PUBLICATION
Adaptive differences in the structure and macromolecular compositions of the air and water corneas of the "four-eyed" fish (Anableps anableps)
- Authors
- Swamynathan, S.K., Crawford, M.A., Robison, Jr., W.G., Kanungo, J., and Piatigorsky, J.
- ID
- ZDB-PUB-031111-12
- Date
- 2003
- Source
- FASEB journal : official publication of the Federation of American Societies for Experimental Biology 17(14): 1996-2005 (Journal)
- Registered Authors
- Piatigorsky, Joram
- Keywords
- none
- MeSH Terms
-
- Actins/metabolism
- Adaptation, Physiological*
- Air
- Amino Acid Sequence
- Animals
- Cornea/anatomy & histology*
- Cornea/chemistry*
- Cornea/ultrastructure
- Cyprinodontiformes/anatomy & histology*
- Cyprinodontiformes/physiology
- Epithelium, Corneal/chemistry
- Gelsolin/chemistry
- Glycogen/analysis
- Molecular Sequence Data
- Protein Structure, Tertiary
- Proteins/analysis
- Proteins/chemistry
- Solubility
- Water/chemistry
- Zebrafish/anatomy & histology
- PubMed
- 14597669 Full text @ FASEB J.
Citation
Swamynathan, S.K., Crawford, M.A., Robison, Jr., W.G., Kanungo, J., and Piatigorsky, J. (2003) Adaptive differences in the structure and macromolecular compositions of the air and water corneas of the "four-eyed" fish (Anableps anableps). FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 17(14):1996-2005.
Abstract
The water meniscus bisects the eyes of the "four-eyed" fish Anableps anableps, resulting in simultaneous vision in air and water. We compare the structure and macromolecular compositions of the Anableps dorsal (air) and ventral (water) corneas with the fully aquatic zebrafish cornea. The Anableps dorsal corneal epithelium is thicker (>20 cell layers), flatter (approximately 1.94 mm radius of curvature), and contains approximately 15-fold more glycogen (0.16 microg/microg water-soluble protein) than the ventral corneal epithelium (5-7 cell layers; approximately 1.63 mm radius of curvature; 0.01 microg glycogen/microg water-soluble protein), which resembles the zebrafish corneal epithelium. Gelsolin is the major water-soluble protein in the zebrafish (approximately 50%) and Anableps dorsal (approximately 38%) and ventral (approximately 21%) corneal epithelia, suggesting that gelsolin was recruited for high corneal expression before these two species diverged at least 100 million years ago and that abundant corneal gelsolin is not limited to aquatic vision. Anableps gelsolin, deduced from its cDNA, is 57% identical to zebrafish gelsolin. Paucity of Anableps corneal F-actin (consistent with high gelsolin) was confirmed by the absence of rhodamine-phalloidin staining. We suggest amphibious refraction and protection from UV irradiation and desiccation in air as selective constraints for the specializations of the Anableps dorsal cornea.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping