Sandra O, Sohm F, de Luze A, Prunet P, Edery M, Kelly P A
Unité 344, Endocrinologie Moléculaire, Institut National de la Santé.
Proc Natl Acad Sci U S A. 1995 Jun 20;92(13):6037-41. doi: 10.1073/pnas.92.13.6037.
By using an expression cloning strategy, we isolated a single positive clone encoding a tilapia prolactin (PRL) receptor. Tilapia PRL188 was used to screen a freshwater tilapia kidney expression library transfected in COS cells. The tilapia PRL receptor is a mature protein of 606 amino acids. The extracellular domain is devoid of the tandem repeat units present in birds and has two pairs of cysteine residues, a Trp-Ser-Xaa-Trp-Ser motif, and two potential N-glycosylation sites. The cytoplasmic domain contains 372 amino acids, including box 1, a sequence previously shown to be important for signal transduction in mammalian species. Thus, the general structure is similar to the long form of mammalian PRL receptors; however, amino acid comparisons reveal a rather low identity (approximately 37%). Northern blot analysis shows the existence of a single transcript in osmoregulatory tissues and reproductive organs. This localization is in agreement with known functions of PRL in teleosts.
通过使用表达克隆策略，我们分离出了一个编码罗非鱼催乳素（PRL）受体的单一阳性克隆。利用罗非鱼PRL188筛选转染到COS细胞中的淡水罗非鱼肾脏表达文库。罗非鱼PRL受体是一种由606个氨基酸组成的成熟蛋白。其胞外结构域没有鸟类中存在的串联重复单元，有两对半胱氨酸残基、一个色氨酸 - 丝氨酸 - Xaa - 色氨酸 - 丝氨酸基序以及两个潜在的N - 糖基化位点。胞质结构域包含372个氨基酸，包括框1，该序列先前已证明对哺乳动物物种的信号转导很重要。因此，其总体结构与哺乳动物PRL受体的长形式相似；然而，氨基酸比较显示同源性相当低（约37%）。Northern印迹分析表明在渗透调节组织和生殖器官中存在单一转录本。这种定位与硬骨鱼中PRL的已知功能一致。
