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The beta-thymosins: intracellular and extracellular activities of a versatile actin binding protein family.

机译:β-胸腺:多功能肌动蛋白结合蛋白家族的细胞内和细胞外活动。

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The beta-thymosins are N-terminally acetylated peptides of about 5 kDa molecular mass and composed of about 40-44 amino acid residues. The first member of the family, thymosin beta4, was initially isolated from thymosin fraction 5, prepared in five steps from calf thymus. Thymosin beta4 was supposed to be specifically produced and released by the thymic gland and to possess hormonal activities modulating the immune response. Various paracrine effects have indeed been reported for these peptides such as cardiac protection, angiogenesis, stimulation of wound healing, and hair growth. Besides these paracrine effects, it was noted that beta-thymosins occur in high concentration in the cytoplasm of many eukaryotic cells and bind to the cytoskeletal component actin. Subsequently it became apparent from in vitro experiments that they preferentially bind to monomeric (G-)actin and stabilize it in its monomeric form. Due to this ability the beta-thymosins are the main intracellular actin sequestering factor, i.e., they posses the ability to remove monomeric actin from the dynamic assembly and disassembly processes of the actin cytoskeleton that constantly occur in activated cells. In this review we will concentrate on the intracellular activity and localization of the beta-thymosins, i.e., their modulating effect on the actin cytoskeleton.
机译:β-胸腺嘧啶是约5kDa分子量的N-末端乙酰化肽,并由约40-44个氨基酸残基组成。本族的第一成员胸腺蛋白β4最初与胸腺素馏分5分离,从小牛胸腺中制备五个步骤。胸腺蛋白β4应该由胸腺腺特异性生产和释放,并具有调节免疫应答的激素活性。对于这些肽,例如心脏保护,血管生成,伤口愈合刺激和毛发生长,据报道了各种旁静脉效应。除了这些旁静脉作用外,还注意到β-胸苷在许多真核细胞的细胞质中出现高浓度,并与细胞骨骼分子肌动蛋白结合。随后,从体外实验中显而易见的是,它们优先与单体(G-)致动蛋白结合并以其单体形式稳定抗体。由于这种能力,β-胸苷是主要的细胞内肌动蛋白螯合因子,即,它们可以从动态组件中除去单体肌动蛋白,并拆解在活化细胞中不断发生的肌动蛋白细胞骨架的拆卸过程。在该综述中,我们将专注于β-胸腺素的细胞内活性和定位,即它们对肌动蛋白细胞骨架的调节作用。

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