胰岛素与人类B淋巴母细胞的结合是HLA单倍型的一种功能。
Insulin binding to human B lymphoblasts is a function of HLA haplotype.
作者信息
Kittur D, Shimizu Y, DeMars R, Edidin M
出版信息
Proc Natl Acad Sci U S A. 1987 Mar;84(5):1351-5. doi: 10.1073/pnas.84.5.1351.
Abstract
A variety of genetic and biochemical evidence points to an association between major histocompatibility complex (MHC) haplotype and several types of cell surface receptors including epidermal growth factor and insulin receptors. We report evidence for such associations between human class I MHC antigens, HLA antigens, and specific insulin binding sites on human B lymphoblasts. We have measured insulin binding to cells of an HLA-heterozygous, Epstein-Barr virus-transformed B-cell line, LCL 721, and to derivative mutants from which all or part of the HLA complex had been deleted. The affinity, Ka, of insulin binding sites is approximately 10(8) M-1 in mutants expressing antigen HLA-B5 together with other HLA antigens and in mutants expressing only HLA-C. HLA-A1; HLA-A1,B8; HLA-A2,C; and HLA null mutants (not expressing any HLA antigens) bind insulin to sites with an affinity of approximately 10(9) M-1.
摘要
多种遗传和生化证据表明，主要组织相容性复合体（MHC）单倍型与多种类型的细胞表面受体之间存在关联，包括表皮生长因子受体和胰岛素受体。我们报告了人类I类MHC抗原、HLA抗原与人类B淋巴母细胞上特定胰岛素结合位点之间存在此类关联的证据。我们测量了胰岛素与HLA杂合的、爱泼斯坦-巴尔病毒转化的B细胞系LCL 721的细胞以及已缺失全部或部分HLA复合体的衍生突变体的结合情况。在表达抗原HLA-B5以及其他HLA抗原的突变体和仅表达HLA-C的突变体中，胰岛素结合位点的亲和力Ka约为10⁸ M⁻¹。HLA-A1；HLA-A1,B8；HLA-A2,C；以及HLA缺失突变体（不表达任何HLA抗原）以约10⁹ M⁻¹的亲和力将胰岛素结合到位点上。
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