TY - JOUR
T1 - The cellular basis of corneal transparency
T2 - Evidence for 'corneal crystallins'
AU - Jester, James V.
AU - Moller-Pedersen, Torben
AU - Huang, Jiying
AU - Sax, Christina M.
AU - Kays, Wm Todd
AU - Cavangh, H. Dwight
AU - Petroll, W. Matthew
AU - Piatigorsky, Joram
PY - 1999
Y1 - 1999
N2 - 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 (~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.
AB - 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 (~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.
KW - Aldehyde dehydrogenase class 1
KW - Corneal transparency
KW - Crystallin
KW - Keratocyte
KW - Transketolase
UR - http://www.scopus.com/inward/record.url?scp=0033000285&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033000285&partnerID=8YFLogxK
M3 - Article
C2 - 9973596
AN - SCOPUS:0033000285
SN - 0021-9533
VL - 112
SP - 613
EP - 622
JO - The Quarterly journal of microscopical science
JF - The Quarterly journal of microscopical science
IS - 5
ER -