Rat Submandibular Gland during the
Maturation Process: Changes in Enzyme Activities, Protein and
Lectin-Binding Profiles
M. PRZYBYŁO, A. LITYŃSKA, D. HOJA-ŁUKOWICZ, E. KREMSER
Department of Animal Physiology, Institute of Zoology, Jagiellonian
University,
Kraków, Poland
Received January 7, 2003
Accepted July 31, 2003
Summary
The total protein glycosylation profile and specific activity of lysosomal
enzymes were investigated in rat submandibular glands isolated from very
young (1-month), young (1.5-months) and adult rats (3-months) rats. The
specific activity of lysosomal hydrolases (i.e. acid phosphatase,
arylsulfatases A and B, β-N-acetyl-D-glucosaminidase, β-galactosidase and
β-glucuronidase) decreased in parallel to increasing age of the animals.
Furthermore, the thermal stability of acid phosphatase and
β-N-acetyl-D-glucosaminidase was influenced by the age of rats.
Age-related changes in protein profile regarding the intensity of
particular bands as well as the appearance of certain proteins limited to
special age groups were also demonstrated as revealed by Coomassie and
lectin staining. Moreover, the marked age-related increase in structures
Man (α1-2, α1-3, α1-6) Man, Fuc (α1-6) GlcNAc as well as Gal (β1-3) GlcNAc
was observed, whereas staining with terminal NeuAc and GlcNAc showed an
inverse correlation. The reaction with (β1-6) branched N-glycans and Gal
(β1-3) Gal structures was limited to 1-month-old rats. No significant
changes in a specific reaction with NeuAc (α2-3) Gal were observed. We
speculate that the observed differences with respect to protein and
glycosylation profiles between 1-month-old rats and older ones could be
caused by a modification of the diet composition as well as by the
functional and morphological maturation of the rat submandibular gland.
Key words
Lectins • Lysosomes • Maturation • Oligosaccharides • Submandibular gland
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