Schepens J, Zeeuwen P, Wieringa B, Hendriks W
Department of Cell Biology & Histology, University of Nijmegen, The Netherlands.
Mol Biol Rep. 1992 Sep;16(4):241-8. doi: 10.1007/BF00419663.
Protein-tyrosine phosphatases (PTPases) form a novel and important class of cell regulatory proteins. We evaluated the expression of PTPases in mouse brain by polymerase chain amplification of cDNA segments that encode the catalytic domains of these enzymes. Degenerate primer pairs devised on the basis of conserved protein motifs were used to generate a series of distinct PCR-derived clones. In this way, murine homologues of the human PTPases LRP, PTP beta, PTP delta, PTP epsilon and LAR were obtained. Corresponding regions in their catalytic domains were used to reveal the evolutionary relationships between all currently known mammalian PTPase protein family members. Phylogenetic reconstruction displayed considerable differences in mutation rates for closely related PTPases.
蛋白酪氨酸磷酸酶（PTPases）构成了一类新型且重要的细胞调节蛋白。我们通过对编码这些酶催化结构域的cDNA片段进行聚合酶链扩增，来评估PTPases在小鼠脑中的表达。基于保守蛋白基序设计的简并引物对，用于生成一系列不同的PCR衍生克隆。通过这种方式，获得了人类PTPases LRP、PTPβ、PTPδ、PTPε和LAR的小鼠同源物。利用它们催化结构域中的相应区域，来揭示所有目前已知的哺乳动物PTPase蛋白家族成员之间的进化关系。系统发育重建显示，亲缘关系较近的PTPases在突变率上存在显著差异。
