Search results for: Ser650
#33974920 2021/05/08 To Up
Androgen and glucocorticoid receptor phosphorylation following resistance exercise and pre-workout supplementation.Consumption of caffeine or caffeine containing pre-workout supplements (SUPP) augments steroid hormone responses to resistance exercise (RE). However, the activation of glucocorticoid (GR) and androgen receptors (AR) following RE SUPP has not been investigated. The purpose of this study was to determine the influence of a pre-workout supplement on AR and GR phosphorylation following RE.
Justin X Nicoll, Andrew C Fry, Eric M Mosier
2639 related Products with: Androgen and glucocorticoid receptor phosphorylation following resistance exercise and pre-workout supplementation.100ug50 ug 5mg100ug1 ml50 ug 100ug100ug100ug100ul100ug100ug
#30928381 2019/03/27 To Up
Activation of PSGR with Î²-ionone suppresses prostate cancer progression by blocking androgen receptor nuclear translocation.The prostate-specific G protein-coupled receptor (PSGR) is a class A G protein-coupled receptor (GPCR) that is specifically expressed in prostate epithelial cells, and its expression has been linked to prostate cancer (PCa) progression. Here, we show that activation of PSGR with its ligand Î²-ionone, an end-ring analog of Î²-carotenoid, can suppress PCa cell growth both in vitro and in vivo model. Dissection of the mechanism underlying this relationship reveals that activation of PSGR by Î²-ionone suppresses AR nuclear translocation via phosphorylation of AR at residue Ser650 by p38 and JNK, which leads to the suppression of AR transactivation, further suppressing PCa cell growth. Overall, we link a cancer cell-specific GPCR with the nuclear AR and show that targeting PSGR can provide us a new target to combat PCa better.
Hongjun Xie, Tianjie Liu, Jiaqi Chen, Zhao Yang, Shan Xu, Yizeng Fan, Jin Zeng, Yule Chen, Zhenkun Ma, Yang Gao, Dalin He, Lei Li
1495 related Products with: Activation of PSGR with Î²-ionone suppresses prostate cancer progression by blocking androgen receptor nuclear translocation.100ug1 ml100ul100ug
#30414425 2018/11/07 To Up
Sex-based differences in resting MAPK, androgen, and glucocorticoid receptor phosphorylation in human skeletal muscle.To determine if there is differential expression and phosphorylation of the androgen receptor (AR), glucocorticoid receptor (GR), and mitogen-activated protein kinases (MAPK) in skeletal muscle at rest between males and females.
Justin X Nicoll, Andrew C Fry, Eric M Mosier
1233 related Products with: Sex-based differences in resting MAPK, androgen, and glucocorticoid receptor phosphorylation in human skeletal muscle.2 Pieces/Box50ul100 μg2 Pieces/Box96 wells (1 kit)2 Pieces/Box20 96 wells (1 kit)2 Pieces/Box100 μg96tests96 wells (1 kit)
#27627109 2016/09/14 To Up
Regulation of Lipolysis and Adipose Tissue Signaling during Acute Endotoxin-Induced Inflammation: A Human Randomized Crossover Trial.Lipolysis is accelerated during the acute phase of inflammation, a process being regulated by pro-inflammatory cytokines (e.g. TNF-Î±), stress-hormones, and insulin. The intracellular mechanisms remain elusive and we therefore measured pro- and anti-lipolytic signaling pathways in adipocytes after in vivo endotoxin exposure.
Nikolaj Rittig, Ermina Bach, Henrik Holm Thomsen, Steen BÃ¸nlykke Pedersen, Thomas Sava Nielsen, Jens O JÃ¸rgensen, Niels Jessen, Niels MÃ¸ller
2993 related Products with: Regulation of Lipolysis and Adipose Tissue Signaling during Acute Endotoxin-Induced Inflammation: A Human Randomized Crossover Trial.1 kit200 4500 500 500 16 Arrays/Slide
#26636645 // To Up
Protein phosphatase 1 suppresses androgen receptor ubiquitylation and degradation.The phosphoprotein phosphatases are emerging as important androgen receptor (AR) regulators in prostate cancer (PCa). We reported previously that the protein phosphatase 1 catalytic subunit (PP1Î±) can enhance AR activity by dephosphorylating a site in the AR hinge region (Ser650) and thereby decrease AR nuclear export. In this study we show that PP1Î± increases the expression of wildtype as well as an S650A mutant AR, indicating that it is acting through one or more additional mechanisms. We next show that PP1Î± binds primarily to the AR ligand binding domain and decreases its ubiquitylation and degradation. Moreover, we find that the PP1Î± inhibitor tautomycin increases phosphorylation of AR ubiquitin ligases including SKP2 and MDM2 at sites that enhance their activity, providing a mechanism by which PP1Î± may suppress AR degradation. Significantly, the tautomycin mediated decrease in AR expression was most pronounced at low androgen levels or in the presence of the AR antagonist enzalutamide. Consistent with this finding, the sensitivity of LNCaP and C4-2 PCa cells to tautomycin, as assessed by PSA synthesis and proliferation, was enhanced at low androgen levels or by treatment with enzalutamide. Together these results indicate that PP1Î± may contribute to stabilizing AR protein after androgen deprivation therapies, and that targeting PP1Î± or the AR-PP1Î± interaction may be effective in castration-resistant prostate cancer (CRPC).
Xiaming Liu, Weiwei Han, Sarah Gulla, Nicholas I Simon, Yanfei Gao, Changmeng Cai, Hongmei Yang, Xiaoping Zhang, Jihong Liu, Steven P Balk, Shaoyong Chen
2146 related Products with: Protein phosphatase 1 suppresses androgen receptor ubiquitylation and degradation.100ul100ug100ul100ug1000 TESTS/0.65ml100ug1000 100ug100ul100ug100ug100ul
#25299849 2014/09/08 To Up
eNOS-JNK1-AR signaling pathway mediates deltamethrin-induced germ cells apoptosis in testes of adult rats.The purpose of this study is to examine germ cells apoptosis and reduction of spermatogenesis which might be induced by deltamethrin (DM). Furthermore, the study is performed to determine if the apoptosis is mediated by the signaling proteins: eNOS, JNK1 and androgen receptor (AR). Fifty-four male SD rats were divided into nine groups (six rats each): blank control group; corn oil treated group; DM treated group; saline treated group; DM+saline treated group; DM+histamine (eNOS specific agonist) treated group; 50% ethanol treated group; DM+50% ethanol group and DM+quercetagetin (JNK1 specific inhibitor) treated group. The experiment was conducted for 15 days. Apoptosis was evaluated by TUNEL; S-nitrosylation of JNK1 was examined by the biotin switch assay; eNOS expression and Ser650 phosphorylation of AR were assessed by immunoblotting and immunohistochemical analysis, respectively. DM treated group showed notable apoptotic cells and reduced production of sperm, while DM plus histamine group and DM plus quercetagetin group showed remarkably decreased apoptosis and improved production of sperm. Administration of DM inhibited spermatogenesis, the activity of eNOS and S-nitrosylation of JNK1. Meanwhile, phosphorylation of AR was shown to be elevated. Histamine and quercetagetin were also examined to have a further confirmation. It is suggested DM-induced germ cells apoptosis and reduction of sperm production were mediated by eNOS-JNK1-AR signaling pathway.
Hong-min Yu, Yang Wu, Pei Ju, Bing-hua Wang, Xiang-dong Yang, Hong-mei Wang, Li-chun Xu
1336 related Products with: eNOS-JNK1-AR signaling pathway mediates deltamethrin-induced germ cells apoptosis in testes of adult rats.2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box2 Pieces/Box
#19018281 2008/11/19 To Up
Ser649 and Ser650 are the major determinants of protein kinase A-mediated activation of human hormone-sensitive lipase against lipid substrates.Hormone-sensitive lipase (HSL) is a key enzyme in the mobilization of fatty acids from stored triacylglycerols. Its activity is regulated by reversible protein phosphorylation. In rat HSL Ser563, Ser659 and Ser660 have been shown to be phosphorylated by protein kinase A (PKA) in vitro as well as in vivo.
Christian Krintel, Peter Osmark, Martin R Larsen, Svante ResjÃ¶, Derek T Logan, Cecilia Holm
1802 related Products with: Ser649 and Ser650 are the major determinants of protein kinase A-mediated activation of human hormone-sensitive lipase against lipid substrates.72 tests100ul250ug100 96 wells (1 kit)250ul96T1mg50 ug100 10
#9191031 // To Up
Cleavage of the complement system C3 component by HIV-1 proteinase.The C3 factor of the complement system and its C3b fragment are cleaved in vitro by the proteinase of the human immunodeficiency virus, type 1 (HIV PR). The cleavage occurs in the alpha-chain of both substrates at multiple sites yielding a 100 kDa fragment of the C3 alpha-chain and multiple fragments of the C3b alpha-chain. The scissile bonds are: Ala86-Glu87, Leu310-Leu311, His641-Trp642 and Arg649-Ser650. The resulting fragments resemble the physiologically occurring inactive fragments of C3: C3c and C3d, suggesting a possible biological role of the HIV-proteinase in the complement inactivation process.
A F Kisselev, R Mentele, K von der Helm100ug100ug1 mg1 mg1 mg100ug10ml1 g1 mg25 mg2.5 mg
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