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A Splice Variant of Arrestin from Human Retina

https://doi.org/10.1006/exer.1996.0069Get rights and content

Abstract

Retinal arrestin is known to participate in the quenching of phototransduction through binding to light-activated and phosphorylated rhodopsin. Recently, a splice variant of retinal arrestin was identified in bovine photoreceptors which could bind unphosphorylated photoactive rhodopsin. In this report, a splice variant of retinal arrestin is identified in the human retina. The variant of human arrestin is produced by splicing out exon 12, unlike the bovine variant which is produced by splicing out exon 16. This 78bp deletion in the human splice variant produces a polypeptide with a calculated molecular weight of 42.2kDa that lacks 26 amino acids when compared to the full-length retinal arrestin. The use of quantitative competitive PCR indicates that the mRNA for the human splice variant of arrestin is present at approximately one-twentieth of the level of human arrestin mRNA.

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Cited by (10)

  • The role of arrestins in visual and disease processes of the eye

    2013, Progress in Molecular Biology and Translational Science
    Citation Excerpt :

    This arrestin1 variant was demonstrated to be a truncated version of full-length arrestin, formed by replacement of the final exon that coded for 35 amino acids of the arrestin1 C-terminus with an alternative exon that coded for a single alanine residue.29 Investigations in other species showed that splice variants of arrestin1 could also be identified in mouse and human retinas,30,31 although the variation occurred at different splicing sites, resulting in different polypeptides. In all cases, however, the splice variants are present in the retina at approximately 5–10% of the amount of the full-length arrestin1.

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    2011, Investigative Ophthalmology and Visual Science
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