Literature DB >> 9663790

Does glycosylation of lysosomal proteins show age-related changes in rat liver?

A Lityńska1, M Przybyło.   

Abstract

We studied the pattern of lectins binding by liver lysosomal proteins from rats between 18 days of gestation and 72 weeks of age. An analysis of the carbohydrate structure was carried out after an electrophoresis and blotting, followed by a very sensitive detection system with highly specific digoxigenin-labelled lectins. The only age-related differences were observed in the reaction with sialic acid--(MAA; Macckia amurensis, SNA; Sambucus nigra) and fucose--(AAA; Aleuria aurantia) specific lectins. Sialylation increased and fucosylation decreased with age. We also observed a specific reaction with Galanthus nivalis (GNA), Phaseolus vulgaris (PHA-L) and peanut agglutinin (PNA), without any significant changes with age.

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Year:  1998        PMID: 9663790     DOI: 10.1016/s0047-6374(98)00006-2

Source DB:  PubMed          Journal:  Mech Ageing Dev        ISSN: 0047-6374            Impact factor:   5.432


  2 in total

Review 1.  Glycan evolution in response to collaboration, conflict, and constraint.

Authors:  Stevan A Springer; Pascal Gagneux
Journal:  J Biol Chem       Date:  2013-01-17       Impact factor: 5.157

2.  Persistent H. pylori colonization in early acquisition age of mice related with higher gastric sialylated Lewis x, IL-10, but lower interferon-γ expressions.

Authors:  Yao-Jong Yang; Hsiao-Bai Yang; Jiunn-Jong Wu; Bor-Shyang Sheu
Journal:  J Biomed Sci       Date:  2008-12-27       Impact factor: 8.410

  2 in total

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