TY - JOUR
T1 - Antiproliferative effects of galectin-1 from Rana catesbeiana eggs on human leukemia cells and its binding proteins in human cells
AU - Yasumitsu, Hidetaro
AU - Mochida, Keiichi
AU - Yasuda, Chie
AU - Isobe, Masaharu
AU - Kawsar, Sarkar M.A.
AU - Fujii, Yuki
AU - Matsumoto, Ryo
AU - Kanaly, Robert A.
AU - Ozeki, Yasuhiro
N1 - Funding Information:
Acknowledgments The authors are grateful to Mr. H. Ito, Kihara Institute for Biological Research for his help. This work was supported by a grant for 2009 Strategic Research Project (No. T2114) of Yokohama City University, Japan and by the grant of 2010 Yokohama Academic Foundation.
PY - 2011/12
Y1 - 2011/12
N2 - Galectin-1 from American bullfrog, RCG1, was isolated to high purity, and its growth inhibitory properties against human cells were examined. The results demonstrated that highly purified RCG1 induced large cell aggregates and revealed cell-type-specific growth inhibition. It significantly inhibited all human leukemia cell lines tested such as HL-60, U937, and K562 cells but did not inhibit human colon cancer cell line, Colo 201, or mouse mammary tumor cell line FM3A cells. Although most of the galectin-induced growth inhibitions are known to be apoptic, RCG1 induced growth arrest and neither apoptosis nor necrosis. RCG1-mediated growth inhibition was specifically suppressed by the corresponding sugar, lactose, but not by sucrose or even the structurally similar sugar, melibiose. Several studies have reported that galectin-mediated biological functions were modulated by charge modification. Since the high purity of RCG1 was demonstrated but a moderate degree of growth inhibition occurred, it is possible protein charge modification was examined by isoelectric focusing, and it was found to be highly heterogeneous in charge. RCG1 binding proteins in human cells were analyzed by lectin blotting using biotinylated RCG1, and lectin blotting revealed that in human cell extracts the specific proteins at molecular weight 37 and 50 kDa possessed the responsive features of RCG1 binding and lactose competition.
AB - Galectin-1 from American bullfrog, RCG1, was isolated to high purity, and its growth inhibitory properties against human cells were examined. The results demonstrated that highly purified RCG1 induced large cell aggregates and revealed cell-type-specific growth inhibition. It significantly inhibited all human leukemia cell lines tested such as HL-60, U937, and K562 cells but did not inhibit human colon cancer cell line, Colo 201, or mouse mammary tumor cell line FM3A cells. Although most of the galectin-induced growth inhibitions are known to be apoptic, RCG1 induced growth arrest and neither apoptosis nor necrosis. RCG1-mediated growth inhibition was specifically suppressed by the corresponding sugar, lactose, but not by sucrose or even the structurally similar sugar, melibiose. Several studies have reported that galectin-mediated biological functions were modulated by charge modification. Since the high purity of RCG1 was demonstrated but a moderate degree of growth inhibition occurred, it is possible protein charge modification was examined by isoelectric focusing, and it was found to be highly heterogeneous in charge. RCG1 binding proteins in human cells were analyzed by lectin blotting using biotinylated RCG1, and lectin blotting revealed that in human cell extracts the specific proteins at molecular weight 37 and 50 kDa possessed the responsive features of RCG1 binding and lactose competition.
KW - Galectin-1
KW - Growth inhibition
KW - Human leukemia cells
KW - Lectin blot
KW - SDS-polyacrylamide electrophoresis
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U2 - 10.1007/s11626-011-9462-z
DO - 10.1007/s11626-011-9462-z
M3 - Article
C2 - 22012416
AN - SCOPUS:84856238402
VL - 47
SP - 728
EP - 734
JO - In Vitro Cellular and Developmental Biology - Plant
JF - In Vitro Cellular and Developmental Biology - Plant
SN - 1071-2690
IS - 10
ER -