Enhancement of milk protein expression in mammary epithelial cells via co-culturing with preadipocyte cells

2017 ◽  
Vol 22 (5) ◽  
pp. 556-560 ◽  
Author(s):  
Won-Young Lee ◽  
Hyun-Jung Park ◽  
Joon Mo Yeo ◽  
Ha Yeon Jeong ◽  
Hyuk Song
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Milk Protein ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial

scholarly journals Beta-Sitosterol Promotes Milk Protein and Fat Syntheses-Related Genes in Bovine Mammary Epithelial Cells

Animals ◽  
2021 ◽  
Vol 11 (11) ◽  
pp. 3238
Author(s):  
Xinlu Liu ◽  
Jinglin Shen ◽  
Jinxin Zong ◽  
Jiayi Liu ◽  
Yongcheng Jin
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Dairy Cows ◽  
Milk Fat ◽  
Milk Protein ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Bovine Mammary Epithelial Cells ◽  
Mrna And Protein Expression ◽  
Fat Synthesis

β-sitosterol, a phytosterol with multiple biological activities, has been used in the pharmaceutical industry. However, there are only a few reports on the use of β-sitosterol in improving milk synthesis in dairy cows. This study aimed to investigate the effects of β-sitosterol on milk fat and protein syntheses in bovine mammary epithelial cells (MAC-T) and its regulatory mechanism. MAC-T cells were treated with different concentrations (0.01, 0.1, 1, 5, 10, 20, 30, or 40 μM) of β-sitosterol, and the expression levels of milk protein and fat synthesis-related genes and proteins were analyzed. β-sitosterol at 0.1, 1, and 10 μM concentrations promoted the mRNA and protein expression of β-casein. β-sitosterol (0.1, 1, 10 μM) increased the mRNA and protein expression levels of signal transducer activator of transcription 5 (STAT5), mammalian target of rapamycin (mTOR), and ribosomal protein S6 kinase beta-1 (S6K1) of the JAK2/STAT5 and mTOR signaling pathways. It also stimulated the milk fat synthesis-related factors, including sterol regulatory element-binding protein 1 (SREBP1), peroxisome proliferator-activated receptor-gamma (PPARγ), acetyl-CoA carboxylase (ACC), lipoprotein lipase (LPL), and stearyl CoA desaturase (SCD). β-sitosterol (0.1, 1, 10 μM) also significantly increased the expression of growth hormone/insulin-like growth factor-1 (GH/IGF-1) axis and hypoxia-inducible factor-1α (HIF-1α)-related genes. Notably, the compound inhibited the expression of the negative regulator, the suppressor of cytokine signaling 2 (SOCS2) at the two lower concentrations (0.1, 1 μM), but significantly promoted the expression at the highest concentration (30 μM). These results highlight the role of β-sitosterol at concentrations ranging from 0.1 to 10 μM in improving milk protein and fat syntheses, regulating milk quality. Therefore, β-sitosterol can be used as a potential feed additive to improve milk quality in dairy cows.

Primary Culture of Porcine Mammary Epithelial Cells as a Model System for Evaluation of Milk Protein Expression

2001 ◽  
Vol 65 (9) ◽  
pp. 2098-2101 ◽  
Author(s):  
Haruto KUMURA ◽  
Atsushi TANAKA ◽  
Youichi ABO ◽  
Saori YUI ◽  
Kei-ichi SHIMAZAKI ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Primary Culture ◽  
Milk Protein ◽  
Mammary Epithelial Cells ◽  
Model System ◽  
Mammary Epithelial

scholarly journals  Gene expression of six major milk proteins in primary bovine mammary epithelial cells isolated from milk during the first twenty weeks of lactation

2012 ◽  
Vol 57 (No. 10) ◽  
pp. 469-480 ◽  
Author(s):  
T. Sigl ◽  
H.H.D. Meyer ◽  
S. Wiedemann
Keyword(s):  
Gene Expression ◽  
Epithelial Cells ◽  
Milk Protein ◽  
Protein Gene ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Milk Protein Gene ◽  
Bovine Mammary Epithelial Cells ◽  
Milk Protein Genes ◽  
Milk Protein Gene Expression

&nbsp;The objective of the present study was to refine a previously developed method to isolate primary bovine mammary epithelial cells (pBMEC) from fresh milk. Using this method, it was tested whether the number of pBMEC and the relation of recovered pBMEC to total somatic cell count vary within the individual lactation stages. Furthermore, the expression levels of the milk protein genes during the first twenty weeks of lactation were determined by quantitative PCR method. A total number of 152 morning milk samples were obtained from twenty-four Holstein-Friesian cows during the first 20 weeks of lactation (day 8, 15, 26, 43, 57, 113, and 141 postpartum). Numbers of extracted pBMEC were consistent at all time-points (1.1 &plusmn; 0.06 to 1.4 &plusmn; 0.03 &times;10<sup>3</sup>/ml) and an average value of RNA integrity number (RIN) was 6.3 &plusmn; 0.3. Percentage of pBMEC in relation to total milk cells (2.0 &plusmn; 0.2 to 6.7 &plusmn; 1.0%) correlated with milk yield. Expression patterns of the casein genes alpha (&alpha;)<sub>S1</sub>, (&alpha;)<sub>S2</sub>, beta (&beta;), and kappa (&kappa;) (CSN1S1, CSN1S2, CSN2, CSN3, respectively) and the whey protein genes &alpha;-lactalbumin (LALBA) and progestagen-associated endometrial protein (PAEP; known as &beta;-lactoglobulin) were shown to be comparable, i.e. transcripts of all six milk protein genes were found to peak during the first two weeks of lactation and to decline continuously towards mid lactation. However, mRNA levels were different among genes with CSN3 showing the highest and LALBA the lowest abundance. We hypothesized that milk protein gene expression has a pivotal effect on milk protein composition with no influence on milk protein concentration. This paper is the first to describe milk protein gene expression during lactation in pBMEC collected in milk. Future studies will be needed to understand molecular mechanisms in pBMEC including regulation of expression and translation throughout lactation. &nbsp;

Alpha-ketoglutarate enhances milk protein synthesis by porcine mammary epithelial cells

Amino Acids ◽  
2016 ◽  
Vol 48 (9) ◽  
pp. 2179-2188 ◽  
Author(s):  
Qian Jiang ◽  
Liuqin He ◽  
Yongqing Hou ◽  
Jiashun Chen ◽  
Yehui Duan ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Epithelial Cells ◽  
Milk Protein ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial

Comparative phosphoproteomics analysis of the effects of L-methionine on dairy cow mammary epithelial cells

2012 ◽  
Vol 92 (4) ◽  
pp. 433-442 ◽  
Author(s):  
Limin Lu ◽  
Xuejun Gao ◽  
Qingzhang Li ◽  
Jianguo Huang ◽  
Rong Liu ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Epithelial Cells ◽  
Dairy Cow ◽  
Milk Protein ◽  
Mammary Epithelial Cells ◽  
Reversed Phase ◽  
Trna Synthetase ◽  
Mammary Epithelial ◽  
Two Dimensional Gel Electrophoresis ◽  
Phosphorylated Proteins

Lu, L., Gao, X., Li, Q., Huang, J., Liu, R. and Li, H. 2012. Comparative phosphoproteomics analysis of the effects of L-methionine on dairy cow mammary epithelial cells. Can. J. Anim. Sci. 92: 433–442. L-methionine is an essential amino acid that plays fundamental roles in protein synthesis. Many nuclear phosphorylated proteins such as Stat5 (signal transducer and activator of transcription 5) and mTOR (mammalian target of rapamycin) regulate milk protein synthesis. But a comprehensive understanding of transcriptional and posttranscriptional regulation of milk protein synthesis is lacking. In the current study, two-dimensional gel electrophoresis (2-DE)/MS-based proteomics analysis was used to identify phosphoproteins responsible for milk protein synthesis in dairy cow mammary epithelial cells (DCMECs). The effects of L-methionine on DCMECs were analyzed by CASY (Counter Analyser System) technique, reversed phase high performance liquid chromatography. The results showed that rate of cell proliferation and expression of β-casein were increased in DCMECs treated with 0.6 mM L-methionine for 24 h. Five proteins for which expression was significantly increased in DCMECs were selected, and their expression changes were verified by quantitative real-time PCR and Western blot analysis. The five up-regulated expressed phosphoproteins included Staphylococcal nuclease domain-containing protein 1(SND1), Septin-6, Glycyl-tRNA synthetase (GARS), Twinfilin-1 and eukaryotic elongation factor1-beta (eEF1B). This study revealed that availability of L-methionine influences the levels of nuclear phosphorylated proteins of DCMECs which opens a new avenue for the study of the molecular mechanism linking to milk protein synthesis.

Sign in / Sign up

Export Citation Format

Share Document