Proteodermatan and Proteokeratan Sulfate (Decorin, Lumican/Fibromodulin) Proteins Are Horseshoe Shaped. Implications for Their Interactions with Collagen

• Published in: Biochemistry (Easton) Vol. 35; no. 27; pp. 8795 - 8799
• Main Author: Scott, John. E
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 09.07.1996
• Subjects: Amino Acid Sequence; Carbohydrate Sequence; Carrier Proteins - metabolism; Carrier Proteins - ultrastructure; Chondroitin Sulfate Proteoglycans - metabolism; Chondroitin Sulfate Proteoglycans - ultrastructure; Collagen - metabolism; Decorin; Dermatan Sulfate - analogs & derivatives; Dermatan Sulfate - metabolism; Dermatan Sulfate - ultrastructure; Extracellular Matrix Proteins; Fibromodulin; Keratan Sulfate - metabolism; Keratan Sulfate - ultrastructure; Lumican; Microscopy, Electron; Models, Molecular; Molecular Sequence Data; Protein Binding; Proteoglycans - metabolism; Proteoglycans - ultrastructure; Repetitive Sequences, Nucleic Acid; Shadowing (Histology)
• ISSN: 0006-2960; 1520-4995
• DOI: 10.1021/bi960773t

The small proteoglycans proteodermatan and proteokeratan sulfates organize collagen fibrils in extracellular matrix [Scott, J. E. (1992) FASEB J. 6, 2639−2645], thus helping to maintain tissue shape. Their interaction with fibrils is probably via the protein. They have been examined by rotary shadowing-electron microscopy, which showed that these leucine-rich-repeat proteins are horseshoe shaped. Morphometry and comparison with polypeptide sequences suggest ways in which decorin could interact with tissue collagen fibrils. It is proposed that decorin is a bidentate ligand attached to two parallel neighboring collagen molecules in the fibril, helping to stabilize fibrils and orient fibrillogenesis.