Effects of photobleaching on selected advanced glycation end products in the human lens

BMC Research Notes

Line Kessel²  Ram H Nagaraj¹  Rooban Nahomi¹  Cibin T Raghavan¹  Thomas Holm² 

[1] Present address: Department of Ophthalmology, University of Colorado School of Medicine, 12800 East 19th Avenue, RC-1 North 5102, Aurora 80045, CO, USA;Department of Ophthalmology, Glostrup Hospital, Ringvej 57, Glostrup, 2600, Denmark

关键词: Treatment;    Laser;    Cataract;    Advanced glycation end products;   

Others  :  1090820
DOI  :  10.1186/s13104-015-0977-3

 received in 2014-12-30, accepted in 2015-01-06,  发布年份 2015

【 摘 要 】

Background

Cataract is the leading cause of blindness, especially in the developing world. To ease access to treatment, we have proposed that cataract could be treated non-invasively by photobleaching of the chemically modified proteins responsible for cataract formation. The present study was aimed at examining the optical and biochemical effects of the proposed treatment.

Methods

Human donor lenses were photobleaced using a 445 nm cw laser. Lens optical quality was assessed before and after photobleaching by light transmission and scattering. The concentration of the advanced glycation end products (AGEs) pentosidine, argpyrimidine, carboxymethyllysine, hydroimidazolone was measured.

Results

Transmission increased and AGE-related fluorescence decreased significantly after photobleaching but no changes were observed in the concentration of the measured AGEs.

Conclusions

We found a significant effect of the photobleaching treatment on lens optical parameters but we could not associate the optical findings to a change in the concentration of the AGEs we measured. This finding suggests that other AGEs were responsible for the observed photobleaching of the human lens after laser treatment. The biochemical nature of the photochemical reactions associated with photobleaching remains to be elucidated.

【 授权许可】

   
2015 Holm et al.; licensee BioMed Central.

【 图 表 】

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【 参考文献 】

• [1]Resnikoff S, Pascolini D, Etya’ale D, Kocur I, Pararajasegaram R, Pokharel GP, et al.: Global data on visual impairment in the year 2002. Bull World Health Organ 2004, 82:844-51.
• [2]Foster A: Who will operate on Africa’s 3 million curably blind people? Lancet 1991, 337:1267-9.
• [3]Bloch SB, Larsen M, Munch IC: Incidence of legal blindness from age-related macular degeneration in denmark: year 2000 to 2010. Am J Ophthalmol 2012, 153:209-13.
• [4]Buch H, Vinding T, Nielsen NV: Prevalence and causes of visual impairment according to World Health Organization and United States criteria in an aged, urban Scandinavian population: the Copenhagen City Eye Study. Ophthalmology 2001, 108:2347-57.
• [5]Tuulonen A, Salminen H, Linna M, Perkola M: The need and total cost of Finnish eyecare services: a simulation model for 2005–2040. Acta Ophthalmol 2009, 87(8):820-9.
• [6]Kessel L, Haargaard B, Boberg-Ans G, Henning V: Time trends in indication for cataract surgery. J Clinic Experiment Ophthalmol 2011, 2:174.
• [7]Ponce A, Sorensen C, Takemoto L: Role of short-range protein interactions in lens opacifications. Mol Vis 2006, 12:879-84.
• [8]Stradner A, Foffi G, Dorsaz N, Thurston G, Schurtenberger P: New insight into cataract formation: Enhanced stability through mutual attraction. Phys Rev Lett 2007, 99(19):198103.
• [9]Bloemendal H, de Jong W, Jaenicke R, Lubsen NH, Slingsby C, Tardieu A: Ageing and vision: structure, stability and function of lens crystallins. Prog Biophysics Mol Biol 2004, 86:407-85.
• [10]Hains PG, Truscott RJ: Age-dependent deamidation of lifelong proteins in the human lens. Invest Ophthalmol Vis Sci 2010, 51:3107-14.
• [11]Su SP, Lyons B, Friedrich M, McArthur JD, Song X, Xavier D, et al.: Molecular signatures of long-lived proteins: autolytic cleavage adjacent to serine residues. Aging Cell 2012, 11:1125-7.
• [12]Friedrich MG, Lam J, Truscott RJ: Degradation of an old human protein: age-dependent cleavage of gammaS-crystallin generates a peptide that binds to cell membranes. J Biol Chem 2012, 287:39012-20.
• [13]Truscott RJ: Macromolecular deterioration as the ultimate constraint on human lifespan. Ageing Res Rev 2011, 10:397-403.
• [14]Nagaraj RH, Linetsky M, Stitt AW: The pathogenic role of Maillard reaction in the aging eye. Amino Acids 2012, 42:1205-20.
• [15]Kessel L, Kalinin S, Soroka V, Larsen M, Johansson LBA: Impact of UVR-A on whole human lenses, supernatants of buffered human lens homogenates, and purified argpyrimidine and 3-OH-kynurenine. Acta Ophthalmol Scand 2005, 83:221-7.
• [16]Kessel L, Eskildsen L, van der Poel M, Larsen M: Non-invasive bleaching of the human lens by femtosecond laser photolysis. PLoS One 2010, 5:e9711.
• [17]Ortwerth BJ, Chemoganskiy V, Olesen PR: Studies on Singlet Oxygen Formation and UVA Light-mediated Photobleaching of the Yellow Chromophores in Human Lenses. Exp Eye Res 2002, 74:217-29.
• [18]Holm T, Brogger-Jensen MR, Johnson L, Kessel L: Glutathione Preservation during Storage of Rat Lenses in Optisol-GS and Castor Oil. PLoS One 2013, 8:e79620.
• [19]Kessel L, Lundeman JH, Herbst K, Andersen TV, Larsen M: Age-related changes in the transmission properties of the human lens and their relevance to circadian entrainment. J Cataract Refract Surg 2010, 36:308-12.
• [20]Puttaiah S, Biswas A, Staniszewska M, Nagaraj RH: Methylglyoxal inhibits glycation-mediated loss in chaperone function and synthesis of pentosidine in alpha-crystallin. Exp Eye Res 2007, 84:914-21.
• [21]Singh R, Barden A, Mori T, Beilin L: Advanced glycation end-products: a review. Diabetologia 2001, 44:129-46.
• [22]Grandhee SK, Monnier VM: Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors. J Biol Chem 1991, 266:11649-53.
• [23]Nahomi RB, Oya-Ito T, Nagaraj RH: The combined effect of acetylation and glycation on the chaperone and anti-apoptotic functions of human alpha-crystallin. Biochim Biophys Acta 1832, 2013:195-203.
• [24]Roberts JE, Wishart JF, Martinez L, Chignell CF: Photochemical studies on xanthurenic acid. Photochem Photobiol 2000, 72:467-71.
• [25]Tessier F, Obrenovich M, Monnier VM: Structure and mechanism of formation of human lens fluorophore LM-1. Relationship to vesperlysine A and the advanced Maillard reaction in aging, diabetes, and cataractogenesis. J Biol Chem 1999, 274:20796-804.
• [26]Cheng R, Feng Q, Argirov OK, Ortwerth BJ: K2P–a novel cross-link from human lens protein. Ann N Y Acad Sci 2005, 1043:184-94.
• [27]Argirov OK, Lin B, Ortwerth BJ: 2-ammonio-6-(3-oxidopyridinium-1-yl)hexanoate (OP-lysine) is a newly identified advanced glycation end product in cataractous and aged human lenses. J Biol Chem 2004, 279:6487-95.
• [28]Giblin FJ, Leverenz VR, Padgaonkar VA, Unakar NJ, Dang L, Lin LR, et al.: UVA light in vivo reaches the nucleus of the guinea pig lens and produces deleterious, oxidative effects. Exp Eye Res 2002, 75:445-58.
• [29]Dillon J, Roy D, Spector A, Walker ML, Hibbard LB, Borkman RF: UV laser photodamage to whole lenses. Exp Eye Res 1989, 49:959-66.
• [30]Mody VC Jr, Kakar M, Elfving A, Soderberg PG, Lofgren S: Ultraviolet radiation-B-induced cataract in albino rats: maximum tolerable dose and ascorbate consumption. Acta Ophthalmol Scand 2006, 84:390-5.
• [31]Oriowo OM, Cullen AP, Chou BR, Sivak JG: Action spectrum and recovery for in vitro UV-induced cataract using whole lenses. Invest Ophthalmol Vis Sci 2001, 42:2596-602.