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溶血磷脂酰胆碱可以调节来自大鼠肝细胞膜的胰高血糖素刺激的腺苷酸环化酶的活性。

Lysophosphatidylcholines can modulate the activity of the glucagon-stimulated adenylate cyclase from rat liver plasma membranes.

作者信息

Houslay M D, Palmer R W

出版信息

Biochem J. 1979 Jan 15;178(1):217-21. doi: 10.1042/bj1780217.

Abstract
  1. Synthetic lysophosphatidylcholines inhibit the glucagon-stimulated adenylate cyclase activity of rat liver plasma membranes at concentrations two to five times lower than those needed to inhibit the fluoride-stimulated activity. 2. Specific 125I-labelled glucagon binding to hormone receptors is inhibited at concentrations similar to those inhibiting the fluoride-stimulated activity. 3. At concentrations of lysophosphatidylcholines immediately below those causing inhibition, an activation of adenylate cyclase activity or hormone binding was observed. 4 These effects are essentially reversible. 5. We conclude that the increased sensitivity of glucagon-stimulated adenylate cyclase to inhibition may be due to the lysophosphatidylcholines interfering with the physical coupling between the hormone receptor and catalytic unit of adenylate cyclase. 6. We suggest that, in vivo, it is possible that lysophosphatidylcholines may modulate the activity of adenylate cyclase only when it is in the hormone-stimulated state.
摘要
  1. 合成溶血磷脂酰胆碱抑制大鼠肝细胞膜中胰高血糖素刺激的腺苷酸环化酶活性时所需的浓度,比抑制氟化物刺激的活性所需浓度低两到五倍。2. 特异性125I标记的胰高血糖素与激素受体的结合在与抑制氟化物刺激活性相似的浓度下受到抑制。3. 在溶血磷脂酰胆碱浓度略低于引起抑制的浓度时,观察到腺苷酸环化酶活性或激素结合的激活。4. 这些效应基本上是可逆的。5. 我们得出结论,胰高血糖素刺激的腺苷酸环化酶对抑制的敏感性增加可能是由于溶血磷脂酰胆碱干扰了激素受体与腺苷酸环化酶催化单位之间的物理偶联。6. 我们认为,在体内,溶血磷脂酰胆碱可能仅在处于激素刺激状态时才调节腺苷酸环化酶的活性。

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