A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors
A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors
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DOI：
10.1074/jbc.272.11.7264
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发表时间：
1997-03-14
影响因子：
4.8
通讯作者：
Lasky, LA
中科院分区：
文献类型：
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作者：
Cheng, J;Wu, K;Lasky, LA
在这里，我们描述了一个新的成员受体样蛋白酪氨酸磷酸酶（PTP）称为PTP λ，这是同源的同型粘附PTP κ和μ。鼠PTP λ含有MAM、IgG、纤连蛋白III型和双磷酸酶结构域。如已经证明的PTP κ和μ，PTP λ介导体外同型粘附，并且PTP λ与肾上皮细胞中的β连环蛋白相关。PTP λ的胞外结构域在细胞培养物中以及在体内被蛋白水解加工。北方印迹分析表明，PTP λ在整个胚胎发育过程中表达，主要存在于成年脑、肺和肾中。对15.5日龄大鼠胚胎的原位杂交显示，PTP λ在多种胚胎神经元部位以及食管、肺细支气管上皮、肾小球上皮、嗅觉上皮和各种软骨部位中表达。新生儿脑的分析表明，PTP λ在海马、皮质和黑质的细胞中表达。最后，免疫组织化学分析揭示了这种PTP在脊髓的特定神经元以及分离的皮质神经元上的表达。
Here we describe a novel member of the receptor-like protein-tyrosine phosphatases (PTPs) termed PTP lambda, which is homologous to the homotypically adherent PTPs kappa and mu. Murine PTP lambda contains MAM, IgG, fibronectin type III, and dual phosphatase domains, As has been demonstrated for PTPs kappa and mu, PTP lambda mediates homotypic adhesion in vitro, and PTP lambda is associated with beta catenin in kidney epithelial cells. The extracellular domain of PTP lambda is proteolytically processed in cell culture as well as in vivo. Northern blot analysis reveals that PTP lambda is expressed throughout embryonic development and is predominately found in adult brain, lung, and kidney. In situ hybridization to 15.5-day old rat embryos reveals that PTP lambda is expressed in a variety of embryonic neuronal sites as well as in the esophagus, lung bronchiolar epithelium, kidney glomerular epithelium, olfactory epithelium, and various cartilagenous sites, Analysis of neonatal brain demonstrates expression in cells of the hippocampus, cortex, and the substantia nigra. Finally, immunohistochemical analysis reveals expression of this PTP on specific neurons of the spinal cord as well as on isolated cortical neurons.