Skeletal ability to resist mechanical stress is determined by bone amount and quality, which relies on macro- and micro-architecture, turnover, bone matrix, and mineralisation; the role of collagen has not been clearly elucidated. Numerous post-translational steps are involved in collagen type I biosynthesis, including residue hydroxylation and glycosylation catalysed by enzymes that work until the protein folds forming the triple helix; therefore, folding rate regulates these processes. Overglycosylated hydroxylysines are poor substrates for e-amino group deamination which initiates cross-link formation. Three clinical conditions associated with fractures may relate collagen overglycosylation with bone quality: (i) Osteogenesis Imperfecta, in which genetic mutations distort triple helix conformation and slow folding rate favouring overglycosylation; (ii) diabetes mellitus, with collagen overglycosylation by AGE accumulation; and, (iii) menopause, according to experimental studies demonstrating ovariectomy-related trabecular bone collagen overglycosylation preventable by 17b-estradiol or tamoxifen. Specific actions on collagen of drugs used for bone protection should be explored in future studies.
|Data di pubblicazione:||2005|
|Titolo:||COLLAGEN OVERGLYCOSYLATION: A BIOCHEMICAL FEATURE THAT MAY CONTRIBUTE TO BONE QUALITY|
|Autori:||DOMINGUEZ LJ; BARBAGALLO M; MORO L|
|Tipologia:||Articolo su rivista|
|Citazione:||DOMINGUEZ LJ, BARBAGALLO M, & MORO L (2005). COLLAGEN OVERGLYCOSYLATION: A BIOCHEMICAL FEATURE THAT MAY CONTRIBUTE TO BONE QUALITY. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 330, 1-4.|
|Appare nelle tipologie:||01 - Articolo su rivista|