Aims-The age-related changes in the biochemical composition of the col
lagenous matrix of the human lamina cribrosa were investigated. Method
s-An age range (3 weeks to 92 years old) of human laminae cribrosae, d
issected free of any surrounding structures which contained collagen,
were analysed for collagen solubility (n=58) total collagen content (n
=46), proportion of collagen types (n=38), and collagen cross linking
(n=30), using hydroxyproline analysis, scanning densitometry of peptid
es after cyanogen bromide digestion, and high performance liquid chrom
atography, respectively. Results-Age-related changes included an incre
ase in total collagen and a decrease in the proportion of type III col
lagen within the lamina cribrosa. The collagen cross link pyridinoline
was present at low levels, but demonstrated no trend with age. An age
-related increase was found in pentosidine, an advanced glycation prod
uct. Conclusion-These changes in collagen composition imply that the m
echanical properties of the lamina cribrosa are altered, resulting in
a stiffer, less resilient structure with age. Such alterations in stru
cture may contribute to the increased susceptibility of the elderly to
axonal damage in chronic open angle glaucoma.