Transcriptional Control of the α-Crystallin Gene Family

  • Ana B. Chepelinsky
  • Eric F. Wawrousek
  • Robert A. Dubin
  • Cynthia J. Jaworski
  • Joan B. McDermott
  • Joram Piatigorsky
Part of the Perspectives in Vision Research book series (PIVR)


Crystallina constitute 80–90% of the soluble protein of the ocular lens. There are a surprisingly large number of crystallin gene families; some (α- and ßγ-crystallins) are present in all vertebrate lenses, whereas others (the enzyme-crystallins) are found only in the lenses of certain species. The enzyme-crystallins are not lens-specific and appear to have a double function, i.e., as structural proteins in the lens and as metabolic enzymes in other tissues (see Wistow and Piatigorsky, 1988; Piatigorsky and Wistow, 1989). In addition to their lens-specific or lens-preferred expression, the synthesis of the crystallin polypeptides is developmentally regulated in a temporal and spatial manner in the lens (see McAvoy, 1981; Piatigorsky, 1981).


Transgenic Mouse Hybrid Gene Small Heat Shock Protein Transient Assay Mouse Lens 
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Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • Ana B. Chepelinsky
    • 1
  • Eric F. Wawrousek
    • 1
  • Robert A. Dubin
    • 1
  • Cynthia J. Jaworski
    • 1
  • Joan B. McDermott
    • 1
  • Joram Piatigorsky
    • 1
  1. 1.Laboratory of Molecular and Developmental Biology, National Eye InstituteNational Institutes of HealthBethesdaUSA

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