Characterization of retinal guanylate cyclase‐activating protein 3 (GCAP3) from zebrafish to man

DOI Web Site Web Site 被引用文献1件

抄録

<jats:title>Abstract</jats:title><jats:p>Calmodulin‐like neuronal Ca<jats:sup>2+</jats:sup>‐binding proteins (NCBPs) are expressed primarily in neurons and contain a combination of four functional and nonfunctional EF‐hand Ca<jats:sup>2+</jats:sup>‐binding motifs. The guanylate cyclase‐activating proteins 1–3 (GCAP1–3), the best characterized subgroup of NCBPs, function in the regulation of transmembrane guanylate cyclases 1–2 (GC1–2). The pairing of GCAPs and GCs <jats:italic>in vivo</jats:italic> depends on cell expression. Therefore, we investigated the expression of these genes in retina using <jats:italic>in situ</jats:italic> hybridization and immunocytochemistry. Our results demonstrate that <jats:italic>GCAP1, GCAP2, GC1 and GC2</jats:italic> are expressed in human rod and cone photoreceptors, while <jats:italic>GCAP3</jats:italic> is expressed exclusively in cones. As a consequence of extensive modification, the <jats:italic>GCAP3</jats:italic> gene is not expressed in mouse retina. However, this lack of evolutionary conservation appears to be restricted to only some species as we cloned all three <jats:italic>GCAP</jats:italic>s from teleost (zebrafish) retina and localized them to rod cells, short single cones (<jats:italic>GCAP1–2</jats:italic>), and all subtypes of cones (<jats:italic>GCAP3</jats:italic>). Furthermore, sequence comparisons and evolutionary trace analysis coupled with functional testing of the different GCAPs allowed us to identify the key conserved residues that are critical for GCAP structure and function, and to define class‐specific residues for the NCBP subfamilies.</jats:p>

収録刊行物

被引用文献 (1)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ