HIGH-SENSITIVITY OF HUMAN-MELANOMA CELL-LINES TO THE GROWTH INHIBITORY ACTIVITY OF MYCOPLASMAL ARGININE DEIMINASE INVITRO

被引:77
作者
SUGIMURA, K
OHNO, T
KUSUYAMA, T
AZUMA, I
机构
[1] Institute of Immunological Science, Hokkaido University, Sapporo
[2] Biosciences Research Laboratory, Mochida Pharmaceutical Co. Ltd., Tokyo, 115, Kita-ku
关键词
ARGININE DEIMINASE; ARGININOSUCCINATE SYNTHETASE; CHEMOTHERAPEUTIC AGENT; GROWTH INHIBITOR; HUMAN MELANOMAS; L-ARGININE DEGRADING ENZYME; MYCOPLASMA; UREA CYCLE ENZYMES;
D O I
10.1097/00008390-199209000-00007
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Arginine deiminase (AD) is a potent growth inhibitor for some but not all tumour cell lines in vitro. As AD catalyses the direct conversion Of L-arginine to L-Citrulline, the AD-sensitivity of various tumour cells might be attributed to the levels of urea cycle enzymes involved in L-arginine biosynthesis. This study demonstrated that human melanoma cells were highly sensitive to the growth inhibitory activity ot AD. Five melanoma cell lines tested also exhibited reduced argininosuccinate synthetase (ASS) gene expression-being almost absent in four cell lines and at low level in one cell line. This resulted in an inability of the cells to utilize L-Citrulline for growth. Based on the tissue-specific regulation of ASS gene, the feature of melanomas suggests that it might be possible to develop agents with strong AD activity for chemotherapeutic use for human melanomas in vivo.
引用
收藏
页码:191 / 196
页数:6
相关论文
共 23 条
[1]  
Fenske J.D., Kenny G.E., Role of arginine deiminase in growth of Mycoplasma hominis, J Bacteriol, 126, pp. 501-510, (1976)
[2]  
Cole B.C., Naot Y., Sranbridge E.J., Et al., Interactions of mycoplasmas and their products with lymphoid cell in vitro, The Mycoplasmas, 4, pp. 203-257, (1985)
[3]  
Barile M.F., Levinthal B.G., Possible mechanisms for mycoplasma inhibition of lymphocyte transformation induced by phytohemagglutinin, Nature, 219, pp. 751-752, (1968)
[4]  
Copperman R., Morton H.E., Reversible inhibition of mitosis in lymphocyte cultures by non-viable mycoplasma, Proc Soc Exp Biol Med, 123, pp. 790-795, (1966)
[5]  
Sugimura K., Fukuda S., Wada Y., Et al., Identification and purification of arginine deiminase that originated from Mycoplasma arginini, Infect Immun, 58, pp. 2510-2515, (1990)
[6]  
Ohno T., Ando O., Sugimura K., Et al., Cloning and nucleotide sequence of the gene encoding arginine deiminase of Mycoplasma arginini, Infect Immun, 58, pp. 3788-3795, (1990)
[7]  
Beaudet A.L., O'brien W.E., Bock H.-G.O., Et al., The human argininosuccinate synthetase locus and citrullinemia, Adv Hum Genet, 15, pp. 161-196, (1986)
[8]  
Sugimura K., Kimura T., Arakawa H., Et al., Elevated argininosuccinate synthetase activity in adult T leukemia cell lines, Leukemia Res, 14, pp. 931-934, (1990)
[9]  
Ohno T., Kimura Y., Sugimura K., Et al., Elevated gene expression of argininosuccinate synthetase in peripheral lymphocytes from systemic lupus erythematosus (SLE) patients, Autoimmunity, (1992)
[10]  
Sugimura K., Ohno T., Fukuda S., Et al., Tumor growth inhibitory activity of a lymphocyte blastogenesis inhibitory factor, Cancer Res, 50, pp. 345-349, (1990)