The functional interactions between CD98, β1-integrins, and CD147 in the induction of U937 homotypic aggregation
The functional interactions between CD98, β1-integrins, and CD147 in the induction of U937 homotypic aggregation
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DOI：
10.1182/blood.v98.2.374
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发表时间：
2001-07-15
期刊：
影响因子：
20.3
通讯作者：
Chain, B
中科院分区：
文献类型：
--
作者：
Cho, JY;Fox, DA;Chain, B
CD 98在造血细胞和非造血细胞上都有表达，并且涉及细胞生理学和免疫生物学的各种不同方面。在这项研究中，CD 98和其他粘附分子的前单核细胞系U937的表面上的功能之间的相互作用进行了检查，通过细胞聚集的定量测定。几种CD 98抗体诱导这些细胞的同型聚集，而不影响细胞活力或生长。通过对EDTA缺乏敏感性和对脱氧葡萄糖敏感性增加，可以区分由CD 98抗体诱导的聚集和由β 1-整合素（CD 29）连接诱导的聚集。通过诱导的蛋白酪氨酸磷酸化模式也可以区分由CD 98和CD 29诱导的聚集。一些CD 29抗体部分抑制CD 98诱导的聚集，这些抗体既不激动聚集，也不抑制β 1-整联蛋白与底物的结合。相反，一些CD 98抗体是CD 29诱导的聚集的有效抑制剂。β 2整联蛋白的抗体也部分抑制CD 29诱导的聚集。出乎意料的是，CD 147（一种功能尚不清楚的免疫球蛋白超家族成员）的2种抗体也是通过CD 98连接诱导的聚集和蛋白酪氨酸磷酸化的有效抑制剂。这项研究的结果支持CD 98在调节细胞聚集的多分子单位中的核心作用。(C)2001年，美国血液学会。
CD98 is expressed on both hematopoietic and nonhematopoietic cells and has been implicated in a variety of different aspects of cell physiology and immunobiology. In this study, the functional interactions between CD98 and other adhesion molecules on the surface of the promonocyte line U937 are examined by means of a quantitative assay of cell aggregation. Several of the CD98 antibodies induced homotypic aggregation of these cells without affecting cellular viability or growth. Aggregation induced by CD98 antibodies could he distinguished from that induced by beta1-integrin (CD29) ligation by lack of sensitivity to EDTA and by increased sensitivity to deoxyglucose, Aggregation induced via CD98 and CD29 could also be distinguished by the pattern of protein tyrosine phosphorylation induced. Some CD29 antibodies partially inhibited CD98-induced aggregation, and these antibodies were neither agonistic for aggregation nor inhibitors of beta1-integrin binding to substrates. Conversely, some CD98 antibodies were potent inhibitors of CD29-induced aggregation. Antibodies to beta2 integrins also partially inhibited CD29-induced aggregation. Unexpectedly, 2 antibodies to CD147, an immunoglobulin superfamily member whose function has remained unclear, were also potent inhibitors of both the aggregation and the protein tyrosine phosphorylation induced via CD98 ligation. The results of this study support a central role for CD98 within a multimolecular unit that regulates cell aggregation. (C) 2001 by The American Society of Hematology.