One member of the γ-crystallin gene family, γs, is expressed in birds

Rens, Geert L. M. van; Jong, Wilfried W. de; Bloemendal, H.

doi:10.1016/0014-4835(91)90156-9

Cited by 27 publications

(7 citation statements)

References 9 publications

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“…Chicken lens does not express the γΑ-F crystallin cluster, or this cluster does not exists in the chicken genome. In addition to the γS-crystallin (van Rens et al, 1991), chick lens contains two taxonspecific δ1 and δ2-crystallins. Second, δ1-crystallin appears first in the chick lens placode, followed by β-and αA-crystallin expression during the lens vesicle stage (see Piatigorsky, 1987).…”

Section: Crystallins: Multifunctional Proteins Highly Expressed In Lensmentioning

confidence: 99%

Regulation of gene expression by Pax6 in ocular cells: a case of tissue-preferred expression of crystallins in lens

Cvekl¹,

Yang²,

Chauhan³

et al. 2004

Int. J. Dev. Biol.

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Section: Crystallins: Multifunctional Proteins Highly Expressed In Lensmentioning

confidence: 99%

Regulation of gene expression by Pax6 in ocular cells: a case of tissue-preferred expression of crystallins in lens

Cvekl¹,

Yang²,

Chauhan³

et al. 2004

Int. J. Dev. Biol.

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“…The selective advantage offered by the stability of the GK motif does not seem to have been exploited for the selection of other lens crystallins. Avians do not have any y-crystallins except yS [93], whereas fish have many y-crystallins. Expression of y-crystallins during early embryogenesis and expression of other GK-containing proteins (see 7.6) further suggests that this motif is also associated with proteins in systems requiring rapid turnover.…”

Section: ~/Y-crystallinsmentioning

confidence: 99%

Crystallins, genes and cataract

Bhat¹

2003

Progress in Drug Research

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Far from being a physical entity, assembled of inanimate structural proteins, the ocular lens epitomizes the biological ingenuity that sustains an essential and near-perfect physical system of immaculate optics. Crystallins (a, 13, and y) provide transparency by dint of their high concentration, but it is debatable whether proteins that provide transparency are any different, biologically or structurally, from those that are present in non-transparent structures or tissues. It is becoming increasingly clear that crystallins may have a plethora of metabolic and regulatory functions, both within the lens as well as outside of it. a-Crystallins are members of a small heat shock family of proteins and l3/y-crystallins belong to the family of epidermis-specific differentiation proteins. Crystallin gene expression has been studied from the perspective of the lens specificity of their promoters. Mutations in a-, 13-, and ycrystallins are linked with the phenotype of the loss of transparency. Understanding catalytiC, non-structural properties of crystallins may be critical for understanding the malfunction in molecular cascades that lead to cataractogenesis and its eventual therapeutic amelioration.Crystallins, genes and cataract

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“…The α-and β-crystallins are well conserved in all major vertebrates (Ogino and Yasuda, 2000). Although γ-crystallins are present in mammals, these proteins, except for γS, are absent from avian species (Van Rens et al, 1991). The primary crystallin in the chick is δ-crystallin, a taxonspecific gene similar to argininosuccinate that is expressed only in avian and reptile species.…”

Section: Lens Differentiation and Crystallin Expressionmentioning

confidence: 99%

Lens differentiation and crystallin regulation: a chick model

Reza¹,

Yasuda²

2004

Int. J. Dev. Biol.

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The vertebrate lens is a transparent polarized tissue that acts as the gateway for vision. The chick lens is an excellent model for studying tissue organogenesis, since it is both accessible and easily manipulated during embryonic stages. The chick lens consists of two morphologically discrete compartments, the epithelium and the fiber-cell mass. Evidence indicates that the early phases of lens development involve several sequential events, including tissue interactions, cell proliferation and differentiation. The morphological change during lens development is associated with the concurrent and distinct functions of numerous transcription factors. Diffusible molecules from the complementary neural tissue play vital roles during the entire process of lens development. Lens tissue is characterized by the ample production of crystallins, lens specific proteins which provide structural integrity and functional properties to the lens. Thus, the study of crystallin regulation should provide insight into the development of a functional lens during embryogenesis. This process has been shown to involve a complex and evolutionary conserved pathway supported by different regulatory proteins.

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One member of the γ-crystallin gene family, γs, is expressed in birds

Cited by 27 publications

References 9 publications

Regulation of gene expression by Pax6 in ocular cells: a case of tissue-preferred expression of crystallins in lens

Regulation of gene expression by Pax6 in ocular cells: a case of tissue-preferred expression of crystallins in lens

Crystallins, genes and cataract

Lens differentiation and crystallin regulation: a chick model

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