F. D'Amico et al., Lectin binding sites in parotid acinar secretory granules of normal and isoproterenol treated rat, J SUBMIC CY, 31(1), 1999, pp. 115-121
Lectin staining patterns in secretory granules of rat parotid gland acinar
cell of untreated and isoproterenol-injected animals were examined by elect
ron microscopy. We used four lectin-gold complexes: Ulex europaeus agglutin
in I (UEA-I), Helix pomatia agglutinin (HPA), wheat germ agglutinin (WGA),
Glycine max agglutinin (SBA). Specimens were low temperature embedded in th
e hydrophilic Lowicryl K4M resin. The normal acinar cells produced glycocon
jugates which were positive for all of the lectins used and with a characte
ristic topographic distribution in relation to the morphological type of gr
anule. The cells of isoproterenol-treated rat showed marked ultrastructural
changes in the size and structure of granules; significant changes in lect
in binding sites in the granules were also observed.