精胺对蛋白激酶C与磷脂囊泡结合的影响。
Effect of spermine on association of protein kinase C with phospholipid vesicles.
作者信息
Moruzzi M S, Monti M G, Piccinini G, Marverti G, Tadolini B
机构信息
Istituto di Chimica Biologica, Università di Modena, Italy.
出版信息
Life Sci. 1990;47(16):1475-82. doi: 10.1016/0024-3205(90)90527-x.
The in vitro mechanism by which polyamines affect protein kinase C (PK C) activation process was investigated in a reconstituted system consisting of purified enzyme and phospholipid vesicles of various phosphatidylserine content. It was found that the addition of spermine greatly interferes with the association of PK C to liposomes. This tetramine, at micromolar concentrations, was most potently effective while other polyamines such as spermidine and putrescine were almost ineffective; therefore the modulatory action appeared to be structure specific. The spermine effect is dramatically influenced by the density of the phosphatidylserine present on the liposome, suggesting the complex formation with the acidic component on phospholipid vesicles to be the mechanism by which this polyamine exerts its modulatory action.
在一个由纯化的酶和不同磷脂酰丝氨酸含量的磷脂囊泡组成的重组系统中，研究了多胺影响蛋白激酶C（PKC）激活过程的体外机制。发现添加精胺会极大地干扰PKC与脂质体的结合。这种四胺在微摩尔浓度时最为有效，而其他多胺如亚精胺和腐胺几乎无效；因此，调节作用似乎具有结构特异性。精胺的作用受到脂质体上磷脂酰丝氨酸密度的显著影响，这表明与磷脂囊泡上的酸性成分形成复合物是这种多胺发挥调节作用的机制。
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