INSULIN RECEPTORS IN LIVER - SPECIFIC BINDING OF [I-125]INSULIN TO PLASMA MEMBRANE AND ITS RELATION TO INSULIN BIOACTIVITY
INSULIN RECEPTORS IN LIVER - SPECIFIC BINDING OF [I-125]INSULIN TO PLASMA MEMBRANE AND ITS RELATION TO INSULIN BIOACTIVITY
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DOI：
10.1073/pnas.68.8.1833
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发表时间：
1971-01-01
影响因子：
11.1
通讯作者：
NEVILLE, DM
中科院分区：
文献类型：
--
作者：
FREYCHET, P;ROTH, J;NEVILLE, DM
[125I]胰岛素在7 × 10-10M下，25%的放射性结合到大鼠肝脏纯化的质膜上。未标记的胰岛素在10-9M （6 ng/ml）时抑制20%的[125I]胰岛素结合，相当于肝门静脉血中的胰岛素浓度；10-7M和10-5M对[125I]胰岛素结合的抑制分别为80%和90%。8种具有100倍以上生物效力的胰岛素及其衍生物抑制[125I]胰岛素与肝膜结合的能力与它们刺激分离脂肪细胞中葡萄糖氧化的能力成正比。无活性胰岛素链、胰高血糖素、促肾上腺皮质激素和人生长激素均无影响。从粗浆液中纯化质膜后，[125I]胰岛素的结合增加了55倍。结合是时间和温度依赖的，添加过量的胰岛素会产生[125I]胰岛素的快速解离。这项研究直接证明了胰岛素与其生物学上重要的受体的结合。
With [125I]insulin at 7 × 10-10M, 25% of the radioactivity was bound to plasma membranes purified from rat liver. 20% of the [125I]insulin binding was inhibited by unlabeled insulin at 10-9M (6 ng/ml), equivalent to insulin concentrations in hepatic portal blood; inhibition of [125I]insulin binding was 80% at 10-7M and 90% at 10-5M. Eight insulins and derivatives with biological potencies that differed over a 100-fold range inhibited the binding of [125I]insulin to liver membranes in direct proportion to their ability to stimulate glucose oxidation in isolated fat cells. Inactive insulin chains, as well as glucagon, ACTH, and human growth harmone were without effect. The binding of [125I]insulin increased 55-fold as plasma membrane was purified from crude homogenate. Binding was time- and temperature-dependent, and addition of excess insulin produced rapid dissociation of [125I]insulin. This study demonstrates directly the binding of insulin to its biologically important receptors.