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Rensselaer Polytechnic Institute Department of Biological Sciences
Biology Faculty
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Department of Biological Sciences
1W14 Jonsson-Rowland Science Center
Rensselaer Polytechnic Institute
110 Eighth Street
Troy, NY 12180-3590

Phone: (518) 276-6446
Fax: (518) 276-2344

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Biology Home Undergraduate Graduate Faculty Research News and Events Contacts
Jane Koretz

Professor Emerita of Biology

Education and Training

Jane Koretz received her B.A. with high honors from Swarthmore College, and her Ph.D. in biophysics from The University of Chicago for her work on skeletal muscle myosin ATPase with Edwin W. Taylor. She was a Muscular Dystrophy Association post-doctoral fellow at the MRC Cell Biophysics Unit, King’s College, London, before joining the faculty at Rensselaer, the recipient of a Fulbright for her sabbatical work at the Nuffield Laboratory of Ophthalmology (University of Oxford), and a senior awardee of the Ruth L. Kirschstein National Research Service Award from NIH.

Contact

E-mail: koretj3@rpi.edu

Rensselaer Polytechnic Institute
110 8th Street
Troy, NY 12180

Research Interests

Modeling the human visual process.
The young human eye is capable of focusing from infinity to the tip of one’s nose, a multifactorial process termed accommodation that involves changing the shape and thickness of the eye’s lens. As people grow older, their ability to focus on near objects gradually diminishes, eventually leading to the need for reading glasses (presbyopia). Changes in the lens and surrounding tissues with age have been implicated in presbyopia. At the same time, the lens grows less transparent, which may ultimately lead to cataracts. As a result, understanding the aging of human vision involves understanding aging processes ranging in scale from the tissue level down to the molecular level. A key factor in lens clarity and refractive power is its protein composition. Mammalian lenses contain unusual proteins, termed crystallins, that contribute to the ability of the lens to refract light for focus on the retina while maintaining lens transparency at extremely high concentrations over a lifetime. The major lens protein is alpha-crystallin, which is assigned to the small heat shock protein family because of its highly conserved core structure. It may contribute to maintenance of lens clarity and transparency by binding damaged or denaturing proteins before they can aggregate into light-scattering clusters, but is itself affected by age-dependent modifications.

The lens grows throughout life, increasing in size and mass, and it is highly likely that this contributes to diminution in focusing range with age. However, it is also believed by some that the lens, in whole or part, also becomes more sclerotic, resistant to the changes in shape and curvature necessary for focus with increasing age. Others have suggested that there is a change in the capability of the ciliary muscle controlling lens shape to effectively act on the lens, or a change in the properties of other tissues associated with focusing. We have developed an analytical model of the focusing process that allows us to address some of these issues, using data about changes in lens shape and other factors, and are working to make it increasingly reflective of what is known about accommodation and aging in the human eye.

Selected Publications

Koretz, J. F., Cook, C. A., Kaufman, P. L. Aging of the human lens: changes in lens shape at zero-diopter accommodation. J Opt Soc Am A Opt Image Sci Vis 18:265-72. [2001].

Koretz, J. F. and Cook, C. A.  Aging of the optics of the human eye:  lens refraction models and principal plane locations.  Optom. and Vis. Sci. (special issue on the aging eye), 78:396-404 [2001].

Burgio, M. R., Bennett, P.M., and Koretz, J.F.  Heat-induced quaternary transitions in hetero- and homo-polymers of  alpha-crystallin.  Mol. Vis., 7:228-233 [2001].

Koretz, J.F., Cook, C. A. and Kaufman, P. L.  Aging of the human lens:  changes in lens shape at zero diopters accommodation. J Opt Soc Am A Opt Image Sci Vis. 19(1):144-51 [2002]

Salerno, J. C., Salerno, K. M., Eifert, C.J.and Koretz, J. F.   Structural diversity in the small heat shock protein superfamily:  Control of aggregation by the N-terminal region.  Prot. Eng., 16(11): 847-51 [2003].

Koretz, J.F. “A system for accommodative stimulation of an eye and simultaneous ipsilateral accommodative imaging. “ Patent #7070276  (2003).

Koretz JF, Strenk SA, Strenk LM, Semmlow JL.  Scheimpflug and high-resolution magnetic resonance imaging of the anterior segment: a comparative study.  J Opt Soc Am A Opt Image Sci Vis. Mar;21(3):346-54 [2004].

Regini JW, Grossmann JG, Burgio MR, Malik NS, Koretz JF, Hodson SA, Elliott GF.  Structural changes in alpha-crystallin and whole eye lens during heating, observed by low-angle X-ray diffraction.  J Mol Biol. Mar 5;336(5):1185-94 [2004].

Strenk SA, Strenk LM, Koretz JF. The mechanism of presbyopia.  Prog Retin Eye Res. May;24(3):379-93 [2005]..

Eifert C, Burgio MR, Bennett PM, Salerno JC, Koretz JF.  N-terminal control of small heat shock protein oligomerization: changes in aggregate size and chaperone-like function. Biochim Biophys Acta. May 15;1748(2):146-56 [2005].

Yang C, Salerno JC, Koretz JF.  NH2-terminal stabilization of small heat shock protein structure: a comparison of two NH2-terminal deletion mutants of alphaA-crystallin. Mol Vis. 11:641-7 [2005].

Li, Ying K., K. R. Schmitz,  J. C. Salerno, and J. F. Koretz. The role of the conserved C-terminal triad in alpha-crystallin aggregation and functionality.  Mol. Vis.,  13:1758-1768 [2007].

Koretz, J.F. “Presbyopia”. Chapter 34 in Ocular Disease: Mechanisms and Management (ed. L.A. Levin and D.M. Albert). New York: Elsevier (2009)
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