Skip to main content

Molecular Interactions of Crystallins in Relation to Optical Properties

  • Chapter
Presbyopia Research

Abstract

The transparency of the lens depends on an even distribution of protein and water over distances comparable to the wavelength of light, while the degree of refraction is controlled partly by the ability of the lens to change shape. The core regions of certain lenses such as carp and rat have an extremely high refractive index as a result of high protein concentration, which confers rigidity on that region of the lens. By contrast the outer regions of these lenses, like the complete human lens, have a lower proportion of protein to water and are malleable (van Heyningen, 1976; Philipson, 1969; Fagerholm et al., 1981). Furthermore, there is an increasing protein concentration gradient from the periphery to the core of the lens, leading to a gradient of refractive index that almost abolishes spherical aberration (Fernald and Wright, 1983; Sivak, 1985).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Alcala, J., Katar, M., Rudner, G., and Maisel, H., 1988, Human beta crystallins: Regional and age related changes, Curr. Eye Res. 7:353–359.

    Article  PubMed  CAS  Google Scholar 

  • Argos, P., 1988, An investigation of protein subunit and domain interfaces, Protein Eng. 2:101–113.

    Article  PubMed  CAS  Google Scholar 

  • Askren, C. C., Yu, N.-T., and Kuck, J. F. R. Jr.,1979, Variation of the concentration of sulphydryl along the visual axis of aging lenses by Raman optical dissection technique, Exp. Eye Res. 29:647–54.

    Article  PubMed  CAS  Google Scholar 

  • Bax, B., and Slingsby C., 1989, Crystallization of a new form of the eye lens protein ßB2-crystallin, J. Mol Biol 208:715–717.

    Article  PubMed  CAS  Google Scholar 

  • Bax, B., Lapatto, R., Nalini, V., Driessen, H., Lindley, P. F., Mahadevan, D., Blundell, T. L., and Slingsby, C., 1990, X-ray analysis of ßB2-crystallin and evolution of oligomeric lens proteins, Nature 347:776–780.

    Article  PubMed  CAS  Google Scholar 

  • Benedek, G. B., Clark, J. I., Serralach, E. N., Young, C. Y., Mengel, L., Sauke, T., Bagg, A., and Benedek, K., 1979, Light scattering and reversible cataracts in the calf and human lens, Phil Trans. R. Soc. [A] 293 :329–340.

    Article  CAS  Google Scholar 

  • Berbers, G. A. M., Boermann, O. C., Bloemendal, H., and de Jong, W. W., 1982, Primary gene products of bovine ß-crystallin and reassociation of its aggregates, Eur. J. Biochem. 128:495–502.

    Article  PubMed  CAS  Google Scholar 

  • Berbers, G. A. M., Hoekman, W. A., Bloemendal, H., de Jong, W. W., Kleinschmidt, T., and Braunitzer, G., 1983, Proline and alanine rich N-terminal extension of the basic bovine ß-crystallin B1 chains, FEBS Lett. 161:225–229.

    Article  PubMed  CAS  Google Scholar 

  • Berbers, G. A. M., Hoekman, W. A., Bloemendal, H., de Jong, W. W., Kleinschmidt, T., and Braunitzer, G., 1984, Homology between the primary structures of the major β-crystallin chains, Eur. J. Biochem. 139:467–479.

    Article  PubMed  CAS  Google Scholar 

  • Bernai, J. D., 1964, The structure of liquids, ProC., R. Soc. [A] 280:299–322.

    Article  Google Scholar 

  • Bindels, J. G., Koppers, A., and Hoenders, H. J., 1981, Structural aspects of bovine β-crystallins: Physical characterization including dissociation-association behaviour, Exp. Eye Res. 33:333–343.

    Article  PubMed  CAS  Google Scholar 

  • Bloemendal, H., Hermsen, T., Dunia, I., and Benedetti, E. L., 1982, Association of the crystallins with the plasma membrane, Exp. Eye Res. 35:61–67.

    Article  PubMed  CAS  Google Scholar 

  • Blundell, T., Lindley, P. F., Miller, L. R., Moss, D. S., Slingsby, C., Turnell, W. G., and Wistow, G., 1981, The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II, Nature 289:771–777.

    Article  PubMed  CAS  Google Scholar 

  • Blundell, T., Lindley, P. F., Miller, L. R., Moss, D. S., Slingsby, C., Turnell, W. G., and Wistow, G., 1983, Interactions of γ-crystallin in relation to eye-lens transparency., Lens Res. 1:109–131.

    CAS  Google Scholar 

  • Breitman, M. L., Lok, S., Wistow, G., Piatigorsky, J., Treton, J. A., Gold, R. J. M., and Tsui, L.-C., 1984,γ-Crystallin family of the mouse lens: Structural and evolutionary relationships, Proc. Natl. Acad. Sci. U.S.A. 81:7762–7766.

    Article  PubMed  CAS  Google Scholar 

  • Chang, T., Jiang, Y.-J., Chiou, S.-H., and Chang, W.-C., 1988, Carp gamma-crystallin with high methionine content: Cloning and sequencing of the complementary DNA, Biochim. Bio-phys. Acta 951:226–229.

    Article  CAS  Google Scholar 

  • Croft, L. R., 1973, Amino and carboxy terminal sequence of γ-crystallin from haddock lens, Biochim. Biophys. Acta 295:174–177.

    Article  PubMed  CAS  Google Scholar 

  • de Jong, W. W., 1981, Evolution of lens and crystallins, in: Molecular and Cellular Biology of the Eye Lens (H. Bloemendal, ed.), John Wiley & Sons, New York, pp. 221–278.

    Google Scholar 

  • Delaye, M., and Tardieu, A., 1983, Short-range order of crystallin proteins accounts for eye lens transparency., Nature 302:415–417.

    Article  PubMed  CAS  Google Scholar 

  • Fagerholm, P. P., Philipson, B. T., and Linstrom, B., 1981, Normal human lens—the distribution of protein, Exp. Eye Res. 33:615–620.

    Article  PubMed  CAS  Google Scholar 

  • Fernald, R. D., and Wright, S. E., 1983, Maintenance of optical quality during crystalline lens growth, Nature 301:618–620.

    Article  PubMed  CAS  Google Scholar 

  • Harding, J. J., and Crabbe, M. J. C., 1984, in: The Eye: The Lens: development, proteins, metabolism, and cataract, vol. IB, 3rd ed. (H. Davson, ed.), Academic Press, London, pp. 207–492.

    Google Scholar 

  • Herbrink, P., van Westreenen, H., and Bloemendal, H., 1975, Further studies on the polypeptide chains of γ-crystallin, Exp. Eye Res. 20:541–548.

    Article  PubMed  CAS  Google Scholar 

  • Hum, T. P., and Augusteyn, R. C., 1987, The nature of disulphide bonds in rat lens proteins, Curr. Eye Res. 6:1103–1108.

    Article  PubMed  CAS  Google Scholar 

  • Janin, J., Miller, S., and Chothia, C., 1988, Surface, subunit interfaces and interior of oligomeric proteins, J. Mol. Biol. 204:155–164.

    Article  PubMed  CAS  Google Scholar 

  • Kuck, J. F. R., Yu, N.-T., and Askren, C. C., 1982, Total sulphydryl by Raman spectroscopy in the intact lens of several species: Variations in the nucleus and along the optical axis during aging, Exp. Eye Res. 34:23–37.

    Article  PubMed  CAS  Google Scholar 

  • Li, L.-K., Roy, D., and Spector, A., 1986, Changes in lens protein in concentric fractions from individual normal human lenses, Curr. Eye Res. 5:127–135.

    Article  PubMed  CAS  Google Scholar 

  • Lubsen, N. H., Aarts, H. J. M., and Schoenmakers, J. G. G., 1988, The evolution of lenticular proteins: The β- and γ-crystallin super gene family., Prog. Biophys. Mol. Biol. 51:47–76.

    Article  PubMed  CAS  Google Scholar 

  • Meakin, S. O., Breitman, M. L., and Tsui, L.-C., 1985, Structural and evolutionary relationships among five members of the human γ-crystallin gene family., Mol. Cell Biol. 5:1408–1414.

    PubMed  CAS  Google Scholar 

  • Philipson, B., 1969, Distribution of protein within the normal rat lens, Invest. Ophthalmol. 8:258–270.

    PubMed  CAS  Google Scholar 

  • Richardson, J. S., 1977, β-Sheet topology and the relatedness of proteins, Nature 268:495–500.

    Article  PubMed  CAS  Google Scholar 

  • Russell, P., Meakin, S. O., Hohman, T. C., Tsui, L.-C., and Breitman, M. L., 1987, Relationships between proteins encoded by three human γ-crystallin genes and distinct polypeptides in the eye lens, Mol. Cell Biol. 7:3320–3323.

    PubMed  CAS  Google Scholar 

  • Sergeev, Y. V., Chirgadze, Y. N., Mylvaganam, S. E., Driessen, H., Slingsby, C., and Blundell, T. L., 1988, Surface interactions of γ-crystallins in the crystal medium in relation to their association in the eye lens, Proteins Struct. Fund. Genet. 4:137–147.

    Article  CAS  Google Scholar 

  • Siezen, R. J., Fisch, M. R., Slingsby, C., and Benedek, G. B., 1985, Opacification of γ-crystallin solutions from calf lens in relation to cold cataract formation, Proc. Natl. Acad. Sci. U.S.A. 82:1701–1705.

    Article  PubMed  CAS  Google Scholar 

  • Siezen, R. J., Anello, R. D., and Thomson, J. A., 1986, Interactions of lens proteins. Concentration dependence of β-crystallin aggregation, Exp. Eye Res. 43:293–303.

    Article  PubMed  CAS  Google Scholar 

  • Siezen, R. J., Thomson, J. A., Kaplan, E. D., and Benedek, G. B., 1987, Human lens γ-crystallins: Isolation, identification, and characterization of the expressed gene products, Proc. Natl. Acad. Sci. U.S.A. 84:6088–6092.

    Article  PubMed  CAS  Google Scholar 

  • Siezen, R. J., Wu, E., Kaplan, E., Thomson, J. A., and Benedek, G. B., 1988, Rat lens γ-crystallins, J. Mol. Biol. 199:475–490.

    Article  PubMed  CAS  Google Scholar 

  • Sivak, J. G., 1985, Optics of the crystalline lens, Am. J. Optom. Physiol. Opt. 62:299–308.

    Article  PubMed  CAS  Google Scholar 

  • Slingsby, C., 1985, Structural variation in lens crystallins, Trends Biochem. Sci. 10:281–284.

    Article  CAS  Google Scholar 

  • Slingsby, C., and Bateman, O. A., 1990, Quaternary interactions in eye lens β-crystallins: Basic and acidic subunits of β-crystallins favor heterologous association, Biochemistry 29:6592–6599.

    Article  PubMed  CAS  Google Scholar 

  • Slingsby, C., Miller, L. R., and Berbers, G. A. M., 1982, Preliminary x-ray crystallographic study of the principle subunit of the lens structural protein, bovine β-crystallin, J. Mol. Biol. 157:191–194.

    Article  PubMed  CAS  Google Scholar 

  • Slingsby, C., Driessen, H. P. C., Mahadevan, D., Bax, B., and Blundell, T. L., 1988a, Evolutionary and functional relationships between the basic and acidic β-crystallins, Exp. Eye Res. 46:375–403.

    Article  PubMed  CAS  Google Scholar 

  • Slingsby, C., Driessen, H. P. C., White, H., Mylvaganam, S., Najmudin, S., Bax, B., Bibby, M. A., Lindley, P. F., Moss, D. S., and Blundell, T. L., 1988b, Molecular interactions in relation to cataract, in: Molecular Biology of the Eye: Genes, Vision, and Ocular Disease, (J. Piatigorsky, T. Shinohara, and P. S. Zelenka, eds.), Alan R. Liss, New York, pp. 419–426.

    Google Scholar 

  • Spector, A., 1984, The search for a solution to senile cataracts, Invest. Ophthalmol. Vis. Sci. 25:130–146.

    PubMed  CAS  Google Scholar 

  • Summers, L., Wistow, G., Marebor, M., Moss, D. S., Lindley, P., Slingsby, C., Blundell, T., Bartunik, H., and Bartels, K., 1984, X-ray studies of the lens specific proteins: The crystallins, Peptide Protein Rev. 3:147–168.

    CAS  Google Scholar 

  • Summers, L. J., Slingsby, C., Blundell, T. L., den Dünnen, J. T., Moormann, R. J. M., and Schoenmakers, J. G. G., 1986, Structural variation in mammalian γ-crystallins based on computer graphics analyses of human, rat and calf sequences, Exp. Eye Res. 43:77–92.

    Article  PubMed  CAS  Google Scholar 

  • van Heyningen, R., 1976, Experimental studies on cataract, Invest. Ophthalmol. 15:685–697.

    Google Scholar 

  • White, H. E., Driessen, H. P. C., Slingsby, C., Moss, D. S., and Lindley, P. F., 1989, Packing interactions in the eye-lens: Structural analysis, internal symmetry and lattice interactions of bovine γIVa-crystallin, J. Mol. Biol. 207:217–235.

    Article  PubMed  CAS  Google Scholar 

  • Wistow, G. J., and Piatigorsky, J., 1988, Lens crystallins: The evolution and expression of proteins for a highly specialized tissue, Annu. Rev. Biochem. 57:479–504.

    Article  PubMed  CAS  Google Scholar 

  • Wistow, G., Slingsby, C., Blundell, T, Driessen, H., de Jong, W., and Bloemendal, H., 1981, Eye lens proteins: The three dimensional structure of ß-crystallin predicted from monomelic γ-crystallin, FEBS Lett. 133:9–16.

    Article  PubMed  CAS  Google Scholar 

  • Wistow, G., Turnell, B., Summers, L., Slingsby, C., Moss, D., Miller, L., Lindley, P., and Blundell, T., 1983, X-ray analysis of the eye lens protein γ-II cry stallin at 1.9 Ã… resolution, J. Mol. Biol. 170:175–202.

    Article  PubMed  CAS  Google Scholar 

  • Yu, N.-T, De Nagel, D. C., Pruett, P. L., and Kuck, J. F. R., Jr., 1985, Disulphide bond formation in the eye lens, Proc. Natl. Acad. Sci. U.S.A. 82:207–214.

    Article  Google Scholar 

  • Zigler, J. S., Jr., and Sidbury, J. B. Jr., 1973, Structure of calf lens β-crystallins, Exp. Eye Res. 16:207–214.

    Article  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1991 Springer Science+Business Media New York

About this chapter

Cite this chapter

Slingsby, C. et al. (1991). Molecular Interactions of Crystallins in Relation to Optical Properties. In: Obrecht, G., Stark, L.W. (eds) Presbyopia Research. Perspectives in Vision Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2131-7_5

Download citation

  • DOI: https://doi.org/10.1007/978-1-4757-2131-7_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4419-3217-4

  • Online ISBN: 978-1-4757-2131-7

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics