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Originally published In Press as doi:10.1074/jbc.M001159200 on May 18, 2000

J. Biol. Chem., Vol. 275, Issue 32, 24645-24652, August 11, 2000
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Evidence for Gelsolin as a Corneal Crystallin in Zebrafish*

Yong-Sheng Xu, Marc KantorowDagger , Janine Davis, and Joram Piatigorsky§

From the Laboratory of Molecular and Developmental Biology, NEI, National Institutes of Health, Bethesda, Maryland 20892-2730

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 ~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.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number AF175294.

Dagger Present address: Dept. of Biology, West Virginia University, Morgantown, WV 26505.

§ To whom correspondence should be addressed: Laboratory of Molecular and Developmental Biology, NEI, NIH, 6 Center Dr., MSC 2730, Bldg. 6/Rm. 201, Bethesda, MD 20892-2730. Tel.: 301-496-9467; Fax: 301-402-0781; E-mail: joramp@intra.nei.nih.gov.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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