活化的人T淋巴细胞表达与β2-微球蛋白不相关的MHC I类重链。
Activated human T lymphocytes express MHC class I heavy chains not associated with beta 2-microglobulin.
作者信息
Schnabl E, Stockinger H, Majdic O, Gaugitsch H, Lindley I J, Maurer D, Hajek-Rosenmayr A, Knapp W
机构信息
Institute of Immunology, Vienna, Austria.
出版信息
J Exp Med. 1990 May 1;171(5):1431-42. doi: 10.1084/jem.171.5.1431.
Abstract
We present here the molecular characterization of a new activation-induced surface structure on human T lymphocytes, termed LA45, with high homology (93% at protein level) to MHC class I molecules. Antigen modulation and sequential immunoprecipitation experiments revealed that LA45 and HLA class I proteins do not crossreact with the corresponding antibodies. Furthermore, LA45 is not associated with beta 2-m. On the other hand, we could show that the separation of HLA-A,B,C and beta 2m molecules, induced by SDS-denaturation, leads to a conformational change in the heavy chain in such a way that it becomes reactive with LA45. The 90/45 kD LA45 proteins thus appear to be non-beta 2m-associated MHC class I alpha chains that are selectively expressed by activated but not by resting human T lymphocytes.
摘要
我们在此展示了人类T淋巴细胞上一种新的活化诱导表面结构LA45的分子特征，它与MHC I类分子具有高度同源性（蛋白质水平为93%）。抗原调节和连续免疫沉淀实验表明，LA45和HLA I类蛋白与相应抗体不发生交叉反应。此外，LA45与β2-微球蛋白不相关。另一方面，我们可以证明，SDS变性诱导的HLA-A、B、C和β2m分子的分离会导致重链构象发生变化，使其能够与LA45发生反应。因此，90/45 kD的LA45蛋白似乎是不与β2-微球蛋白相关的MHC I类α链，它们由活化的而非静止的人类T淋巴细胞选择性表达。
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