Your browser doesn't support javascript.
loading
Reduced Expression of EXTL2, a Member of the Exostosin (EXT) Family of Glycosyltransferases, in Human Embryonic Kidney 293 Cells Results in Longer Heparan Sulfate Chains.
Katta, Kirankumar; Imran, Tabasum; Busse-Wicher, Marta; Grønning, Mona; Czajkowski, Szymon; Kusche-Gullberg, Marion.
Afiliación
  • Katta K; From the Department of Biomedicine, University of Bergen, N-5009 Bergen, Norway and.
  • Imran T; From the Department of Biomedicine, University of Bergen, N-5009 Bergen, Norway and.
  • Busse-Wicher M; the Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom.
  • Grønning M; From the Department of Biomedicine, University of Bergen, N-5009 Bergen, Norway and.
  • Czajkowski S; From the Department of Biomedicine, University of Bergen, N-5009 Bergen, Norway and.
  • Kusche-Gullberg M; From the Department of Biomedicine, University of Bergen, N-5009 Bergen, Norway and Marion.Kusche@biomed.uib.no.
J Biol Chem ; 290(21): 13168-77, 2015 May 22.
Article en En | MEDLINE | ID: mdl-25829497
Heparan sulfate proteoglycans are ubiquitously located on cell surfaces and in the extracellular matrices. The negatively charged heparan sulfate chains interact with a multitude of different proteins, thereby influencing a variety of cellular and developmental processes, for example cell adhesion, migration, tissue morphogenesis, and differentiation. The human exostosin (EXT) family of genes contains five members: the heparan sulfate polymerizing enzymes, EXT1 and EXT2, and three EXT-like genes, EXTL1, EXTL2, and EXTL3. EXTL2 has been ascribed activities related to the initiation and termination of heparan sulfate chains. Here we further investigated the role of EXTL2 in heparan sulfate chain elongation by gene silencing and overexpression strategies. We found that siRNA-mediated knockdown of EXTL2 in human embryonic kidney 293 cells resulted in increased chain length, whereas overexpression of EXTL2 in the same cell line had little or no effect on heparan sulfate chain length. To study in more detail the role of EXTL2 in heparan sulfate chain elongation, we tested the ability of the overexpressed protein to catalyze the in vitro incorporation of N-acetylglucosamine and N-acetylgalactosamine to oligosaccharide acceptors resembling unmodified heparan sulfate and chondroitin sulfate precursor molecules. Analysis of the generated products revealed that recombinant EXTL2 showed weak ability to transfer N-acetylgalactosamine to heparan sulfate precursor molecules but also, that EXTL2 exhibited much stronger in vitro N-acetylglucosamine-transferase activity related to elongation of heparan sulfate chains.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: N-Acetilglucosaminiltransferasas / Proteínas Supresoras de Tumor / Heparitina Sulfato / Proteínas de la Membrana Límite: Animals / Humans Idioma: En Revista: J Biol Chem Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: N-Acetilglucosaminiltransferasas / Proteínas Supresoras de Tumor / Heparitina Sulfato / Proteínas de la Membrana Límite: Animals / Humans Idioma: En Revista: J Biol Chem Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos