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首页> 美国卫生研究院文献>Immunology >Lymphocyte chemotaxis in inflammation. IX. Further characterization of lymphocyte chemotactic lymphokines produced by purified protein derivative-stimulation in vitro and in vivo.
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Lymphocyte chemotaxis in inflammation. IX. Further characterization of lymphocyte chemotactic lymphokines produced by purified protein derivative-stimulation in vitro and in vivo.

机译：炎症中的淋巴细胞趋化性。九。体外和体内纯化蛋白衍生物刺激产生的淋巴细胞趋化性淋巴因子的进一步表征。

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As recently reported, one lymphocyte chemotactic factor (beta-LCF, mol. wt. about 27,000) released from activated guinea-pig lymphocytes appeared to be identical to one of the LCFs (LCF-d) isolated from extract of purified protein derivative (PPD)-induced delayed-type hypersensitivity skin reaction sites in guinea-pigs with respect to antigenicity and chemotactic effect for T cells. However, the mol. wt. of LCF-d (about 300,000) was clearly distinct from beta-LCF. The experiments were undertaken to clarify the problem. beta-LCF appeared to be bound to some protein of normal guinea-pig serum (GPS) because the chemotactic activity was revealed in the fraction corresponding to that of LCF-d when the mixtures of beta-LCF with GPS were applied to a Sephadex G-200 column. Additionally, binding experiments using fluorescein isothiocyanate (FITC)-labelled beta-LCF were performed; fluorescence was only detected in the chemotactic fraction. It was thus assumed that the lymphokine (beta-LCF) would be released from activated lymphocytes around the inflammatory tissue, then bound with serum protein exuded in the site and function as LCF-d. The possibility was supported by the evidence that beta-LCF like-chemotactic substance (mol. wt. about 27,000) was dissociated from LCF-d under acid conditions. The factor dissociated from LCF-d was also bound with GPS protein under neutral conditions and converted to high molecular substance resembling LCF-d physiochemically. Furthermore, the chemotactic activity of LCF-d was almost completely absorbed by antibody against GPS. It is thus considered that the chemotactic activity of LCF-d may be attributed to beta-LCF released from activated lymphocytes and that some serum protein which binds beta-LCF may function as a carrier protein in the DTH sites.
机译：如最近报道的，从活化的豚鼠淋巴细胞释放的一种淋巴细胞趋化因子（β-LCF，摩尔重量约27,000）似乎与从纯化蛋白衍生物（PPD）提取物中分离出的LCF之一（LCF-d）相同。 ）诱导豚鼠的迟发型超敏性皮肤反应位点对T细胞的抗原性和趋化作用。但是，摩尔。重量LCF-d（约300,000）的明显不同于beta-LCF。进行实验以弄清问题。 β-LCF似乎与正常豚鼠血清（GPS）的某些蛋白质结合，因为当将β-LCF与GPS的混合物应用于Sephadex G时，其趋化活性显示在与LCF-d相对应的分数中-200列。另外，进行了使用异硫氰酸荧光素（FITC）标记的β-LCF的结合实验；仅在趋化部分中检测到荧光。因此，假定淋巴因子（β-LCF）将从炎性组织周围的活化淋巴细胞中释放出来，然后与该部位渗出的血清蛋白结合并起LCF-d的作用。有证据表明在酸性条件下，β-LCF类趋化物质（摩尔重量约27,000）从LCF-d上解离了。从LCF-d解离的因子在中性条件下也与GPS蛋白结合，并在理化上转化为类似于LCF-d的高分子物质。此外，LCF-d的趋化活性几乎完全被抗GPS抗体吸收。因此认为，LCF-d的趋化活性可以归因于从活化的淋巴细胞释放的β-LCF，并且一些结合β-LCF的血清蛋白可以在DTH位点中充当载体蛋白。

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