Characteristics of the human lymphocyte insulin receptor.
Characteristics of the human lymphocyte insulin receptor.
复制标题
人淋巴细胞胰岛素受体的特征。
DOI：
10.1016/s0021-9258(19)44205-1
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发表时间：
1973
期刊：
影响因子：
--
通讯作者：
D. Buell
中科院分区：
文献类型：
--
作者：
J. Gavin;P. Gorden;J. Roth;J. A. Archer;D. Buell
用125i -胰岛素研究了胰岛素与人淋巴细胞的相互作用。循环淋巴细胞中的受体与培养细胞中的受体难以区分，淋巴细胞受体与脂肪细胞和肝脏制剂中的受体结构惊人地相似。在淋巴细胞中，胰岛素或胰岛素类似物抑制125i -胰岛素结合的能力与该制剂抑制标记激素与纯化肝膜结合或刺激脂肪细胞中葡萄糖氧化的能力成正比。125i -胰岛素与淋巴细胞的结合是一个快速且可逆的过程。在15°时结合最大。解离率曲线为双相曲线，常数为8.3x10-5s-1和8.3x10-4s-1。两级结合位点在培养淋巴细胞中的表观亲和力常数分别为1.2x1010m-1和1.1 x1010m-1，而在正常循环淋巴细胞中的表观亲和力常数分别为2.0 x1010m-1和1.4x108m-1。在30°时，淋巴细胞对标记胰岛素的降解很少，在15°时，培养或循环细胞没有可检测到的降解。125i -胰岛素与培养淋巴细胞的结合不受钙、镁或EDTA的影响。结合的最佳pH值约为7.8。胰岛素与细胞的结合不受dna酶、rna酶或神经氨酸酶消化的影响。然而，胰蛋白酶消化会破坏细胞结合胰岛素的能力。
Insulin interactions with human lymphocytes in established cultures and with isolated peripheral lymphocytes have been studied using125I-insulin. Receptors in circulating lymphocytes are indistinguishable from those found in cultured cells, and the lymphocyte receptors show striking similarities to those structures described in fat cell and liver preparations. In lymphocytes, the ability of insulin or insulin analogues to inhibit binding of125I-insulin is directly proportional to the ability of that preparation to inhibit binding of labeled hormone to purified liver membranes or to stimulate glucose oxidation in the fat cell.Binding of125I-insulin to lymphocytes is a rapid and reversible process. Binding is maximal at 15°. Dissociation rate studies revealed a biphasic curve and the constants obtained were 8.3x10-5s-1and 8.3x10-4s-1. The apparent affinity constants of the two orders of binding sites in the cultured lymphocytes were 1.2x1010m-1and 1.1x109m-1, whereas in the normal circulating lymphocytes the values were 2.0x109m-1and 1.4x108m-1. At 30° there is very little degradation of labeled insulin by lymphocytes, and at 15° there is no detectable degradation with cultured or circulating cells.Binding of125I-insulin to cultured lymphocytes is unaffected by Ca++, Mg++, or EDTA. The optimum pH for binding occurs at about 7.8. Insulin binding to cells is unaffected by digestion with DNase, RNase, or neuraminidase. However, tryptic digestion destroys the capacity of the cells to bind insulin.