The in Vivo Glycation of Diabetic Tendon Collagen Studied by Neutron Diffraction
| Autor: | L Wess, Tim J Wess, J D Baird, A Miller, R M Lindsay |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Male
Tail Glycosylation Neutron diffraction Tendons chemistry.chemical_compound Structural Biology Glycation medicine Animals Rats Inbred BB Molecular Biology Glycoproteins Neutrons Crystallography biology Cross-link Periodate Deuterium Rats Tendon Hydroxylysine Diabetes Mellitus Type 1 medicine.anatomical_structure Proteoglycan chemistry biology.protein Female Collagen Oxidation-Reduction |
| Zdroj: | Journal of Molecular Biology. 230:1297-1303 |
| ISSN: | 0022-2836 |
| Popis: | Glycation (non-enzymatic glycosylation) sites in the axial unit cell of diabetic tendon collagen were investigated by neutron diffraction. Samples of diabetic and control tendon were reacted with sodium borodeuteride and sodium cyanoborodeuteride. This facilitated deuteration at aldimine, aldol or ketoimine groups in the molecule. These are natural collagen cross-links and sites where non-enzymatic glycation had occurred. The introduction of a deuteron at specific locations allowed the diabetic glycation collagen to be treated as multiple isomorphous derivatives for neutron fibre diffraction. Neutron diffraction was conducted at the Institut Laue Langevin, Grenoble. Standard crystallographic refinement techniques (modified for axial projections) were used to determine the structure of the control (non-diabetic) and diabetic samples. The results are shown as difference maps, these indicate that glycation takes place at different rates within the collagen axial unit cell. The position of glycation correlates well with the position of hydroxylysine residues. The reactions of periodate with enzymatically attached sugars, proteoglycan, natural cross-links and glycation products lead to complications in map interpretation. |
| Databáze: | OpenAIRE |
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