Differential in vitro and in vivo glycosylation of human erythropoietin expressed in adenovirally transduced mouse mammary epithelial cells

2005 ◽  
Vol 1726 (1) ◽  
pp. 48-56 ◽  
Author(s):  
Jorge R. Toledo ◽  
Oliberto Sánchez ◽  
Raquel Montesino Seguí ◽  
Yaiza Fernández García ◽  
María P. Rodríguez ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Human Erythropoietin

scholarly journals A Dual Role for Oncostatin M Signaling in the Differentiation and Death of Mammary Epithelial Cells in Vivo

2008 ◽  
Vol 22 (12) ◽  
pp. 2677-2688 ◽  
Author(s):  
Paul G. Tiffen ◽  
Nader Omidvar ◽  
Nuria Marquez-Almuina ◽  
Dawn Croston ◽  
Christine J. Watson ◽  
...  
Keyword(s):  
Gene Expression ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Oncostatin M ◽  
Specific Gene ◽  
Mammary Involution

Abstract Recent studies in breast cancer cell lines have shown that oncostatin M (OSM) not only inhibits proliferation but also promotes cell detachment and enhances cell motility. In this study, we have looked at the role of OSM signaling in nontransformed mouse mammary epithelial cells in vitro using the KIM-2 mammary epithelial cell line and in vivo using OSM receptor (OSMR)-deficient mice. OSM and its receptor were up-regulated approximately 2 d after the onset of postlactational mammary regression, in response to leukemia inhibitory factor (LIF)-induced signal transducer and activator of transcription-3 (STAT3). This resulted in sustained STAT3 activity, increased epithelial apoptosis, and enhanced clearance of epithelial structures during the remodeling phase of mammary involution. Concurrently, OSM signaling precipitated the dephosphorylation of STAT5 and repressed expression of the milk protein genes β-casein and whey acidic protein (WAP). Similarly, during pregnancy, OSM signaling suppressed β-casein and WAP gene expression. In vitro, OSM but not LIF persistently down-regulated phosphorylated (p)-STAT5, even in the continued presence of prolactin. OSM also promoted the expression of metalloproteinases MMP3, MMP12, and MMP14, which, in vitro, were responsible for OSM-specific apoptosis. Thus, the sequential activation of IL-6-related cytokines during mammary involution culminates in an OSM-dependent repression of epithelial-specific gene expression and the potentiation of epithelial cell extinction mediated, at least in part, by the reciprocal regulation of p-STAT5 and p-STAT3.

scholarly journals Regulatory function of whey acidic protein in the proliferation of mouse mammary epithelial cells in vivo and in vitro

2004 ◽  
Vol 274 (1) ◽  
pp. 31-44 ◽  
Author(s):  
Naoko Nukumi ◽  
Kayoko Ikeda ◽  
Megumi Osawa ◽  
Tokuko Iwamori ◽  
Kunihiko Naito ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Whey Acidic Protein ◽  
Mammary Epithelial ◽  
Acidic Protein ◽  
Regulatory Function

Menthol from Mentha piperita Suppresses the Milk Production of Lactating Mammary Epithelial Cells In Vivo and In Vitro

2020 ◽  
Vol 64 (24) ◽  
pp. 2000853
Author(s):  
Norihiro Suzuki ◽  
Yusaku Tsugami ◽  
Haruka Wakasa ◽  
Takahiro Suzuki ◽  
Takanori Nishimura ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Milk Production ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Mentha Piperita

Adenoviral-mediated gene transfer into primary human and mouse mammary epithelial cells in vitro and in vivo

1995 ◽  
Vol 98 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Jason Yang ◽  
Tetsuya Tsukamoto ◽  
Nikolay Popnikolov ◽  
Raphael C. Guzman ◽  
Xiaoyan Chen ◽  
...  
Keyword(s):  
Gene Transfer ◽  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Human And Mouse

cAMP levels in proliferating rat mammary epithelial cells in vitro and in vivo

1989 ◽  
Vol 182 (2) ◽  
pp. 653-658 ◽  
Author(s):  
Stephen P. Ethier ◽  
Rochelle M. Van De Velde ◽  
Kimberly C. Cundiff
Keyword(s):  
Epithelial Cells ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Camp Levels

scholarly journals UFM1-Specific Ligase 1 Ligating Enzyme 1 Mediates Milk Protein and Fat Synthesis-Related Gene Expression via the JNK Signaling Pathway in Mouse Mammary Epithelial Cells

2020 ◽  
Vol 2020 ◽  
pp. 1-14 ◽  
Author(s):  
Meiqian Kuang ◽  
Min Yang ◽  
Lian Li ◽  
Chengmin Li ◽  
Genlin Wang
Keyword(s):  
Protein Synthesis ◽  
Epithelial Cells ◽  
Milk Fat ◽  
Milk Protein ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Fat Synthesis ◽  
Jnk Activation

Ubiquitin-like modifier 1 ligating enzyme 1 (UFL1) has been characterized as a ubiquitin-like (Ubl) protein that affects a range of cellular processes across various pathways. In this study, mouse mammary epithelial cells (HC11 cell line) and UFL1 knockout (KO) mice were used to establish UFL1 knockdown models to explore the influence of UFL1 on milk protein and fat synthesis in the mouse mammary gland and the underlying mechanisms. This is the first study to show UFL1 localization in mouse mammary epithelial cells. UFL1 depletion by transfected UFL1 siRNA (siUFL1) caused aggravated apoptosis. In addition, UFL1 depletion suppressed milk protein synthesis-related protein level in vivo and in vitro. Conversely, ACACA and FASN expressions increased in UFL1-deficient mice. Moreover, UFL1 depletion increased triglyceride synthesis levels and inhibited the p-JNK expression. Importantly, the expression of proteins related to milk protein synthesis was decreased in JNK- and UFL1-deficient cells, whereas proteins related to milk fat synthesis showed the opposite trend, indicating that UFL1 affects milk protein and fat synthesis via the suppression of JNK activation. Overall, our findings indicate that UFL1 plays a key role in mammary milk and fat synthesis via JNK activation.

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