胰岛素可改变外周环磷酸腺苷磷酸二酯酶的靶标大小，但不改变肝细胞膜中完整的环鸟苷酸刺激的环磷酸腺苷磷酸二酯酶的靶标大小。
Insulin alters the target size of the peripheral cyclic AMP phosphodiesterase but not the integral cyclic GMP-stimulated cyclic AMP phosphodiesterase in liver plasma membranes.
作者信息
Wallace A V, Martin B R, Houslay M D
机构信息
Institute of Biochemistry, University of Glasgow.
出版信息
Biochem Biophys Res Commun. 1990 Jun 15;169(2):377-82. doi: 10.1016/0006-291x(90)90342-k.
Radiation inactivation of the two high affinity cyclic AMP phosphodiesterases (PDE) found in liver plasma membranes afforded an estimation of their molecular target sizes in situ. The activity of the peripheral plasma membrane PDE decayed as a single exponential with a target size corresponding to a monomer of circa 54 kDa. The integral, cyclic GMP-stimulated PDE decayed as a dimer of circa 125 kDa. Preincubation of plasma membranes with insulin (10nM), prior to irradiation, caused the target size of only the peripheral plasma membrane PDE to increase. We suggest that insulin addition causes the peripheral plasma membrane PDE to alter its coupling to an integral plasma membrane protein with a target size of circa 90 kDa.
对肝细胞膜中发现的两种高亲和力环磷酸腺苷磷酸二酯酶（PDE）进行辐射失活，从而对其原位分子靶标大小进行了估计。外周质膜PDE的活性呈单指数衰减，其靶标大小对应于约54 kDa的单体。完整的、受环鸟苷酸刺激的PDE以约125 kDa的二聚体形式衰减。在辐照前用胰岛素（10 nM）预孵育质膜，仅导致外周质膜PDE的靶标大小增加。我们认为，添加胰岛素会使外周质膜PDE改变其与靶标大小约为90 kDa的完整质膜蛋白的偶联。
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