THE ROLE OF TUMOR-NECROSIS-FACTOR RECEPTORS IN CELL SIGNALING AND THE SIGNIFICANCE OF SOLUBLE FORM LEVELS IN THE SERUM

被引:12
作者
ABE, Y
WATANABE, Y
KIMURA, S
机构
[1] The Second Department of Surgery, Ehime University School of Medicine
来源
SURGERY TODAY-THE JAPANESE JOURNAL OF SURGERY | 1994年 / 24卷 / 03期
关键词
TUMOR NECROSIS FACTOR; RECEPTOR; SIGNALING; SERUM LEVEL;
D O I
10.1007/BF02032887
中图分类号
R61 [外科手术学];
学科分类号
摘要
Two types of tumor necrosis factor membrane receptors (TNF-R) have been identified, namely 55 and 75 kDa TNF-R. Soluble forms of these receptors are present in the human serum. Recent findings on the role of these two TNF-R in biological cell signaling and the clinical significance of the serum levels of soluble TNF-R (sTNF-R) were reviewed. It is not the uptake of TNF molecules into cells but rather the molecular capping of TNF-R on the cell membrane that initiates the biological activity of TNF. The 55 kDa TNF-R mediates major bioactivities of TNF, while the significance of 75 kDa TNF-R remains unclear. We herein suggest a new concept of the role of these two TNF-R: The 75 kDa TNF-R signal appeared to enhance that of 55 kDa TNF-R in the induction of ICAM-1 expression on HL-60 human promyelocytic leukemic cells. High serum levels of sTNF-R are reported in patients with malignancy, endotoxin shock, pneumonia, and autoimmune diseases. However, the source of elevated serum sTNF-R remains unclear. Studies on the clinical usefulness of serum sTNF-R levels as cancer and inflammation markers are now being carried out.
引用
收藏
页码:197 / 202
页数:6
相关论文
共 55 条
[1]  
Van Ostade X., Vandenabeele P., Everaerdt B., Loetscher H., Gentz R., Brockhaus M., Lesslauer W., Tavernier J., Brouckaert P., Fiers W., Human TNF mutants with selective activity on the p55 TNF receptor, Nature, 361, pp. 266-269, (1993)
[2]  
Old L.J., Tumor necrosis factor. Another chapter in the long history of endotoxin, Nature, 330, pp. 602-603, (1987)
[3]  
Sugarman B.J., Aggarwal B.B., Hass P.E., Figari I.S., Palladino M.A., Shepard H.M., Recombinant human tumor necrosis factor-α: Effects on proliferation of normal and transformed cells in vitro, Science, 230, pp. 943-945, (1985)
[4]  
Granger G.A., Willia T.W., Lymphocyte cytotoxicity in vitro: Activation and release of a cytotoxic factor, Nature, 218, pp. 1253-1254, (1968)
[5]  
Gray P.W., Aggarwal B.B., Benton C.V., Bringman T.S., Henzel W.J., Jarrett J.A., Leung D.W., Moffat B., Ng P., Svedersky L.P., Palladino M.A., Nedwin G.E., Cloning and expression of cDNA for human lymphotoxin, a lymphokine with tumour necrosis activity, Nature, 312, pp. 721-724, (1984)
[6]  
Pennica D., Nedwin G.E., Hayflick J.S., Seeburg P.H., Derynck R., Palladino M.A., Kohr W.J., Aggarwal B.B., Goeddel D.V., Human tumour necrosis factor: Precursor structure, expression, and homology to lymphotoxin, Nature, 312, pp. 724-729, (1984)
[7]  
Yokota S., Geppert T.D., Lipsky P.E., Enhancement of antigen- and mitogen-induced human T lymphocyte proliferation by tumor necrosis factor-α, J Immunol, 140, pp. 531-536, (1988)
[8]  
Kehrl J.H., Alvarez-Mon M., Delsing G.A., Fauci A.S., Lymphotoxin is an important T cell-derived growth factor for human B cells, Science, 238, pp. 1144-1146, (1987)
[9]  
Collins T., Lapierre L.A., Fiers W., Strominge J.L., Pober J.S., Recombinant human tumor necrosis factor increases mRNA levels and surface expression of HLA-A, B antigens in vascular endothelial cells and dermal fibroblasts in vitro, Proc Natl Acad Sci USA, 83, pp. 446-450, (1986)
[10]  
Most J., Schwaeble W., Drach J., Sommerauer A., Dierich M.P., Regulation of the expression of ICAM-1 on human monocytes and monocytic tumor cell lines, J Immunol, 148, pp. 1635-1642, (1992)