Changes in the collagenous matrix of the aging human lamina cribrosa
Autor: | Wojciech S S Karwatowski, Victor Colin Duance, N. Avery, David L. Easty, Julie Albon |
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Jazyk: | angličtina |
Rok vydání: | 1995 |
Předmět: |
Adult
medicine.medical_specialty Lamina Adolescent Retinal Artery Matrix (biology) Arginine Cellular and Molecular Neuroscience chemistry.chemical_compound Hydroxyproline Glycation Internal medicine medicine Humans Pentosidine Amino Acids Child Aged Aged 80 and over Pyridinoline business.industry Lysine Age Factors Infant Newborn Infant Anatomy Middle Aged Sensory Systems Ophthalmology Collagen type I alpha 1 Endocrinology chemistry Solubility Child Preschool Cyanogen bromide sense organs Collagen business Sclera Research Article |
Popis: | AIMS--The age-related changes in the biochemical composition of the collagenous matrix of the human lamina cribrosa were investigated. METHODS--An age range (3 weeks to 92 years old) of human laminae cribrosae, dissected 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 peptides after cyanogen bromide digestion, and high performance liquid chromatography, respectively. RESULTS--Age-related changes included an increase in total collagen and a decrease in the proportion of type III collagen 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 product. CONCLUSION--These changes in collagen composition imply that the mechanical properties of the lamina cribrosa are altered, resulting in a stiffer, less resilient structure with age. Such alterations in structure may contribute to the increased susceptibility of the elderly to axonal damage in chronic open angle glaucoma. |
Databáze: | OpenAIRE |
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