FIND ARTICLE

MUSCULAR DYSTROPHIES DUE TO DYSTROGLYCAN GLYCOSYLATION DISORDERS

Disorders in a unique type of posttranslational modification of a-dystroglycan lay at a background of a group of congenital muscular dystrophies, called dystroglycanopathies. To bind laminin in a basal membrane the protein has to be glycosylated in a special way, with mannose linked with O-glycosidic bond to serine or threonine in a mucin-like region. The nascent glycan is then elongated with N-acetylglucosamine, galactose, sialic acid and optionally fucose. It is also suggested that proper function of dystroglycan depends on mannose phosphorylation.

THE ROLE OF GLYCOPROTEINS IN IMMUNITY

Glycans are structures involved in many immunological processes. They covers the surfaces of all cells and they are added to protein and lipid backbones in the process called glycosylation. These molecules are recognized by variety of receptors presented or secreted by some of immunological system cells. Three the most significant receptors that recognize glycans has been described and these are galectins, C-type lectins and Siglecs.

The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

Editorial address:
Katedra i Zakład Histologii i Embriologii Uniwersytetu Medycznego w Poznaniu, ul. Święcickiego 6, 60-781 Poznań, tel. +48 61 8546453, fax. +48 61 8546440, email: mnowicki@ump.edu.pl

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