Changes of endoplasmic reticulum and mitochondria in mammary epithelial cells during mammogenesis in Chinese Holstein dairy cows

2012 ◽  
Vol 114 (5) ◽  
pp. 448-453 ◽  
Author(s):  
Bo Qu ◽  
Yujun Jiang ◽  
Feng Zhao ◽  
Jianhua Xiao ◽  
Qing Zhang Li
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Dairy Cows ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Chinese Holstein ◽  
Holstein Dairy Cows

scholarly journals Chemerin Regulates Epithelial Barrier Function of Mammary Glands in Dairy Cows

Animals ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 3194
Author(s):  
Yutaka Suzuki ◽  
Sachi Chiba ◽  
Koki Nishihara ◽  
Keiichi Nakajima ◽  
Akihiko Hagino ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Epithelial Cell ◽  
Epithelial Cells ◽  
Dairy Cows ◽  
Barrier Function ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Epithelial Barrier ◽  
Epithelial Tissue ◽  
Epithelial Barrier Function

Epithelial barrier function in the mammary gland acts as a forefront of the defense mechanism against mastitis, which is widespread and a major disorder in dairy production. Chemerin is a chemoattractant protein with potent antimicrobial ability, but its role in the mammary gland remains unelucidated. The aim of this study was to determine the function of chemerin in mammary epithelial tissue of dairy cows in lactation or dry-off periods. Mammary epithelial cells produced chemerin protein, and secreted chemerin was detected in milk samples. Chemerin treatment promoted the proliferation of cultured bovine mammary epithelial cells and protected the integrity of the epithelial cell layer from hydrogen peroxide (H2O2)-induced damage. Meanwhile, chemerin levels were higher in mammary tissue with mastitis. Tumor necrosis factor alpha (TNF-α) strongly upregulated the expression of the chemerin-coding gene (RARRES2) in mammary epithelial cells. Therefore, chemerin was suggested to support mammary epithelial cell growth and epithelial barrier function and to be regulated by inflammatory stimuli. Our results may indicate chemerin as a novel therapeutic target for diseases in the bovine mammary gland.

scholarly journals MiR-125b regulates inflammation in bovine mammary epithelial cells by targeting the NKIRAS2 gene

2021 ◽  
Vol 52 (1) ◽  
Author(s):  
Zhuo-Ma Luoreng ◽  
Da-Wei Wei ◽  
Xing-Ping Wang
Keyword(s):  
T Cells ◽  
Epithelial Cells ◽  
Dairy Cows ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Luciferase Reporter ◽  
Regulation Mechanism ◽  
Bovine Mammary Epithelial Cells ◽  
Tnf Α

AbstractMastitis is a complex inflammatory disease caused by pathogenic infection of mammary tissue in dairy cows. The molecular mechanism behind its occurrence, development, and regulation consists of a multi-gene network including microRNA (miRNA). Until now, there is no report on the role of miR-125b in regulating mastitis in dairy cows. This study found that miR-125b expression is significantly decreased in lipopolysaccharide (LPS)-induced MAC-T bovine mammary epithelial cells. Also, its expression is negatively correlated with the expression of NF-κB inhibitor interacting Ras-like 2 (NKIRAS2) gene. MiR-125b target genes were identified using a double luciferase reporter gene assay, which showed that miR-125b can bind to the 3′ untranslated region (3′ UTR) of the NKIRAS2, but not the 3′UTR of the TNF-α induced protein 3 (TNFAIP3). In addition, miR-125b overexpression and silencing were used to investigate the role of miR-125b on inflammation in LPS-induced MAC-T. The results demonstrate that a reduction in miR-125b expression in LPS-induced MAC-T cells increases NKIRAS2 expression, which then reduces NF-κB activity, leading to low expression of the inflammatory factors IL-6 and TNF-α. Ultimately, this reduces the inflammatory response in MAC-T cells. These results indicate that miR-125b is a pro-inflammatory regulator and that its silencing can alleviate bovine mastitis. These findings lay a foundation for elucidating the molecular regulation mechanism of cow mastitis.

MicroRNA-141 participates in milk lipid metabolism by targeting SIRT1 in bovine mammary epithelial cells

2020 ◽  
Vol 60 (16) ◽  
pp. 1877
Author(s):  
Yujia Sun ◽  
Hailei Xia ◽  
Xubin Lu ◽  
Chong Xu ◽  
Mingxun Li ◽  
...  
Keyword(s):  
Lipid Metabolism ◽  
Epithelial Cells ◽  
Dairy Cows ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Luciferase Assay ◽  
Milk Lipid ◽  
Potential Candidate ◽  
Bovine Mammary Epithelial Cells ◽  
Sirt1 Gene

Context The regulation of milk lipids is important for the evaluation of dairy cows’ performance. Lipids are produced and secreted by mammary gland under the regulation of steroid hormones, growth factors and microRNAs (miRNAs). MicroRNAs have been verified to be involved in numerous biological processes. Previous studies have shown that miR-141 is expressed at higher levels in dairy cows at peak lactation than in those at early lactation. However, the roles of miR-141 in bovine mammary epithelial cells (BMECs) and the mechanisms how it affects lipid metabolism are as yet unknown. Aims The aims of this study were to clarify (i) the molecular mechanisms of miR-141 in milk lipid metabolism, and (ii) how miR-141 affects milk lipid metabolism in BMECs. Methods Triglycerides were observed in BMECs using triglyceride analysis after overexpression or inhibition of miR-141; selected potential candidate genes that are targeted by miR-141 using TargetScan. The regulatory relationship among miR-141, SIRT1 gene and lipid metabolism-related genes (SREBF1, FASN and PPARγ) by using the dual luciferase assay, quantitative real-time PCR and western blotting. Key results Through overexpression or inhibition of miR-141 expression, we found that miR-141 promoted lipid metabolism in BMECs and an increase in triglycerides was observed in these cells. Further, miR-141 targets the 3′UTR of SIRT1 mRNA, and negative regulates the expression of SIRT1 gene in BMECs. Also, the expression levels of SREBF1, FASN and PPARγ, which are related to milk lipid metabolism, were also altered after overexpression miR-141. Conclusions Our results have revealed that miR-141 could promote milk lipid metabolism in BMECs by means of negative regulates SIRT1 gene and positive effects lipid metabolism-related genes (SREBF1, FASN and PPARγ) in BMECs. Implications Our research indicates that miR-141 could be considered a marker in cattle breeding to obtain high quality dairy products. It would be useful to study the function of miRNAs in milk lipid metabolism and synthesis. In the long term these findings might be helpful in developing practical means to improve the quality of ruminant milk.

Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells

1999 ◽  
Vol 112 (19) ◽  
pp. 3399-3412 ◽  
Author(s):  
E. Chanat ◽  
P. Martin ◽  
M. Ollivier-Bousquet
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Golgi Apparatus ◽  
Rough Endoplasmic Reticulum ◽  
Mammary Epithelial Cells ◽  
Whey Proteins ◽  
Mammary Epithelial ◽  
The Other ◽  
Soluble Form ◽  
Beta Casein

In lactating mammary epithelial cells, interaction between caseins is believed to occur after their transport out of the endoplasmic reticulum. We show here that, in alpha(S1)-casein-deficient goats, the rate of transport of the other caseins to the Golgi apparatus is highly reduced whereas secretion of whey proteins is not significantly affected. This leads to accumulation of immature caseins in distended rough endoplasmic reticulum cisternae. Casein micelles, nevertheless, were still observed in secretory vesicles. In contrast, no accumulation was found in mammary epithelial cells which lack beta-casein. In mammary epithelial cells secreting an intermediate amount of alpha(S1)-casein, less casein accumulated in the rough endoplasmic reticulum, and the transport of alpha(S1)-casein to the Golgi occurred with kinetics similar to that of control cells. In prolactin-treated mouse mammary epithelial HC11 cells, which do not express alpha(S)-caseins, endoplasmic reticulum accumulation of beta-casein was also observed. The amount of several endoplasmic reticulum-resident proteins increased in conjunction with casein accumulation. Finally, the permeabilization of rough endoplasmic reticulum vesicles allowed the recovery of the accumulated caseins in soluble form. We conclude that optimal export of the caseins out of the endoplasmic reticulum is dependent upon alpha(S1)-casein. Our data suggest that alpha(S1)-casein interacts with the other caseins in the rough endoplasmic reticulum and that the formation of this complex is required for their efficient export to the Golgi.

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