The cellular basis of corneal transparency: evidence for 'corneal crystallins'

In vivo corneal light scattering measurements using a novel confocal microscope demonstrated greatly increased backscatter from corneal stromal fibrocytes (keratocytes) in opaque compared to transparent corneal tissue in both humans and rabbits. Additionally, two water-soluble proteins, transketolas...

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Bibliographic Details
Published in:	Journal of cell science Vol. 112 ( Pt 5); no. 5; pp. 613 - 622
Main Authors:	Jester, J V, Moller-Pedersen, T, Huang, J, Sax, C M, Kays, W T, Cavangh, H D, Petroll, W M, Piatigorsky, J
Format:	Journal Article
Language:	English
Published:	England 01-03-1999
Subjects:	Aldehyde Dehydrogenase - genetics Aldehyde Dehydrogenase - metabolism Aldehyde Dehydrogenase 1 Family Amino Acid Sequence Animals Base Sequence Cornea - cytology Cornea - metabolism Crystallins - metabolism DNA, Complementary - genetics Eye Injuries - genetics Eye Injuries - metabolism Eye Injuries - pathology Gene Expression Regulation, Enzymologic Humans Isoenzymes - genetics Isoenzymes - metabolism Light Microscopy, Confocal Molecular Sequence Data Rabbits Retinal Dehydrogenase RNA, Messenger - genetics RNA, Messenger - metabolism Scattering, Radiation Transketolase - genetics Transketolase - metabolism
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Summary:	In vivo corneal light scattering measurements using a novel confocal microscope demonstrated greatly increased backscatter from corneal stromal fibrocytes (keratocytes) in opaque compared to transparent corneal tissue in both humans and rabbits. Additionally, two water-soluble proteins, transketolase (TKT) and aldehyde dehydrogenase class 1 (ALDH1), isolated from rabbit keratocytes showed unexpectedly abundant expression ( approximately 30% of the soluble protein) in transparent corneas and markedly reduced levels in opaque scleral fibroblasts or keratocytes from hazy, freeze injured regions of the cornea. Together these data suggest that the relatively high expressions of TKT and ALDH1 contribute to corneal transparency in the rabbit at the cellular level, reminiscent of enzyme-crystallins in the lens. We also note that ALDH1 accumulates in the rabbit corneal epithelial cells, rather than ALDH3 as seen in other mammals, consistent with the taxon-specificity observed among lens enzyme-crystallins. Our results suggest that corneal cells, like lens cells, may preferentially express water-soluble proteins, often enzymes, for controlling their optical properties.
ISSN:	0021-9533 1477-9137
DOI:	10.1242/jcs.112.5.613