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同种异体移植排斥反应期间存在一种增强精氨酸酶活性的淋巴因子的证据。

Evidence for a lymphokine enhancing arginase activity during allograft rejection.

作者信息

Dy M, Schneider E, Mavier P, Kamoun P, Lebel B, Hamburger J

出版信息

J Immunol. 1983 Apr;130(4):1937-42.

PMID:6187826
Abstract

The production of urea and ornithine is increased greatly in spleen cell cultures of an allograft recipient in the presence of donor cells (secondary MLC) in comparison to that of primary MLC (without previous allograft). This phenomenon appears after 24 hr of culture and reaches its maximum at 48 hr. The greatest increase in urea production is observed when the recipient spleen cells are collected at the time of allograft rejection. To obtain this extra production of urea, the stimulating cells in MLC should specifically be of the donor type or at least bear one homology with donor cells at the K or D locus. The increased production of urea and ornithine during MLC results from the action of a lymphokine released by recipient cells in the presence of donor cells. This factor acts upon cells present in bone marrow, spleen, and elicited peritoneal cells but is absent or is present in smaller quantities in thymus and lymph node cells. Target cells of this factor possess numerous macrophage features and could be immature cells of the macrophage line. The lymphokine responsible for this phenomenon is heat-stable, destroyed by trypsin, chymotrypsin, and neuraminidase, and has a m.w. around 32,000. It acts upon its target cells by increasing arginase activity, which results in the production of a large amount of ornithine, an important precursor of polyamine biosynthesis.

摘要

与初次混合淋巴细胞培养(无先前同种异体移植)相比,在存在供体细胞的同种异体移植受体的脾细胞培养物(二次混合淋巴细胞培养)中,尿素和鸟氨酸的产生显著增加。这种现象在培养24小时后出现,并在48小时达到最大值。当在同种异体移植排斥时收集受体脾细胞时,观察到尿素产生的最大增加。为了获得这种额外的尿素产生,混合淋巴细胞培养中的刺激细胞应特别为供体类型,或者至少在K或D位点与供体细胞有一个同源性。混合淋巴细胞培养期间尿素和鸟氨酸产生的增加是由于受体细胞在存在供体细胞时释放的一种淋巴因子的作用。该因子作用于骨髓、脾脏和诱导腹膜细胞中的细胞,但在胸腺和淋巴结细胞中不存在或含量较少。该因子的靶细胞具有许多巨噬细胞特征并且可能是巨噬细胞系的未成熟细胞。负责这种现象的淋巴因子是热稳定的,被胰蛋白酶、糜蛋白酶和神经氨酸酶破坏,并且分子量约为32,000。它通过增加精氨酸酶活性作用于其靶细胞,这导致产生大量鸟氨酸,鸟氨酸是多胺生物合成的重要前体。

相似文献

1
Evidence for a lymphokine enhancing arginase activity during allograft rejection.同种异体移植排斥反应期间存在一种增强精氨酸酶活性的淋巴因子的证据。
J Immunol. 1983 Apr;130(4):1937-42.
2
[Production of urea during mixed leukocyte culture (MLC). Effect of presensitization by a skin allograft].[混合淋巴细胞培养(MLC)过程中尿素的产生。皮肤同种异体移植预致敏的影响]
C R Seances Acad Sci D. 1979 Dec 17;289(16):1245-9.
3
Demonstration of a concanavalin A-induced lymphokine enhancing arginase activity. Effect of presensitization by a skin allograft.刀豆球蛋白A诱导的淋巴因子增强精氨酸酶活性的证明。皮肤同种异体移植预致敏的影响。
Eur J Immunol. 1983 Dec;13(12):977-83. doi: 10.1002/eji.1830131205.
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Homogeneous interleukin 3 enhances arginase activity in murine hematopoietic cells.同源白细胞介素3增强小鼠造血细胞中的精氨酸酶活性。
Lymphokine Res. 1985 Spring;4(2):95-102.
5
Histamine production during the anti-allograft response. Demonstration of a new lymphokine enhancing histamine synthesis.抗同种异体移植反应过程中的组胺产生。一种增强组胺合成的新淋巴因子的证实。
J Exp Med. 1981 Feb 1;153(2):293-309. doi: 10.1084/jem.153.2.293.
6
Skin allografts generate an enhanced production of histamine and histamine-producing cell-stimulating factor (HCSF) by spleen cells in response to T cell mitogens.皮肤同种异体移植会使脾细胞在对T细胞有丝分裂原的反应中,组胺和组胺生成细胞刺激因子(HCSF)的产生增加。
J Immunol. 1983 May;130(5):2343-7.
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[Histamine production in mixed culture between allograft donor and recipient lymphocytes].
C R Seances Acad Sci D. 1979 Jun 11;288(21):1635-8.
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Targeted gene disruption of the heat shock protein 72 gene (hsp70.1) in the donor tissue is associated with a prolonged rejection-free survival in the murine skin allograft model.供体组织中热休克蛋白72基因(hsp70.1)的靶向基因破坏与小鼠皮肤同种异体移植模型中延长的无排斥存活期相关。
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Immunosuppressive and trafficking properties of donor splenic and bone marrow dendritic cells.供体脾脏和骨髓树突状细胞的免疫抑制及迁移特性
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Demonstration of a human lymphokine which renders macrophages cytotoxic.一种能使巨噬细胞产生细胞毒性的人体淋巴因子的证明。
Ann Immunol (Paris). 1977 Apr-Jun;128C(3):621-32.

引用本文的文献

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Arginase: an emerging key player in the mammalian immune system.精氨酸酶:哺乳动物免疫系统中的一个新兴关键分子。
Br J Pharmacol. 2009 Oct;158(3):638-51. doi: 10.1111/j.1476-5381.2009.00291.x. Epub 2009 Sep 17.