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Rac1 links integrin-mediated adhesion to the control of lactational differentiation in mammary epithelia
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The expression of tissue-specific genes during mammary gland differentiation relies on the coincidence of two distinct signaling events: the continued engagement of beta1 integrins with the extracellular matrix (ECM) and a hormonal stimulus from prolactin (Prl). How the integrin and Prl receptor (PrlR) systems integrate to regulate milk protein gene synthesis is unknown. In this study, we identify Rac1 as a key link. Dominant-negative Rac1 prevents Prl-induced synthesis of the milk protein beta-casein in primary mammary epithelial cells cultured as three-dimensional acini on basement membrane. Conversely, activated Rac1 rescues the defective beta-casein synthesis that occurs under conditions not normally permissive for mammary differentiation, either in beta1 integrin-null cells or in wild-type cells cultured on collagen. Rac1 is required downstream of integrins for activation of the PrlR/Stat5 signaling cascade. Cdc42 is also necessary for milk protein synthesis but functions via a distinct mechanism to Rac1. This study identifies the integration of signals provided by ECM and hormones as a novel role for Rho family guanosine triphosphatases. 相似文献
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Sen Zhang Hao Qi Xue-Peng Wen Ping Li Xue-Jun Gao Jin-Xia Ao 《Journal of cellular physiology》2019,234(5):6077-6090
Tudor staphylococcal nuclease (Tudor-SN) is a multifunctional protein involved in a variety of cellular processes and plays a critical role in the regulation of gene expression. Recently, Tudor-SN was found to be upregulated in mammary epithelial cells during lactation in response to prolactin, which further to regulate milk protein synthesis. However, the detailed regulatory mechanism of Tudor-SN to milk protein still remains to be elucidated. In our study, we observed that the levels of Tudor-SN and phosphor-Tudor-SN (Thr103) were both enhanced upon prolactin stimulation. Immunofluorescence assays demonstrated that prolactin treatment facilitated the nuclear transport of Tudor-SN. Further study revealed that the phosphorylation of Tudor-SN was depended on activated JNK. Coimmunoprecipitation assays disclosed that Tudor-SN might be phosphorylated directly by JNK. Using gene mutation assays, we further discovered that mutation of Thr to Ala at site of 103 prevented the nuclear transport of Tudor-SN. Thus, these results suggested the essential mechanism of the activated Tudor-SN in milk protein regulation in response to prolactin, which may provide some new sights into improve milk protein production. 相似文献
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Signal transducer and activator of transcription (Stat) 5 controls the proliferation and differentiation of mammary alveolar epithelium. 总被引:12,自引:0,他引:12
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Keiko Miyoshi Jonathan M. Shillingford Gilbert H. Smith Sandra L. Grimm Kay-Uwe Wagner Takami Oka Jeffrey M. Rosen Gertraud W. Robinson Lothar Hennighausen 《The Journal of cell biology》2001,155(4):531-542
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A novel approach identified the FOLR1 gene, a putative regulator of milk protein synthesis 总被引:1,自引:0,他引:1
Karensa K. Menzies Christophe Lefèvre Julie A. Sharp Keith L. Macmillan Paul A. Sheehy Kevin R. Nicholas 《Mammalian genome》2009,20(8):498-503
This study has utilised comparative functional genomics to exploit animal models with extreme adaptation to lactation to identify
candidate genes that specifically regulate protein synthesis in the cow mammary gland. Increasing milk protein production
is valuable to the dairy industry. The lactation strategies of both the Cape fur seal (Artocephalus pusillus pusillus) and the tammar wallaby (Macropus eugenii) include periods of high rates of milk protein synthesis during an established lactation and therefore offer unique models
to target genes that specifically regulate milk protein synthesis. Global changes in mammary gene expression in the Cape fur
seal, tammar wallaby, and the cow (Bos taurus) were assessed using microarray analysis. The folate receptor α (FOLR1) showed the greatest change in gene expression in
all three species [cow 12.7-fold (n = 3), fur seal 15.4-fold (n = 1), tammar 2.4-fold (n = 4)] at periods of increased milk protein production. This compliments previous reports that folate is important for milk
protein synthesis and suggests FOLR1 may be a key regulatory point of folate metabolism for milk protein synthesis within
mammary epithelial cells (lactocytes). These data may have important implications for the dairy industry to develop strategies
to increase milk protein production in cows. This study illustrates the potential of comparative genomics to target genes
of interest to the scientific community. 相似文献