Changes in N-acetyl-β-D-glucosaminidase binding system in rat liver during growth

In this paper, we characterize the binding of N-acetyl-β-D-glucosaminidase to membranes of rat liver during development. Cation-independent phosphomannosyl receptors were shown to be involved in the recognition of the enzyme at the following ages: 18 days of fetal life, 10-, 30- and 90-day-old rats....

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Bibliographic Details
Published in:Mechanisms of ageing and development 1996-02, Vol.86 (2), p.75-81
Main Authors: Sosa, Miguel A., Belmonte, Silvia, Bertini, Francisco
Format: Article
Language:English
Subjects:
Acetylglucosaminidase - metabolism
Aging - metabolism
Analytical, structural and metabolic biochemistry
Animals
Animals, Newborn
Binding Sites
Biological and medical sciences
Enzymes and enzyme inhibitors
Female
Fetus - metabolism
Fundamental and applied biological sciences. Psychology
Hydrolases
Liver
Liver - enzymology
Lysosomal enzymes
N-acetyl-β-D-glucosaminidase
Pregnancy
Rats
Rats, Sprague-Dawley
Receptors
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Summary:In this paper, we characterize the binding of N-acetyl-β-D-glucosaminidase to membranes of rat liver during development. Cation-independent phosphomannosyl receptors were shown to be involved in the recognition of the enzyme at the following ages: 18 days of fetal life, 10-, 30- and 90-day-old rats. We remark here two important differences in the binding of the fetal enzyme when compared with that in 90-day-old rats; (a) in addition to an optimal binding at pH 7.0, the fetal enzyme showed another peak of binding at acidic pH (5.0), and (b) the binding of the fetal enzyme was also inhibited by galactose-6-phosphate. This inhibition was higher than that of mannose-6-phosphate at the acidic pH. We concluded that the lysosomal enzymes and their receptors undergo important changes around birth.
ISSN:0047-6374
1872-6216
DOI:10.1016/0047-6374(95)01678-3