L. Valladares et al., Characterization of the oligosaccharides of plasma sex hormone binding globulin from noncirrhotic alcoholic patients, STEROIDS, 65(5), 2000, pp. 275-280
In previous reports we have demonstrated high plasma levels of sex hormone-
binding globulin (SHBG) in asymptomatic alcoholic men. In the present work
the physicochemical properties of SHBG from plasma of noncirrhotic alcoholi
c patients have been further compared with SHBG of control subjects. Steroi
d binding to SHBG was similar for tilt: two groups: alcoholic men, K-d of 0
.62 +/- 0.07 nM and control individuals, K-d of 0.70 +/- 0.10 nM. The struc
ture of oligosaccharides attached to SHBG from controls and alcoholic men w
ere determined by using serial chromatography. Our data indicated that 7% o
f SHBG of control individuals was not retarded by the Con-A column, whereas
similar to 30% of SHBG of alcoholic men eluted in the void Volume of Con A
. Approximately 46% of SHBG of alcoholics applied to Con A, possessed biant
ennary complex oligosaccharides, as indicated by the fact that it could be
eluted with methyl-alpha-D-glucopyranoside and by its retention on wheat ge
rm agglutinin; in contrast, when SHBG from control men was analyzed, simila
r to 51% was eluted with methyl-alpha-D-glucopyranoside. Approximately 9% o
f the biantennary complex oligosaccharides on SHBG of control men and none
of those on SHBG from alcoholic men were fucosylated on the chitobiose core
, as determined by chromatography on Lenn culinaris lectin. Galactosylated
oligosaccharides were also present on the SHBG fraction as indicated by its
interaction with Ricinus communis-I. Approximately 24% of SHBG of alcoholi
c men and 39% of those on SHBG from control individuals applied to Con-A we
re retained and could be eluted with methyl-alpha-D-mannopyranoside. Eviden
ce based on the binding on mannoside-eluted SHBG to Con-A, wheat germ agglu
tinin, and R. communis-I indicated that at least the SHBG in this fraction,
from alcoholics or controls, contained two glycosylation sites and that th
e sites were differentially glycosylated. (C) 2000 Elsevier Science Inc. Al
l rights reserved.