Mechanism of formation of human IgE-binding factors (soluble CD23): III. Evidence for a receptor (Fc epsilon RII)-associated proteolytic activity.

Mechanism of formation of human IgE-binding factors (soluble CD23): III. Evidence for a receptor (Fc epsilon RII)-associated proteolytic activity.
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DOI:
10.1084/jem.172.3.693
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发表时间:
1990-09-01
期刊:
The Journal of experimental medicine
影响因子:
--
通讯作者:
Delespesse G
Delespesse G
中科院分区:
其他
文献类型:
--
作者:
Letellier M;Nakajima T;Pulido-Cejudo G;Hofstetter H;Delespesse G

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越来越多的证据表明Fc CD 23及其可溶性片段(IgE结合因子[BF]或可溶性CD 23)具有多效性活性。IgE-BF主要通过表面Fc ε RII的蛋白水解切割形成;它们首先作为37-和33-kD不稳定分子释放,随后转化为25-kD IgE-BF。在这项研究中,纯化和放射性碘标记的37-kD IgE-BFs以及45-kD Fc β RII被用作底物,以鉴定导致25-kD IgE-BFs形成的蛋白酶。当与几种携带Fc RII的细胞(包括CHO 1 -7细胞(用Fc RII cDNA转染))孵育时,这些底物产生25-kD IgE-BF;相比之下,Fc RII-细胞(包括CHO对照细胞)没有影响。高度纯化的未标记的天然37-kD和重组29-kD IgE-BF也将标记的45-kD Fc ε RII切割成25-kD IgE-BF。这些纯化的IgE-BF的蛋白水解活性通过与针对IgE-BF的抗体的免疫沉淀而被特异性地去除。这些数据有力地表明,Fc β RII和它的一些可溶性片段在产生IgE-BF的蛋白水解机制中起着积极的作用。由CHO 1 -7细胞释放的IgE-BF在与B细胞衍生的IgE-BF完全相同的位点被切割的观察结果支持了上述观点。总的来说,结果与自体蛋白水解过程相容。
There is mounting evidence that Fc epsilon RII (CD23) and its soluble fragments (IgE-binding factors [BFs] or soluble CD23) have pleiotropic activities. IgE-BFs are formed mainly by the proteolytic cleavage of surface Fc epsilon RII; they are first released as 37- and 33-kD unstable molecules that are subsequently transformed into 25-kD IgE- BFs. In this study, purified and radioiodinated 37-kD IgE-BFs as well as 45-kD Fc epsilon RII were used as substrates to identify the proteases leading to the formation of 25-kD IgE-BFs. These substrates generate 25-kD IgE-BFs when incubated with several Fc epsilon RII- bearing cells, including CHO1-7 cells (transfected with Fc epsilon RII cDNA); by contrast Fc epsilon RII- cells, including CHO control cells, have no effect. Highly purified unlabeled native 37-kD and recombinant 29-kD IgE-BFs also cleave labeled 45-kD Fc epsilon RII into 25-kD IgE- BFs. The proteolytic activity of these purified IgE-BFs is specifically removed by immunoprecipitation with an antibody against IgE-BFs. These data strongly suggest that Fc epsilon RII and some of its soluble fragments play an active role in the proteolytic mechanism generating IgE-BFs. They are supported by the observation that IgE-BFs released by CHO1-7 cells are cleaved exactly at the same sites as B cell-derived IgE-BFs. Taken collectively, the results are compatible with an autoproteolytic process.
DOI: 10.1016/0167-5699(86)90184-2
发表时间: 1986-01-01
期刊: IMMUNOLOGY TODAY
影响因子: --
作者:
CAPRON, A;DESSAINT, JP;TONNEL, AB
通讯作者: TONNEL, AB
DOI: 10.1073/pnas.82.24.8325
发表时间: 1985-12-01
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作者:
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发表时间: 1988-10-01
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发表时间: 1989-12-01
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发表时间: 1988-11-01
影响因子: 5.4
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