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Changes in the activities of protein phosphatase type 1 and type 2A in sea urchin embryos during early development

机译:海胆胚胎早期发育过程中1型和2A型蛋白磷酸酶活性的变化

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摘要

In the eggs and embryos of sea urchins, the activity of protein phosphatase type 2A (PP2A) increased during the developmental period between fertilization and the morula stage, decreased after the prehatching blastula stage and increased again afterhatching. The PP2A activity changed keeping pace with alteration to the activities of cAMP-dependent protein kinase (A kinase), Ca~(2+)/calmodulin-dependent protein kinase (CaM kinase) and casein kinase. Probably, PP2A contributes to the quick turning off of cellular signals because of protein phosphorylation. The activity of protein phosphatase type 1 (PP1) was not detectable up to the morula stage and appreciably increased thereafter. In the isolated nucleus fraction, specific activities of PP1 and PP2A were higher than in whole embryos at all stages in early development. Exponential increase in the number of nuclei because of egg cleavage probably makes PP1 activity detectable in whole embryos after the morula stage. In isolated nuclei, the activities of PP1 and PP2A appreciably decreased after hatching, whereas the activities of A kinase, Ca~(2+)/phospholipid-dependent protein kinase (C kinase) and CaM kinase, as well as casein kinase, became higher. In nuclei, cellular signals caused by proteinphosphorylation after hatching do not seem to be turned off by these protein kinases so quickly as before hatching. The PP1 and PP2A in nuclei also seem to contribute to the elimination of signal noise.
机译:在海胆的卵和胚胎中,2A型蛋白磷酸酶(PP2A)的活性在受精至桑ula期之间的发育期间增加,在孵化前的囊胚期后降低,而在孵化后又增加。 PP2A活性随cAMP依赖性蛋白激酶(A激酶),Ca〜(2 +)/钙调蛋白依赖性蛋白激酶(CaM激酶)和酪蛋白激酶活性变化而变化。 PP2A可能由于蛋白质的磷酸化而有助于细胞信号的快速关闭。直到桑期为止,都无法检测到1型蛋白磷酸酶(PP1)的活性,此后其活性明显增加。在分离的细胞核部分中,PP1和PP2A的比活性在早期发育的所有阶段都高于整个胚胎。由于卵卵裂而使核数呈指数增加,可能使桑ula期后的整个胚胎中可检测到PP1活性。在分离的核中,孵化后PP1和PP2A的活性明显降低,而A激酶,Ca〜(2 +)/磷脂依赖性蛋白激酶(C激酶)和CaM激酶以及酪蛋白激酶的活性更高。在细胞核中,孵化后由蛋白质磷酸化引起的细胞信号似乎并没有像孵化前那样被这些蛋白激酶关闭。原子核中的PP1和PP2A似乎也有助于消除信号噪声。

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