TNF RECEPTORS IN CHRONIC LYMPHOCYTIC-LEUKEMIA

被引：20

作者：

WAAGE, A

ESPEVIK, T

机构：

[1] Section of Haematology, Department of Medicine

[2] Institute of Cancer Research, University of Trondheim

来源：

LEUKEMIA & LYMPHOMA | 1994年 / 13卷 / 1-2期

关键词：

CHRONIC LYMPHOCYTIC LEUKEMIA; TUMOR NECROSIS FACTOR; TUMOR NECROSIS FACTOR RECEPTOR;

D O I：

10.3109/10428199409051650

中图分类号：

R73 [肿瘤学];

学科分类号：

100214 ;

摘要：

Two transmembrane receptors for tumor necrosis factor (TNF) with different molecular weight, 55 kD (p55) and 75 kD (p75), have been identified. In addition, the extracellular part of both receptors are shedded by proteolytic cleavage and exist as soluble receptors which bind to TNF in plasma and other biological fluids. Normal B cells produce TNF and express TNF receptors (R), mainly p75, upon stimulation. TNF costimulates DNA synthesis via the p75 receptor in normal B cells. The B cells from patients with chronic lymphocytic leukemia (CLL) produce TNF and have the capacity to express both receptor types. Also in malignant B cells the p75 receptor is dominant. TNF induce DNA synthesis in CLL cells via both receptors. CLL patients have elevated serum levels of soluble (s) TNFR and this is more pronounced in advanced disease. In conclusion, there is considerable support for TNF as an autocrine growth factor in CLL. However, the net effect of TNF is determined by the quantitative relationship between TNFR on the cell surface, TNF in plasma and sTNFR in plasma, and the affinities between TNF-p55 and TNF-p75. Due to increasing serum levels of sTNFR the significance of TNF as a growth factor is probably less important in advanced disease.

引用

页码：41 / 46

页数：6

共 35 条

[1]

Hohmann H.P., Remy R., Brockhaus M., van Loon A.P.G.M., Two different cell types have different major receptors for human tumor necrosis factor (TNFα), J. Biol. Chem., 264, pp. 14927-14934, (1989)

[2]

Banner D.W., D'arcy A., Janes W., Gentz R., Schoen-Feld H.-J., Broger C., Loetscher H., Lesslauer W., Crystal structure of the soluble human 55 kd TNF-receptor-human TNFbeta complex: implications for TNF activation, Cell, 73, pp. 431-445, (1993)

[3]

Lewis M., Tartaglia L.A., Lee A., Bennett G.L., Rice G.C., Wong G.H.W., Chen E.Y., Goeddel D.V., Cloning and expression of cDNA for two distinct mu-rine tumor necrosis factor receptors demonstrate one receptor is species specific, Proc. Natl. Acad. Sci. USA, 88, pp. 2830-2834, (1991)

[4]

Espevik T., Brockhaus M., Loetscher H., Nonstad U., Shalaby R., Characterization of binding and biological effects of monoclonal antibodies against a human tumor ne crosis factor receptor, J. Exp. Med., 171, pp. 415-426, (1990)

[5]

Tartaglia L.A., Goeddel D.V., Two TNF re ceptors, Immunol. Today, 13, pp. 151-153, (1992)

[6]

Shalaby M.R., Sundan A., Loetscher H., Brockhaus M., Lesslauer W., Espevik T., Binding and regulation of cellular functions by monoclonal antibodies against human tumor necrosis factor receptors, J. Exp. Med., 172, pp. 1517-1520, (1990)

[7]

Lantz M., Gullberg U., Nilsson E., Olsson I., Characterization in vitro of a human tumor necrosis factor-binding protein. A soluble form of a tumor necrosis factor receptor, J. Clin. Invest., 86, pp. 1396-1402, (1990)

[8]

Naume B., Johnsen A.-C., Espevik T., Sundan A., Gene expression and secretion of cytokines and cy-tokine receptors from highly purified CD56+ NK cells stim ulated with IL-2, IL-7 and IL-12, Eur. J. Immunol., (1993)

[9]

Porteu F., Brockhaus M., Wallach D., Engelmann H., Nathan C.F., Human neutrophil elastase releases a ligand-binding fragment from the 75.-kDa tumor necrosis fac tor (TNF) receptor, J. Biol. Chem., 266, pp. 18846-18853, (1991)

[10]

Liabakk N.-B., Sundan A., Lien E., Laegreid A., Bom-Bara M.P., Ranges G., Espevik T., The release of p55 TNF receptor from U937 cells studied by a new p55 immunoassay, J. Immunol. Methods, (1993)

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