Spectroscopic and biochemical correlations during the course of human lens aging
Open Access
- 6 March 2006
- journal article
- research article
- Published by Springer Nature in BMC Ophthalmology
- Vol. 6 (1) , 10
Abstract
Background: With age, the human lens accumulates variety of substances that absorbs and fluorescence, which explains the color of yellow, brunescent and nigrescent cataract in terms of aging. The aim of this study was to assess lens fluorophores with properties comparable to those of advanced glycated end products (AGEs) in relation to age in human lenses. These fluorescent compounds are believed to be involved in the development of cataract. Methods: Spectroscopic (UV-Vis-NIR) and fluorescence photography (CCD-Digital based image analysis) studies were carried out in randomly selected intact human lenses (2–85 years). AGE-like fluorophores were also measured in water soluble and insoluble (alkali soluble) fractions of human lenses (20–80 years). Results: Our experimental findings suggest that there was a progressive shift in the absorbance characteristic of intact lens in the range of λ 210 nm -λ 470 nm . A relative increase in the absorptivity at λ (511–520 nm) , with age, was also observed. In addition, the ratio of absorptivity at λ(511–520 nm) versus the maximum absorbance recorded at blue-end cut-off (210–470 nm) was also found to increase, with age. The fluorescent intensity in the intact lens at both UV-B (λ Ex312 nm) and UV-A (λ Ex365 nm ) were found to be positively correlated (r 2 = 0.91 & 0.94, respectively; Confidence interval 95%) upto 50 years of age. In addition, a concomitant changes in AGE- like fluorophores were also observed in the processed lens samples (soluble and insoluble fractions) along the age. A significant increase in the concentration of AGE- like fluorophores, both in intact and processed lens was observed during the period of 40 – 50 years. Conclusion: Based on the present investigation, it was concluded that significant changes do occur in the AGE-like fluorophores of human lenses during the period of 40–50 years.Keywords
This publication has 33 references indexed in Scilit:
- Human Lens Coloration and AgingJournal of Biological Chemistry, 1999
- Role of the Maillard Reaction in Diabetes Mellitus and Diseases of AgingDrugs & Aging, 1996
- ADVANCED PROTEIN GLYCOSYLATION IN DIABETES AND AGINGAnnual Review of Medicine, 1995
- Isolation and characterization of a blue fluorophore from human eye lens crystallins: In vitro formation from Maillard reaction with ascorbate and riboseBiochimica et Biophysica Acta (BBA) - General Subjects, 1992
- Glycation of lens proteins by the oxidation products of ascorbic acidBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- In vitro non-enzymatic glycation and formation of browning products in the bovine lens α-crystallinExperimental Eye Research, 1990
- Production and characterization of antibodies to advanced glycation products on proteinsBiochemical and Biophysical Research Communications, 1989
- Lipid peroxidation in cataract of the humanLife Sciences, 1986
- Accumulation of diabetic rat peripheral nerve myelin by macrophages increases with the presence of advanced glycosylation endproducts.Journal of Experimental Medicine, 1984
- Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived ProteinsScience, 1981