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Effect of Green Light from Doubled Frequency Neodymium-Doped Yttrium Aluminum Garnet (Nd:YAG) Laser in the Nanosecond Range on Rabbit’s Lens –In Vitro Study

Salwa Ahmed Abdelkawi, Nahed Hassan, Monazah Khafagi





INTRODUCTION: The unprotected eye is extremely sensitive to laser radiation and can be permanently damaged from direct or reflected beams. The area of the eye damaged by laser energy is dependent upon the wavelength of the incident laser beam, duration of exposure and tissue characteristics. This study aims to investigate the effect of intense green light from doubled frequency Neodymium-Doped Yttrium Aluminum Garnet (Nd:YAG) (532nm) in the nanosecond range on the protein of rabbits lenses after short and prolonged (6, 18 seconds) exposures.

METHODS: The fundamental wavelength (1064 nm) was frequency doubled in β- Barium Borate (BBO) crystal for second harmonic generation (SHG). Rabbits’ lenses were irradiated in vitro, and the effect of the laser was evaluated by comparing the protein concentration, structure and conformation by sodium dodecyle sulphate polyacrylamide electrophoresis (SDS-PAGE) and Fourier transform infrared spectroscopy (FTIR).

RESULTS: The results indicated a significant change in the soluble protein content, the molecular weights and the backbone structure of different lens crystallin fractions. These effects were more distinct when using laser with prolonged irradiation for 18 seconds than for 6 seconds.

CONCLUSION: Irradiation with frequency doubled Nd-YAG green laser seem to be cataractous if the lens is exposed to laser that is intense enough to warrant thermal protein aggregation, folding and denaturation


green light; Nd:YAG; SDS-PAGE


Shen Y R. The principles of nonlinear optics. John Wiley and Sons, Inc., Hoboken, New Jersey; 2002.

Agrawal G P. Applications of nonlinear fiber optics (4th ed.). Academic Press, San Diego, California, USA; 2006.

Boyd R W. Parametric versus nonparametric processes, In: Nonlinear Optics (3rd ed.), 2008. 13-15.

Han M, Giese G, Bille J. Second harmonic generation imaging of collagen fibrils in cornea and sclera. Opt express 2005; 13: 5791–7.

Brown DJ, Morishige N, Neekhra A, Minckler DS, Jester JV. Application of second harmonic imaging microscopy to assess structural changes in optic nerve head structure ex vivo. J Biomed Opt. 2007;12: 024029.

Galang J, Restelli A, Hagley EW,. Clark C W. A green laser pointer hazard. Natl Inst Stand Tech 2010;1668: 1-9.

Te EA. The next generation in laser treatments and the role of the green light high-performance system laser. Rev Urol 2006; 8: S24–S30.

Walsh LJ. The current status of laser applications in dentistry. Aust Dent J 2003; 48:146–55.

Bloemendal H. Molecular and cellular biology of the eye lens. Wiley, New York; 1981. 1-47.

Wistow GJ, Piatigorsky J. Lens crystallins: the evolution and expression of proteins for a highly specialized tissue. Annu Rev Biochem 1988; 57: 479- 504.

Delaye M, Tardieu A. Short-range order of crystalline proteins accounts for eye lens transparency. Nature 1983; 302:415- 7.

Spector A. The search for a solution to senile cataracts. Proctor lecture. Invest Ophthalmol Vis Sci 1984; 25: 130-46.

Kalasinsky VF, Johnson FB, Ferwerda R. Fourier transform infrared and Raman microspectroscopy of materials in tissue. Cell Mol Biol 1998; 44: 141-4.

Boskey A. Mineral changes in osteopetrosis. Crit Rev Eukaryo. Gene Expr 2003;13: 109-16.

Petry R, Schmitt M, Popp J. Raman spectroscopy – a prospective tool in the life sciences. Chem phys chem. 2003; 4: 14-30.

Lin SY, Li M J, Liang RC, Lee SM. Non-destructive analysis of the conformational changes in human lens lipid and protein structures of the immature cataracts associated with glaucoma. Spectrochim Acta A Mol Biomol Spectrosc 1998; 54: 1509 -17.

Lin SY, Chen K H, Li M J, Cheng W T and Wang S L. Evidence of octacalcium phosphate and type-B carbonated apatites deposited on the surface of explanted acrylic hydrogel intraocular lens. J Biomed Mater Res B Appl Biomater. 2004; 70: 203-8.

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurements with Folin Phenol reagent. J Biol Chem 1951; 193: 265-75.

Laemmli UK. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature1970; 2777: 680-5.

Lamba OP, Borchman D, Sinha SK, Shah J, Renugopalakrishanan V, Yappert MC. Estimation of the secondary structure and conformation of bovine lens crystallins by infrared spectroscopy: quantitative analysis and resolution by Fourier self-deconvolution and curve fit. Biochem Biophys Acta. 1993; 1163: 113- 23.

Haris PI, Chapman D. Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. Methods Mol Biol 1994; 22: 183-202.

Jackson M, Mantsch HH. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit Rev Biochem Mol Biol 1995; 30: 95-120.

Snedecor GW, Cochran WG. Statistical Methods,» 6th ed., Ames., Iowa, USA;1976.

Rigas S, Morgello s, Goldman IS, Wong PT. Human colorectal cancers display abnormal Fourier-transform infrared spectra. Proc Natl Acad Sci USA 1990; 87: 8140-4.

Steinert RF, Puliafito CA. Laser in ophthalmology: Principles and clinical applications of photodisruption., Philadelphia WB Saunders Co; 1985. 22- 35.

Puliafito CA, Wasson PJ, Steinert RF, Gragoudas ES. Neodymium –YAG laser surgery on experimental vitreous membranes. Arch Ophthalmol 1984;102: 843- 7.

Abdelkawi SA, Elawadi AI. Liquefaction of the vitreous humor floaters is a risk factor for lens opacity and retinal dysfunction. J Am Sci 2011; 7: 911-8.

Juhasz T, Loesel FH, Kurtz RM, Horvath C, Bille JF, Mourou G. Corneal refractive surgery with femtosecond lasers. IEEE J Select Topics Quantum Electron 1999; 5: 902–10.

Yilmaz S, Yilmaz E. Effect of melatonin and vitamin E on oxidative –antioxidative status in rats exposed to irradiation. Toxicology 2006; 222: 1-7.

Kessel L, Eskildsen L, Lundeman JH, Jensen OB, Larsen M. Optical effects of exposing intact human lenses to ultraviolet radiation and visible light. BMC Ophthalmol 2011; 11:41.

Regini JW, Grossmann JG, Timmins P, Harding JJ, Quantock AJ, Hodson SA. X-ray- and neutron-scattering studies of alpha-crystallin and evidence that the target protein sits in the fenestrations of the alpha crystalline shell. Invest Ophthalmol Vis Sci 2007;48: 2695-700.

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: 198103.

Takemoto L, Sorensen CM. Protein-protein interactions and lens transparency. Exp Eye Res 2008; 87: 496-501.

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.

Davies MJ, Truscott RJ. Photo-oxidation of proteins and its role in cataractogenesis. J Photochem Photobiol 2001; 63:114-25.

Erckens RJ, Jongsma FH, Wicksted JP, Hendrikse F, March WF, Motamedi M. Raman spectroscopy in ophthalmology: from experimental tool to applications in vivo. Lasers Med Sci 2001;16: 236–52.

Chen KH, Cheng WT, LI M J, Yang DM, Lin SY. Calcification of senile cataractous lens determined by Fourier transform infrared (FTIR) and Raman microspectroscopies. J Microsc 2005; 219: 36–41.

Trevino SR, Schaefer S, Scholtz JM, Pace CN. Increasing protein conformational stability by optimizing beta-turn sequence. J Mol Biol 2007; 373: 211–8.

Susi H, Byler DM. Protein structure by Fourier transform infrared spectroscopy: second derivative spectra. Biochem Biophys Res Commun 1983; 115: 391-7.

Bron AJ, Vrensen GF, Koretz J, Maraini G, Harding JJ. The ageing lens. Ophthalmologica 2000; 214: 86-104.

Warwick R. Anatomy of the Eye and Orbit, Philadelphia,W. B. Saunders Co; 1976.

Kuck J FR Jr. Chemical constituents of the lens. In: Gray More CN. Biochemistry of the Eye. New York, Academic Press, Inc; 1970. 183-260.

Surewicz WK, Olesen PR. On the thermal stability of alpha-crystallin a new insight from infrared spectroscopy. Biochemistry 1995; 34: 9655-60.

Fullera AA, Du D, Liu F, Davoren JE, Bhabha G, Kroon G. Evaluating beta-turn mimics as beta-sheet folding nucleators. Proc Natl Acad Sci USA 2009;106:11067-72.

Rose GD, Young WB, Gierasch LM. Interior turns in globular proteins. Nature 1983; 304: 654-7.

Orpiszewski J, Schoromann N, Kluve-Beckerman M, Liepnieks JJ, Benson MD. Protein aging hypothesis of Alzheimer disease. FASEB J 2000; 14: 1255-63.

Khakshoor O, Nowick JS. Artificial beta-sheets: Chemical Models of beta-Sheets. Curr Opin Chem Biol 2008; 12:722–9.

Szalontai B. Membrane protein dynamics: Limited lipid control. PMC Biophys 2009; 2: 1-17.

DOI: https://doi.org/10.22037/jlms.v3i4.3330