PUBLICATION
Evidence for gelsolin as a corneal crystallin in zebrafish
- Authors
- Xu, Y.S., Kantorow, M., Davis, J., and Piatigorsky, J.
- ID
- ZDB-PUB-000824-8
- Date
- 2000
- Source
- The Journal of biological chemistry 275(32): 24645-24652 (Journal)
- Registered Authors
- Piatigorsky, Joram
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- Cloning, Molecular
- Cornea/cytology
- Cornea/physiology
- Crystallins/analysis
- Crystallins/chemistry*
- Crystallins/genetics
- Epithelium, Corneal/cytology
- Epithelium, Corneal/physiology*
- Fishes
- Gelsolin/analysis
- Gelsolin/chemistry*
- Gelsolin/genetics*
- Humans
- Immunohistochemistry
- Mice
- Molecular Sequence Data
- RNA, Messenger
- Sequence Alignment
- Sequence Homology, Amino Acid
- Sharks
- Transcription, Genetic
- Zebrafish
- PubMed
- 10818094 Full text @ J. Biol. Chem.
Citation
Xu, Y.S., Kantorow, M., Davis, J., and Piatigorsky, J. (2000) Evidence for gelsolin as a corneal crystallin in zebrafish. The Journal of biological chemistry. 275(32):24645-24652.
Abstract
We have shown that gelsolin is one of the most prevalent water-soluble proteins in the transparent cornea of zebrafish. There are also significant amounts of actin. In contrast to actin, gelsolin is barely detectable in other eye tissues (iris, lens, and remaining eye) of the zebrafish. Gelsolin cDNA hybridized intensely in Northern blots to RNA from the cornea but not from the lens, brain, or headless body. The deduced zebrafish gelsolin is approximately 60% identical to mammalian cytosolic gelsolin and has the characteristic six segmental repeats as well as the binding sites for actin, calcium, and phosphatidylinositides. In situ hybridization tests showed that gelsolin mRNA is concentrated in the zebrafish corneal epithelium. The zebrafish corneal epithelium stains very weakly with rhodamine-phalloidin, indicating little F-actin in the cytoplasm. In contrast, the mouse corneal epithelium contains relatively little gelsolin and stains intensely with rhodamine-phalloidin, as does the zebrafish extraocular muscle. We propose, by analogy with the diverse crystallins of the eye lens and with the putative enzyme-crystallins (aldehyde dehydrogenase class 3 and other enzymes) of the mammalian cornea, that gelsolin and actin-gelsolin complexes act as water-soluble crystallins in the zebrafish cornea and contribute to its optical properties.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping