUSCLE ACTIN DIFFERENTIATION
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DOI：
10.1111/j.1432-0436.1979.tb01021.x
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发表时间：
1979-01-01
期刊：
影响因子：
2.9
通讯作者：
WEBER, K
中科院分区：
文献类型：
--
作者：
VANDEKERCKHOVE, J;WEBER, K
报道了4种哺乳动物肌肉肌动蛋白的完整氨基酸序列：牛骨骼肌肌动蛋白、牛心脏肌动蛋白、牛主动脉肌动蛋白和兔慢肌肌动蛋白。因此，在具有完整氨基酸序列的高等哺乳动物中，不同肌动蛋白的数量从2个增加到5个。对不同的平滑肌组织的筛选显示，除了主动脉类型肌动蛋白外，还有第二个平滑肌肌动蛋白，它看起来与鸡肌动蛋白非常相似，如果不是完全相同的话。由于鸡肌动蛋白的序列已知，目前在高等哺乳动物中有6种不同的肌动蛋白。牛主动脉肌动蛋白和鸡胆肌动蛋白这两种肌动蛋白只有3个氨基酸替换，均位于氨基末端。在其余的序列中，这两个平滑肌肌动蛋白都有相同的4个氨基酸替换，这是它们与骨骼肌肌动蛋白的区别。心肌肌动蛋白与骨骼肌肌动蛋白只有4个氨基酸交换。比较兔快肌和慢肌肌动蛋白时，没有发现氨基酸替代。讨论了6种不同哺乳动物肌动蛋白的氨基酸替代模式及其组织特异性。与非肌肉肌动蛋白相比，这4种肌动蛋白之间存在着非常密切的关系。骨骼肌肌动蛋白是分化程度最高的肌动蛋白形式，而平滑肌肌动蛋白与非肌肉肌动蛋白的关系更为密切。根据这些标准，心肌肌动蛋白介于骨骼肌肌动蛋白和平滑肌肌动蛋白之间。
Complete amino acid sequences for 4 mammalian muscle actins are reported: bovine skeletal muscle actin, bovine cardiac actin, the major component of bovine aorta actin and rabbit slow skeletal muscle actin. The number of different actins in a higher mammal for which full amino sequences are now available is therefore increased from 2 to 5. Screening of different smooth muscle tissues revealed in addition to the aorta type actin a 2nd smooth muscle actin, which appears very similar if not identical to chicken gizzard actin. Since the sequence of chicken gizzard actin is known, 6 different actins are presently characterized in a higher mammal. The 2 smooth muscle actins, bovine aorta actin and chicken gizzard actin, differ by only 3 amino acid substitutions, all located in the amino-terminal end. In the rest of their sequences both smooth muscle actins share the same 4 amino acid substitutions, which distinguish them from skeletal muscle actin. Cardiac muscle actin differs from skeletal muscle actin by only 4 amino acid exchanges. No amino acid substitutions were found when actins from rabbit fast and slow skeletal muscle were compared. The amino acid substitution patterns of the 6 different mammalian actins and their tissue specificity are discussed. A very close relationship exists between the 4 muscle actins in comparison to the nonmuscle actins. Skeletal muscle actin is the highest differentiated actin form, whereas smooth muscle actins show a noticeably closer relation to nonmuscle actins. By these criteria cardiac muscle actin lies between skeletal muscle actin and smooth muscle actins.