FIND ARTICLE

Volume: 
Issue: 
2
Date of issue: 

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. Six genes are involved in the molecular pathoge- nesis of dystroglycanopathies: POMT-1, POMT-2, POMGnT-1, FKT, FKRP and LARGE. The former three are proved, and the further putative glycosyltransferases of O-mannosylation pathway. The mechanisms of dystroglycanopathy once again underline the peculiar regulatory role of glycosylation, indispensable for a proper function of particular proteins.

Author of the article: 

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

PBK Postępby biologi komórki