Determinants of Glycosaminoglycan (GAG) Structure
Proteoglycans (PGs) are glycosylated proteins of biological importance at cell surfaces, in the extracellular matrix, and in the circulation. PGs are produced and modified by glycosaminoglycan (GAG) chains in the secretory pathway of animal cells. The most common GAG attachment site is a serine resi...
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| Format: | Article |
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MDPI AG
2015-08-01
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| Series: | Biomolecules |
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| Online Access: | http://www.mdpi.com/2218-273X/5/3/2003 |
| _version_ | 1818021807113895936 |
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| author | Kristian Prydz |
| author_facet | Kristian Prydz |
| author_sort | Kristian Prydz |
| collection | DOAJ |
| description | Proteoglycans (PGs) are glycosylated proteins of biological importance at cell surfaces, in the extracellular matrix, and in the circulation. PGs are produced and modified by glycosaminoglycan (GAG) chains in the secretory pathway of animal cells. The most common GAG attachment site is a serine residue followed by a glycine (-ser-gly-), from which a linker tetrasaccharide extends and may continue as a heparan sulfate, a heparin, a chondroitin sulfate, or a dermatan sulfate GAG chain. Which type of GAG chain becomes attached to the linker tetrasaccharide is influenced by the structure of the protein core, modifications occurring to the linker tetrasaccharide itself, and the biochemical environment of the Golgi apparatus, where GAG polymerization and modification by sulfation and epimerization take place. The same cell type may produce different GAG chains that vary, depending on the extent of epimerization and sulfation. However, it is not known to what extent these differences are caused by compartmental segregation of protein cores en route through the secretory pathway or by differential recruitment of modifying enzymes during synthesis of different PGs. The topic of this review is how different aspects of protein structure, cellular biochemistry, and compartmentalization may influence GAG synthesis. |
| first_indexed | 2024-04-14T08:24:01Z |
| format | Article |
| id | doaj.art-3b05e7359f5f46c0a0ee09604ece2a7d |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-04-14T08:24:01Z |
| publishDate | 2015-08-01 |
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| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-3b05e7359f5f46c0a0ee09604ece2a7d2022-12-22T02:04:08ZengMDPI AGBiomolecules2218-273X2015-08-01532003202210.3390/biom5032003biom5032003Determinants of Glycosaminoglycan (GAG) StructureKristian Prydz0Department of Biosciences, University of Oslo, Box 1066, Blindern OSLO 0316, NorwayProteoglycans (PGs) are glycosylated proteins of biological importance at cell surfaces, in the extracellular matrix, and in the circulation. PGs are produced and modified by glycosaminoglycan (GAG) chains in the secretory pathway of animal cells. The most common GAG attachment site is a serine residue followed by a glycine (-ser-gly-), from which a linker tetrasaccharide extends and may continue as a heparan sulfate, a heparin, a chondroitin sulfate, or a dermatan sulfate GAG chain. Which type of GAG chain becomes attached to the linker tetrasaccharide is influenced by the structure of the protein core, modifications occurring to the linker tetrasaccharide itself, and the biochemical environment of the Golgi apparatus, where GAG polymerization and modification by sulfation and epimerization take place. The same cell type may produce different GAG chains that vary, depending on the extent of epimerization and sulfation. However, it is not known to what extent these differences are caused by compartmental segregation of protein cores en route through the secretory pathway or by differential recruitment of modifying enzymes during synthesis of different PGs. The topic of this review is how different aspects of protein structure, cellular biochemistry, and compartmentalization may influence GAG synthesis.http://www.mdpi.com/2218-273X/5/3/2003ProteoglycansglycosaminoglycansPAPS3'-phosphoadenosine-5'-phosphosulfateGolgi apparatussecretory pathwayepithelial cellslinker region |
| spellingShingle | Kristian Prydz Determinants of Glycosaminoglycan (GAG) Structure Biomolecules Proteoglycans glycosaminoglycans PAPS 3'-phosphoadenosine-5'-phosphosulfate Golgi apparatus secretory pathway epithelial cells linker region |
| title | Determinants of Glycosaminoglycan (GAG) Structure |
| title_full | Determinants of Glycosaminoglycan (GAG) Structure |
| title_fullStr | Determinants of Glycosaminoglycan (GAG) Structure |
| title_full_unstemmed | Determinants of Glycosaminoglycan (GAG) Structure |
| title_short | Determinants of Glycosaminoglycan (GAG) Structure |
| title_sort | determinants of glycosaminoglycan gag structure |
| topic | Proteoglycans glycosaminoglycans PAPS 3'-phosphoadenosine-5'-phosphosulfate Golgi apparatus secretory pathway epithelial cells linker region |
| url | http://www.mdpi.com/2218-273X/5/3/2003 |
| work_keys_str_mv | AT kristianprydz determinantsofglycosaminoglycangagstructure |