Famulski K S, Pilarska M, Wrzosek A, Sarzała M G
Department of Cellular Biochemistry, Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw.
Eur J Biochem. 1988 Jan 15;171(1-2):364-8. doi: 10.1111/j.1432-1033.1988.tb13799.x.
Enzymatic properties and the protein pattern of sarcolemma fractions isolated from three groups of rabbits: euthyroid, hyperthyroid and hypothyroid, were studied. The amount of phosphorylated intermediate formed by the calmodulin-dependent (Ca2+-Mg2+)ATPase and the activity of this enzyme as well as that of (Na+-K+)ATPase were the highest in membranes isolated at the hyperthyroid state. On the other hand, sarcolemma obtained from the hypothyroid animals exhibited a decreased activity of (Na+-K+)ATPase, while the activity of calmodulin-dependent (Ca2+-Mg2+)ATPase was the same as in the preparations obtained from euthyroid animals. Thyroid hormones also changed the protein pattern of muscle sarcolemma. Membranes isolated from hyperthyroid animals lacked peptides of apparent molecular masses of 41 kDa and 53 kDa, while a peptide of the apparent molecular mass of 63 kDa was enriched in the preparation from hypothyroid animals. Thyroid hormones affected endogenous cAMP-dependent protein phosphorylation. The sarcolemma fraction obtained from hyperthyroid animals exhibited a decreased phosphorylation of peptides of apparent molecular masses of 30 kDa and 47 kDa, while the cAMP-independent phosphorylation of several other peptides was augmented. Moreover, sarcolemma preparations isolated from hyperthyroid animals showed higher activity of cAMP-independent protein kinase(s) and lower activity of cAMP-dependent protein kinase when compared to the euthyroid preparations. It is proposed that thyroxine increases the content of calmodulin-dependent (Ca2+-Mg2+)ATPase protein and affects the activity of cAMP-independent and cAMP-dependent protein kinases bound to sarcolemma.
研究了从三组兔子（甲状腺功能正常、甲状腺功能亢进和甲状腺功能减退）分离的肌膜组分的酶学特性和蛋白质模式。由钙调蛋白依赖性（Ca2 + -Mg2 +）ATP酶形成的磷酸化中间体的量以及该酶和（Na + -K +）ATP酶的活性在甲状腺功能亢进状态下分离的膜中最高。另一方面，从甲状腺功能减退动物获得的肌膜显示（Na + -K +）ATP酶活性降低，而钙调蛋白依赖性（Ca2 + -Mg2 +）ATP酶的活性与从甲状腺功能正常动物获得的制剂中的活性相同。甲状腺激素也改变了肌肉肌膜的蛋白质模式。从甲状腺功能亢进动物分离的膜缺乏表观分子量为41 kDa和53 kDa的肽，而表观分子量为63 kDa的肽在甲状腺功能减退动物的制剂中富集。甲状腺激素影响内源性cAMP依赖性蛋白磷酸化。从甲状腺功能亢进动物获得的肌膜组分显示表观分子量为30 kDa和47 kDa的肽的磷酸化降低，而其他几种肽的非cAMP依赖性磷酸化增加。此外，与甲状腺功能正常的制剂相比，从甲状腺功能亢进动物分离的肌膜制剂显示非cAMP依赖性蛋白激酶的活性更高，而cAMP依赖性蛋白激酶的活性更低。有人提出，甲状腺素增加了钙调蛋白依赖性（Ca2 + -Mg2 +）ATP酶蛋白的含量，并影响与肌膜结合的非cAMP依赖性和cAMP依赖性蛋白激酶的活性。
