V. Lo Cascio et al., Urinary galactosyl-hydroxylysine in postmenopausal osteoporotic women: A potential marker of bone fragility, J BONE MIN, 14(8), 1999, pp. 1420-1424
Alterations of the collagen matrix, e.g., increased hydroxylation and glyco
sylation of lysyl residues in collagen I, were found in human osteoporotic
bone, and it was suggested that they could alter the mechanical properties
of skeleton. To test this hypothesis, we evaluated the content of galactosy
l-hydroxylysine (GHYL) in bone collagen, as assessed by its urinary excreti
on, and related it to the occurrence of fracture. Two hundred and fifteen u
nselected postmenopausal women with osteoporosis were divided in two subgro
ups (comparable for age, age of menopause, bone mineral density, and bioche
mical parameters of bone turnover) on the basis of the history of fragility
fracture; 115 patients had suffered no fracture and 100 patients had suffe
red one or more fractures 3 or more years before. Four urinary markers of b
one turnover (hydroxyproline, cross-linked N-telopeptide, free deoxypyridol
ine, and GHYL) were evaluated in all patients. There was: no difference bet
ween the two groups with regard to all the parameters studied except for GH
YL, which was significantly higher in the group with a history of fracture
(1.35 +/- 0.82 mmol/mol of creatinine [Cr] versus 1.03 +/- <0.48 mmol/mol.
Cr, p < 0.001); this marker did not correlate with other markers of bone re
modeling in the fracture group, indicating a possible defect in bone collag
en. In conclusion, provided that increased levels of urinary GHYL do reflec
t overglycosylation of hydroxylysine in bone collagen, the GHYL may be cons
idered a marker of bone collagen quality. Our results, showing higher urina
ry GHYL in osteoporosis patients with fracture, seem to confirm this sugges
tion.