Piatigorsky J
Laboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892-2730, USA.
Prog Retin Eye Res. 1998 Apr;17(2):145-74. doi: 10.1016/s1350-9462(97)00004-9.
The major water-soluble proteins (crystallins) responsible for the optical properties of the cellular lenses of vertebrates and invertebrates are surprisingly diverse and often differ among species (i.e., are taxon-specific). Many crystallins are encoded by the identical gene specifying a stress protein or a metabolic enzyme which has non-refractive functions in numerous tissues. This double use of a distinct protein has been called gene sharing. Abundant expression of various metabolic enzymes also occurs in a taxon-specific manner in corneal epithelial cells, suggesting that gene sharing extends to this transparent tissue. It has been proposed that one of the most abundant corneal enzymes (aldehyde dehydrogenase class 3) may protect the eye by directly absorbing ultraviolet light, as well as by providing an enzymatic function. It also seems possible that the high expression of corneal enzymes (5-40% of the water-soluble proteins) may reduce scattering in the corneal epithelium by minimizing spatial fluctuations in refractive index as they do in the lens. Thus, gene sharing may be a widespread phenomenon encompassing the lens, cornea and probably other systems. Lens-preferred expression of crystallin genes is integrated in a complex developmental program utilizing in many cases Pax-6. The differential expression of alpha B-crystallin (a small heat shock protein) in different tissues involves the combinatorial use of both shared and lens-specific cis-control elements. Corneal-preferred gene expression appears to depend in part on induction by environmental influences. Among the implications of gene sharing are that gene duplication is not required for the evolution of a new protein phenotype, a change in gene regulation is sufficient, that proteins may be under more than one selective constraint, affecting their evolutionary clock, and that it would be prudent to consider the possibility that any given gene may have important, unrecognized roles when planning to implement gene therapy in the future.
负责脊椎动物和无脊椎动物细胞晶状体光学特性的主要水溶性蛋白质(晶状体蛋白)惊人地多样,且常常因物种而异(即具有分类群特异性)。许多晶状体蛋白由同一个基因编码,该基因指定一种应激蛋白或一种代谢酶,这些蛋白或酶在许多组织中具有非屈光功能。这种对一种独特蛋白质的双重利用被称为基因共享。各种代谢酶在角膜上皮细胞中也以分类群特异性的方式大量表达,这表明基因共享也延伸到了这个透明组织。有人提出,角膜中最丰富的酶之一(3类醛脱氢酶)可能通过直接吸收紫外线以及提供酶促功能来保护眼睛。角膜酶的高表达(占水溶性蛋白质的5 - 40%)也有可能像在晶状体中那样,通过最小化折射率的空间波动来减少角膜上皮中的散射。因此,基因共享可能是一种广泛存在的现象,涵盖晶状体、角膜以及可能的其他系统。晶状体蛋白基因在晶状体中的优先表达整合在一个复杂的发育程序中,在许多情况下利用了Pax - 6。αB -晶状体蛋白(一种小分子热休克蛋白)在不同组织中的差异表达涉及共享的和晶状体特异性的顺式调控元件的组合使用。角膜优先的基因表达似乎部分取决于环境影响的诱导。基因共享的影响包括,新蛋白质表型的进化不需要基因复制,基因调控的改变就足够了;蛋白质可能受到不止一种选择约束,从而影响其进化时钟;并且在未来计划实施基因治疗时,谨慎考虑任何给定基因可能具有重要的、未被认识到的作用这一可能性是明智的。