Initiation of the decorin glycosaminoglycan chain in the endoplasmic reticulum-Golgi intermediate compartment
Författare
Summary, in English
We have transiently expressed decorin with a C- terminal KDEL endoplasmic reticulum retention signal peptide in COS- 7 cells to study initiation of galactosaminoglycan synthesis in the endoplasmic reticulum- Golgi intermediate compartment. All decorin- KDEL molecules were substituted with N- linked oligosaccharides sensitive to endoglycosidase H, indicating that the core protein was located proximal to the medial- Golgi. O-Linked glycosylation was only initiated in a minor fraction of the molecules. The O- linked saccharides were characterized by gel filtration after stepwise degradations using chondroitin ABC/ AC-I lyases, beta1 - 3- glycuronidase, beta-galactosidase, and alkaline phosphatase. The major O- linked saccharide was the linkage region pentasaccharide GalNAcbeta1-4GlcUAbeta1-3Galbeta1-3Galbeta1-4-Xyl- 2- phosphate, demonstrating initiation of chondroitin synthesis in the endoplasmic reticulum- Golgi intermediate compartment. In the presence of brefeldin A, partial elongation of a chondroitin chain took place, indicating retrieval of polymerases but not of sulfotransferases.
Avdelning/ar
- Bröstcancer-genetik
- Matrix Biology
- Institutionen för experimentell medicinsk vetenskap
- Åke Oldberg´s group
Publiceringsår
2003
Språk
Engelska
Sidor
21415-21420
Publikation/Tidskrift/Serie
Journal of Biological Chemistry
Volym
278
Issue
24
Dokumenttyp
Artikel i tidskrift
Förlag
American Society for Biochemistry and Molecular Biology
Ämne
- Cell and Molecular Biology
Status
Published
Forskningsgrupp
- Matrix Biology
- Åke Oldberg´s group
ISBN/ISSN/Övrigt
- ISSN: 1083-351X