Garbati Michael R, Welgan Catherine A, Landefeld Sally H, Newell Laura F, Agarwal Anupriya, Dunlap Jennifer B, Chourasia Tapan K, Lee Hyunjung, Elferich Johannes, Traer Elie, Rattray Rogan, Cascio Michael J, Press Richard D, Bagby Grover C, Tyner Jeffrey W, Druker Brian J, Dao Kim-Hien T
Knight Cancer Institute, Hematology and Medical Oncology, Oregon Health and Science University, Portland, Oregon.
Knight Cancer Institute, Oregon Health and Science University, Portland, Oregon.
Am J Hematol. 2016 Feb;91(2):211-9. doi: 10.1002/ajh.24245.
Mutations in the calreticulin gene (CALR) were recently identified in approximately 70-80% of patients with JAK2-V617F-negative essential thrombocytosis and primary myelofibrosis. All frameshift mutations generate a recurring novel C-terminus. Here we provide evidence that mutant calreticulin does not accumulate efficiently in cells and is abnormally enriched in the nucleus and extracellular space compared to wildtype calreticulin. The main determinant of these findings is the loss of the calcium-binding and KDEL domains. Expression of type I mutant CALR in Ba/F3 cells confers minimal IL-3-independent growth. Interestingly, expression of type I and type II mutant CALR in a nonhematopoietic cell line does not directly activate JAK/STAT signaling compared to wildtype CALR and JAK2-V617F expression. These results led us to investigate paracrine mechanisms of JAK/STAT activation. Here we show that conditioned media from cells expressing type I mutant CALR exaggerate cytokine production from normal monocytes with or without treatment with a toll-like receptor agonist. These effects are not dependent on the novel C-terminus. These studies offer novel insights into the mechanism of JAK/STAT activation in patients with JAK2-V617F-negative essential thrombocytosis and primary myelofibrosis.
钙网蛋白基因(CALR)突变最近在约70 - 80%的JAK2 - V617F阴性原发性血小板增多症和原发性骨髓纤维化患者中被发现。所有移码突变都会产生一个重复出现的新C末端。在此我们提供证据表明,与野生型钙网蛋白相比,突变型钙网蛋白在细胞内不能有效积累,并且在细胞核和细胞外空间异常富集。这些发现的主要决定因素是钙结合域和KDEL域的缺失。I型突变CALR在Ba/F3细胞中的表达赋予了最小程度的白细胞介素-3非依赖性生长。有趣的是,与野生型CALR和JAK2 - V617F的表达相比,I型和II型突变CALR在非造血细胞系中的表达不会直接激活JAK/STAT信号通路。这些结果促使我们研究JAK/STAT激活的旁分泌机制。在此我们表明,来自表达I型突变CALR细胞的条件培养基,无论是否用Toll样受体激动剂处理,都会夸大正常单核细胞的细胞因子产生。这些效应不依赖于新的C末端。这些研究为JAK2 - V617F阴性原发性血小板增多症和原发性骨髓纤维化患者中JAK/STAT激活的机制提供了新的见解。