Novak U, Harpur A G, Paradiso L, Kanagasundaram V, Jaworowski A, Wilks A F, Hamilton J A
University of Melbourne, Department of Medicine, Royal Melbourne Hospital, Parkville, Australia.
Blood. 1995 Oct 15;86(8):2948-56.
Colony-stimulating factor 1 (CSF-1) causes the activation of STAT1 and STAT3 transcription factors in bone marrow macrophages (BMM), in the macrophage cell line BAC1.2F5, and in fibroblasts that express the wild-type receptor for CSF-1. Fibroblasts expressing a mutant receptor in which the tyrosine 809 is replaced with phenylalanine do not activate STAT proteins in response to CSF-1. The activation of the STAT proteins in BMM is accompanied by tyrosine phosphorylation of Tyk2. In fibroblasts, the activation of the STAT proteins is accompanied by tyrosine phosphorylation of Tyk2 and JAK1. We propose that these JAK kinases are subjected to very rapid phosphorylation in response to CSF-1, followed by rapid dephosphorylation. Furthermore, we propose that kinases other than JAK kinase may be involved in the phosphorylation of the STAT proteins in response to CSF-1.
集落刺激因子1（CSF-1）可导致骨髓巨噬细胞（BMM）、巨噬细胞系BAC1.2F5以及表达CSF-1野生型受体的成纤维细胞中的STAT1和STAT3转录因子激活。表达酪氨酸809被苯丙氨酸取代的突变受体的成纤维细胞，在CSF-1刺激下不会激活STAT蛋白。BMM中STAT蛋白的激活伴随着Tyk2的酪氨酸磷酸化。在成纤维细胞中，STAT蛋白的激活伴随着Tyk2和JAK1的酪氨酸磷酸化。我们认为，这些JAK激酶在CSF-1刺激下会经历非常快速的磷酸化，随后快速去磷酸化。此外，我们认为除JAK激酶外的其他激酶可能参与了CSF-1刺激下STAT蛋白的磷酸化。
