Matveev V V
Biokhimiia. 1987 Aug;52(8):1274-8.
Mouse low-differentiated rhabdomyosarcoma (LD RMS) A7 contains 4.5 mg/cm3 of skeletal muscle type myosin and 9.7 mg/cm3 of actin. When recalculated to a volume of cytoplasm of A7 cells, the myosin concentration increases to 12.5 mg/cm3, while that of actin increases to 27.1 mg/cm3. In skeletal muscles the tissue concentrations of myosin and actin is close to the cytoplasmic concentrations. In mouse femoral muscles the tissue and cytoplasmic concentrations of myosin (approximately 102 mg/cm3) and actin (approximately 67 mg/cm3) are 8 (for myosin) and 2.5 times (for actin) higher than the cytoplasmic concentrations of these proteins in tumour cells. The molar ratio of myosin to actin concentrations is 1:26 in the tumour and 1:8 in the muscles. Possible causes of the absence of skeletal muscle type myofibrils and the manifestations of coordination and discoordination of gene expression in LD RMS cells are discussed.
小鼠低分化横纹肌肉瘤(LD RMS)A7含有4.5毫克/立方厘米的骨骼肌型肌球蛋白和9.7毫克/立方厘米的肌动蛋白。当重新计算到A7细胞的细胞质体积时,肌球蛋白浓度增加到12.5毫克/立方厘米,而肌动蛋白浓度增加到27.1毫克/立方厘米。在骨骼肌中,肌球蛋白和肌动蛋白的组织浓度接近细胞质浓度。在小鼠股四头肌中,肌球蛋白(约102毫克/立方厘米)和肌动蛋白(约67毫克/立方厘米)的组织和细胞质浓度分别是肿瘤细胞中这些蛋白质细胞质浓度的8倍(肌球蛋白)和2.5倍(肌动蛋白)。肿瘤中肌球蛋白与肌动蛋白浓度的摩尔比为1:26,而在肌肉中为1:8。本文讨论了LD RMS细胞中缺乏骨骼肌型肌原纤维的可能原因以及基因表达的协调和失调表现。