Abstract
Understanding the anatomical structure and normal physiology of the lens is essential for understanding the pathogenesis of lens diseases. The anatomical structure of the pediatric lens is still developing after birth, including the size, weight and volume, the thickness and elasticity of the lens capsule, the density and proliferation rate of lens epithelial cells, the number of zonular fibers, the relationship between the posterior lens capsule and the anterior vitreous body, and so on. This chapter discusses how the anatomy and physiology of the lens change with age, the maintenance of lens transparency, and its associated factors, as well as the role of the lens in the refraction and accommodation of the eye, all of which will provide useful information for deciding on the appropriate therapeutic regimen for pediatric patients with lens diseases.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Iribarren R. Crystalline lens and refractive development. Prog Retin Eye Res. 2015;47:86–106.
Augusteyn RC, Nankivil D, Mohamed A, et al. Human ocular biometry. Exp Eye Res. 2012;102:70–5.
Augusteyn RC. On the growth and internal structure of the human lens. Exp Eye Res. 2010;90(6):643–54.
Augusteyn RC. Growth of the human eye lens. Mol Vis. 2007;13:252–7.
Brown NP, Bron AJ. Lens disorders: a clinical manual of cataract diagnosis. 3rd ed. Oxford: Butterworth-Heinemann; 1996. p. 19–23.
Bours J, Födisch HJ, Hockwin O. Age-related changes in water and crystallin content of the fetal and adult human lens, demonstrated by a microsectioning technique. Ophthalmic Res. 1987;19(4):235–9.
Scammon RE, Hesdorffer MB. Growth in mass and volume of the human lens in postnatal life. Arch Ophthalmol. 1937;17:104–12.
Broekhuyse RM. Phospholipids in tissues of the eye. 3. Composition and metabolism of phospholipids in human lens in relation to age and cataract formation. Biochim Biophys Acta. 1969;187(3):354–65.
Clapp CA. A communication upon the weight of infant’s lenses and their solids. Arch Ophthalmol. 1913;42:618–24.
Smith P. Diseases of crystalline lens and capsule. 1. On the growth of the crystalline lens. Trans Ophthalmol Soc UK. 1883;3:79–99.
Dische Z, Zelmenis G. The content and structural characteristics of the collagenous protein of rabbit lens capsules at different ages. Invest Ophthalmol. 1965;4:174–80.
Parmigiani CM, McAvoy JW. A morphometric analysis of the development of the rat lens capsule. Curr Eye Res. 1989;8(12):1271–7.
Fox J. Anatomy of the lens. Nurs Mirror. 1984;158(18):31–5.
Boulton M, Albon J. Stem cells in the eye. Int J Biochem Cell Biol. 2004;36:643–57.
Francois J, Victoria-Troncoso V. Histology of the epithelium of the normal and cataractous lens. Ophthalmologica. 1978;177(3):168–74.
Vrensen GF. Aging of the human eye lens-a morphological point of view. Comp Biochem Physiol A Physiol. 1995;111(4):519–32.
Wallentin N, Wickstrom K, Lundberg C. Effect of cataract surgery on aqueous TGF-beta and lens epithelial cell proliferation. Invest Ophthalmol Vis Sci. 1998;39(8):1410–8.
Meacock WR, Spalton DJ, Stanford MR. Role of cytokines in the pathogenesis of posterior capsule opacification. Br J Ophthalmol. 2000;84(3):332–6.
Duncan G. Lens cell growth and posterior capsule opacification: in vivo and in vitro observations. Br J Ophthalmol. 1998;82(10):1102–3.
Streeten BW. The nature of the ocular zonule. Trans Am Ophthalmol Soc. 1982;80:823–54.
Streeten BW, Swann DA, Licari PA, et al. The protein composition of the ocular zonules. Invest Ophthalmol Vis Sci. 1983;24(1):119–23.
Streeten BW, Licari PA. The zonules and the elastic microfibrillar system in the ciliary body. Invest Ophthalmol Vis Sci. 1983;24(6):667–81.
Mackool RJ, Chhatiawala H. Pediatric cataract surgery and intraocular lens implantation: a new technique for preventing or excising postoperative secondary membranes. J Cataract Refract Surg. 1991;17(1):62–6.
Trokel S. The physical basis for transparency of the crystalline lens. Invest Ophthalmol. 1962;1:493–501.
Lo WK, Biswas SK, Brako L, et al. Aquaporin-0 targets interlocking domains to control the integrity and transparency of the eye lens. Invest Ophthalmol Vis Sci. 2014;55(3):1202–12.
Cvekl A, Ashery-Padan R. The cellular and molecular mechanisms of vertebrate lens development. Development. 2014;141(23):4432–47.
Jaenicke R, Slingsby C. Lens crystallins and their microbial homologs: structure, stability, and function. Crit Rev Biochem Mol Biol. 2001;36(5):435–99.
Bassnett S. On the mechanism of organelle degradation in the vertebrate lens. Exp Eye Res. 2009;88(2):133–9.
Rhodes JD, Sanderson J. The mechanisms of calcium homeostasis and signalling in the lens. Exp Eye Res. 2009;88(2):226–34.
Lee DB. Error tolerance in helmholtzian accommodation. Ophthalmology. 2002;109(9):1589–90.
Schachar RA. Cause and treatment of presbyopia with a method for increasing the amplitude of accommodation. Ann Ophthalmol. 1992;24(12):445–7, 452.
Schachar RA, Cudmore DP, Black TD. Experimental support for Schachar’s hypothesis of accommodation. Ann Ophthalmol. 1993;25(11):404–9.
Kirkwood BJ, Kirkwood RA. Accommodation and presbyopia. Insight. 2013;38(3):5–8.
Sliney DH. How light reaches the eye and its components. Int J Toxicol. 2002;21(6):501–9.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2017 Springer Science+Business Media Singapore
About this chapter
Cite this chapter
Chen, W., Tan, X., Chen, X. (2017). Anatomy and Physiology of the Crystalline Lens. In: Liu, Y. (eds) Pediatric Lens Diseases. Springer, Singapore. https://doi.org/10.1007/978-981-10-2627-0_3
Download citation
DOI: https://doi.org/10.1007/978-981-10-2627-0_3
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-10-2626-3
Online ISBN: 978-981-10-2627-0
eBook Packages: MedicineMedicine (R0)