Journal of Applied Physiology, Vol 60, Issue 5 1615-1622, Copyright © 1986 by American Physiological Society
Origin of periodic acid-Schiff-reactive glycoprotein in human eccrine sweat
S. Yanagawa, H. Yokozeki and K. Sato
To evaluate the possible involvement of ductal blockade with periodic
acid-Schiff (PAS)-positive materials in the mechanism of hidromeiosis in
humans, skin slices were incubated with methacholine for 2 h and
PAS-positive materials localized histologically in the ductal lumen. In 20%
of the glands complete ductal blockade with PAS-positive materials was
noted. The characteristics and origin of such PAS-positive glycoproteins in
human sweat were then studied using various electrophoretic techniques.
One-dimensional sodium dodecylsulfate-polyacrylamide gel electrophoresis
(1-D SDS-PAGE) demonstrated considerable individual variation in the
electrophoretic pattern; however, four major bands at 45, 28, 20, and 18K
shared by different individuals, were PAS positive. Further studies using
two-dimensional SDS-PAGE, immunodiffusion and immunoaffinity chromatography
demonstrated that the PAS-positive glycoproteins are not derived directly
from serum because they are electrophoretically and antigenically distinct
from serum proteins, including alpha 1-glycoprotein, alpha
2-HS-glycoprotein, and alpha 1-antitrypsin. Since only dark cell granules
are densely stained in the histochemical PAS staining, and because
antiserum produced against the PAS-positive band selectively stained cells
facing the secretory coil lumen (which are most likely dark cells), it is
suggested that PAS-positive sweat glycoproteins are derived predominantly
from the dark cells.
