Characterization of a Rana catesbeiana lectin-resistant mutant of leukemia P388 cells.

نویسندگان

  • K Nitta
  • K Ozaki
  • Y Tsukamoto
  • S Furusawa
  • Y Ohkubo
  • H Takimoto
  • R Murata
  • M Hosono
  • N Hikichi
  • K Sasaki
چکیده

Sialic acid-binding lectin (SBL-C) from Rana catesbeiana eggs inhibits the growth of tumor cells such as P388 and L1210 leukemia cells (K. Nitta et al., Cancer Res., 54: 920-927, 1994). Here we report the establishment of an SBL-resistant P388 variant cell line, RC-150. Both P388 and RC-150 cells were agglutinated by SBL-C; however, growth of RC-150 cells was unaffected by SBL-C. Cytoplasmic free Ca2+ concentration and transglutaminase activity of RC-150 cells were 0.5 (110 nM) and 3 times (0.62 nmol/mg/min) as high as those of P388 cells, respectively. Microvilli and microplicae were observed on the surface of P388 cells by scanning electron microscopy but were rarely seen on RC-150 cells. Dansylcadaverine-labeled SBL-C bound to both P388 and RC-150 cells. Binding of SBL-C to these tumor cells appears to be mediated by two species of wheat germ agglutinin-stained cell membrane sialoglycoproteins. Labeled SBL-C entered P388 but not RC-150 cells, suggesting that internalized SBL-C acts as an inhibitor of cell proliferation.

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منابع مشابه

Inhibition of cell proliferation by Rana catesbeiana and Rana japonica lectins belonging to the ribonuclease superfamily.

Two frog egg lectins [Rana catesbeiana lectin (SBL-C) and Rana japonica lectin] preferentially agglutinate a large variety of human and animal tumor cells but not blood cells, lymphocytes, or fibroblasts. These lectins belong to the superfamily of pyrimidine base-specific RNases. The two lectins bound to a heparin-Sepharose column and were eluted from the column by an increase of NaCl molarity....

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Isolation and Characterization of Rana catesbeiana Lectin and Demonstration of the Lectin-binding Glycoprotein of Rodent and Human Tumor Cell Membranes1

A lectin isolated from Rana catesbeiana eggs preferentially aggluti nates a large variety of human and animal tumor cells but not normal red blood cells, lymphocytes, or fibroblasts. The phenomenon correlates with a higher binding activity of the lectin with tumor cells. Chemical and physical analysis of the purified lectin indicates that the lectin is a low molecular weight basic polypeptide w...

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Inhibition of Cell Proliferation by Rana catesbeiana and Rana japonica Lectins Belonging to the Ribonuclease Superfamily

Two frog egg lectins [Rana catesbeiana lectin (SBL-C) and Rana japonica lectin] preferentially agglutinate a large variety of human and animal tumor cells but not blood cells, lymphocytes, or fibroblasts. These lectins belong to the superfamily of pyrimidine base-specific RNases. The two lectins bound to a heparin-Sepharose column and were eluted from the column by an increase of NaC! molarity....

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Inhibition of Cell Proliferation by Rana catesbeiana and Rana japonica Lectins Belonging to the Ribonuclease Superfamily

Two frog egg lectins [Rana catesbeiana lectin (SBL-C) and Rana japonica lectin] preferentially agglutinate a large variety of human and animal tumor cells but not blood cells, lymphocytes, or fibroblasts. These lectins belong to the superfamily of pyrimidine base-specific RNases. The two lectins bound to a heparin-Sepharose column and were eluted from the column by an increase of NaC! molarity....

متن کامل

Inhibition of Cell Proliferation by Rana catesbeiana and Rana japonica Lectins Belonging to the Ribonuclease Superfamily

Two frog egg lectins [Rana catesbeiana lectin (SBL-C) and Rana japonica lectin] preferentially agglutinate a large variety of human and animal tumor cells but not blood cells, lymphocytes, or fibroblasts. These lectins belong to the superfamily of pyrimidine base-specific RNases. The two lectins bound to a heparin-Sepharose column and were eluted from the column by an increase of NaC! molarity....

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عنوان ژورنال:
  • Cancer research

دوره 54 4  شماره 

صفحات  -

تاریخ انتشار 1994