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Expression of the duck α‐enolase/τ‐crystallin gene in transgenic mice
Author(s) -
Kim Robert Y.,
Wistow Graeme J.
Publication year - 1993
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.7.5.8462788
Subject(s) - enolase , crystallin , transgene , genetically modified mouse , gene , biology , microbiology and biotechnology , gene expression , genetics , immunohistochemistry , immunology
In many vertebrates, metabolic enzymes have been directly recruited to an additional structural role as crystallins in the eye lens. In some species the glycolytic enzyme α‐enolase (αENO) attains high concentrations in the lens, as τ‐crystallin (τCRY). A line of transgenic mice was constructed containing the entire duck α ENO /τ CRY gene with 5′‐ and 3′‐flanking regions and all introns. Full‐sized duck αENO mRNA was expressed in the transgenic mice with the same pattern as the endogenous mouse αENO isozyme. Although there was no evidence for tissue preference, the concentration of enolase increased markedly in transgenic lens as well as in other tissues. In spite of this, transgenic lenses were transparent and the animals were normal in appearance. The increase in enolase levels in the transgenic lens mimics the stepped increase that might occur in the early stages of enzyme crystallin recruitment. These results demonstrate that lens transparency is sufficiently robust to be refractory to some increase in metabolic enzyme concentration without the need for compensatory adaptation.— Kim, R. Y.; Wistow, G. J. Expression of the duck α‐enolase/τ‐crystallin gene in transgenic mice. FASEB J. 7: 464‐469; 1993.