Serial lectin affinity chromatography demonstrates altered asparagine-linked sugar chain structures of gamma-glutamyltransferase in human renal cell carcinoma.
Differences between human renal cortex and human renal cell carcinoma (RCC) in asparagine (Asn)-linked sugar chain structures of gamma-glutamyltransferase (GGT) were investigated by using a serial lectin affinity chromatographic technique. The relative amounts of GGT which passed through the concanavalin A (Con A) column but bound to the phytohaemagglutinin E column, were significantly decreased in RCC, but there were significant increases in the relative amounts of GGT which bound weakly to the Con A column and passed through the pea lectin (PSA) column, and bound strongly to the Con A column and bound to the wheat germ agglutinin column in RCC compared with those of the normal renal cortex. A significant correlation was observed in RCC between nuclear grade and relative amount of GGT which bound weakly to the Con A column and passed through the PSA column. The findings indicate that Asn-linked sugar chain structures are altered in RCC and suggest that studies of qualitative differences of sugar chain structures of GGT might lead to a useful diagnostic tool for human RCC.
Yoshida
K
K
Department of Urology, Dokkyo University School of Medicine, Tochigi, Japan.
Sumi
S
S
Honda
M
M
Hosoya
Y
Y
Yano
M
M
Arai
K
K
Ueda
Y
Y
D000328:Adult; D000368:Aged; D001216:Asparagine / Q000032:analysis*; D002292:Carcinoma, Renal Cell / Q000201:enzymology*; D002846:Chromatography, Affinity; D006801:Humans; D007202:Indicators and Reagents; D007672:Kidney Cortex / Q000201:enzymology; D007680:Kidney Neoplasms / Q000201:enzymology*; D037102:Lectins / Q000737:chemistry*; D008875:Middle Aged; D005723:gamma-Glutamyltransferase / Q000737:chemistry*
D007202:Indicators and Reagents; D037102:Lectins; D001216:Asparagine; D005723:gamma-Glutamyltransferase