Specificity of immunoglobulin E and immunoglobulin G against human (recombinant DNA) insulin in human insulin allergy and resistance.

Specificity of immunoglobulin E and immunoglobulin G against human (recombinant DNA) insulin in human insulin allergy and resistance.
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发表时间:
1987-02
期刊:
The Journal of laboratory and clinical medicine
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通讯作者:
L. Grammer;M. Roberts;Thomas A. Buchanan;R. Fitzsimons;Boyd E. Metzger;R. Patterson
L. Grammer;M. Roberts;Thomas A. Buchanan;R. Fitzsimons;Boyd E. Metzger;R. Patterson
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其他
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作者:
L. Grammer;M. Roberts;Thomas A. Buchanan;R. Fitzsimons;Boyd E. Metzger;R. Patterson

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使用酶联免疫吸附试验方法,我们已经证明了免疫球蛋白E(IgE)和免疫球蛋白G(IgG)对人(重组DNA)胰岛素的患者的血清样本中的胰岛素治疗仅与人胰岛素。在开始人胰岛素治疗妊娠期糖尿病的12天内,患者出现了与人胰岛素高水平IgE相关的大的局部反应。随着局部反应消退,人胰岛素IgE水平降低。该患者的胰岛素需求量在妊娠期异常高,并随着人胰岛素IgG水平的下降而下降,提示存在免疫胰岛素抵抗因素。除了抗人胰岛素的IgE和IgG外,我们还能够证明该患者血清样本中存在抗猪和牛胰岛素的IgE和IgG。患者对每种胰岛素的即刻皮肤反应性相似。在抑制研究中,发现相似量的猪胰岛素、牛胰岛素或人胰岛素对人胰岛素与IgE或IgG结合的抑制率为50%。过量的猪胰岛素或牛胰岛素导致人胰岛素与IgE或IgG结合的完全抑制。因此,即使在胰岛素治疗的初始形式是人胰岛素的患者中,也发生了胰岛素过敏和可能导致胰岛素抵抗的人胰岛素IgG。此外,人胰岛素诱导的抗体识别的抗原决定簇也可能存在于牛胰岛素和猪胰岛素上,如本例所示。
Using an enzyme-linked immunosorbent assay method, we have demonstrated immunoglobulin E (IgE) and immunoglobulin G (IgG) against human (recombinant DNA) insulin in serum samples of a patient whose insulin therapy was only with human insulin. Within 12 days of initiation of human insulin for gestational diabetes, large local reactions developed in the patient in association with high levels of IgE to human insulin. As the local reactions subsided, the levels of IgE to human insulin decreased. The patient's insulin requirement was unusually high for pregnancy and tended to decrease in parallel with falling levels of IgG to human insulin, suggesting an element of immunologic insulin resistance. In addition to IgE and IgG against human insulin, we were able to demonstrate the presence of IgE and IgG against porcine and bovine insulin in the serum samples of this patient. The patient had similar immediate cutaneous reactivity to each insulin. In inhibition studies, similar amounts of porcine insulin, bovine insulin, or human insulin were found to produce 50% inhibition of human insulin binding to IgE or IgG against human insulin. Excess porcine insulin or bovine insulin resulted in total inhibition of human insulin binding to IgE or IgG. Thus even in a patient whose initial form of insulin therapy was human insulin, there was development of insulin allergy and of IgG to human insulin that may have contributed to insulin resistance. Moreover, the antigenic determinants recognized by antibody induced by human insulin may also be present on bovine insulin and porcine insulin as demonstrated in this case.