期刊
DEVELOPMENTAL DYNAMICS
卷 239, 期 10, 页码 2700-2713出版社
WILEY-BLACKWELL
DOI: 10.1002/dvdy.22392
关键词
retinal development; photoreceptor differentiation; thyroid hormone; thyroid hormone receptor; opsin expression; cone; rod; in situ hybridization; immunohistochemistry; fish
资金
- NSERC
Thyroid hormone and its receptors (TRs) regulate photoreceptor differentiation and visual pigment protein (opsin) expression in the retinas of several vertebrates, including rodents and fish. In some of these animals, opsin expression can arise through switches within differentiated cone photoreceptors. In salmonid fishes, single cones express ultraviolet (SWS1) opsin during embryonic development and switch to blue (SWS2) opsin as the fishes grow. It is unknown whether thyroid hormone regulates opsin expression during early cone differentiation and acts through TRs to induce opsin switches in differentiated cones of the salmonid retina. Using in situ hybridization, we characterized the spatiotemporal dynamics of opsin expression and switching in embryos treated with exogenous thyroid hormone or propylthiouracil (PTU), a pharmacological inhibitor of thyroid hormone synthesis. We combined immunohistochemistry with in situ hybridization to map TR alpha expression with respect to cones undergoing the opsin switch in older juvenile fish. Thyroid hormone accelerated opsin expression in differentiating cones and induced the opsin switch in differentiated single cones, whereas PTU repressed the opsin switch. TR alpha was not detected in differentiating photoreceptors as opsin expression initiated, but was later expressed in differentiated single cones before the onset of the opsin switch. TR alpha expression exhibited a dynamic dorsoventral distribution that paralleled the progression of the opsin switch. Together, our results show that thyroid hormone is required for opsin switching in the retina of salmonid fishes and suggest that TR alpha may be involved in regulating this phenomenon. Developmental Dynamics 239:2700-2713, 2010. (C) 2010 Wiley-Liss, Inc.
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