I. Melezinek et al., TUMOR-TISSUE IS A SOURCE OF GAMMA-GLUTAMYL-TRANSPEPTIDASE SIALOFORM IN THE SERA OF MELANOMA-BEARING MICE, Melanoma research, 8(1), 1998, pp. 39-45
The total serum activity of gamma-glutamyl transpeptidase (GGT) was sh
own to increase with the growth of transplantable B16 and S91 melanoma
s in inbred mice. In an effort to define the source of the GGT shed in
to the bloodstream the physicochemical characteristics of the partiall
y purified GGT isoforms from liver, serum and B16 melanoma were compar
ed. The molecular weights of the serum and melanoma isoforms were iden
tical (86 kDa) and differed from that of the liver isoform (69 kDa). I
n polyacrylamide gel electrophoresis the serum and melanoma isoforms h
ad a similar mobility which exceeded that of the liver enzyme. Treatme
nt of the enzyme preparations with neuraminidase removed the differenc
es in the electrophoretic mobility of the three GGT isoforms studied.
On ion exchange chromatography on a DEAE-Spheron 300 LC column the mel
anoma and serum isoforms had an affinity to the sorbent unlike the liv
er isoform. Our observations suggest that melanoma cells express a sia
loform of GGT which is responsible for an increase in the total GGT se
rum activity. Biochemical and histochemical analyses did not reveal an
y increase in liver GGT production associated with melanoma developmen
t. Detection of the GGT isoform of tumour origin in sera ranks GGT amo
ng the specific melanoma markers. (C) 1998 Rapid Science Ltd.