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30-Day Get Moving Challenge

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Dobrynya Shiryaev
Dobrynya Shiryaev

How to Install and Play Pump It Up M: Beat Finger Step APK on Your Device



Among existing drugs, proton pump inhibitors (PPIs) have promising potential to be repurposed for the treatment of IPF [5, 6]. Originally approved to reduce gastric acidity, a number of studies have linked the use of PPIs with improvement in measures of lung function leading to significantly longer transplant-free survival time in patients with well-defined IPF [7,8,9,10,11]. A recent official clinical practice guideline representing leading Thoracic Societies also conditionally recommended the use of PPIs for IPF [12]. However, mechanistic understanding of how PPIs regulate processes involved in lung remodeling is lacking. In this regard, we recently reported that PPIs directly inhibit an enzyme, dimethylarginine dimethylaminohydrolase (DDAH) [10], that is upregulated in lung tissues explanted from IPF patients [13, 14], and has been shown to promote experimental lung fibrosis [13].




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YTG is an inventor on patents, owned by Stanford University and Baylor College of Medicine, that protect the use of agents, including proton pump inhibitors (PPIs), for therapeutic use of new indications. MDB is an inventor on the patent application owned by Baylor College of Medicine.


Metastatic melanoma is the most aggressive type of skin cancer. Previously, we identified the plasma membrane Ca2+ pump isoform 4b (PMCA4b or ATP2B4) as a putative metastasis suppressor in BRAF mutant melanoma cells. Metastasis suppressors are often downregulated in cancer, therefore, it is important to identify the pathways involved in their degradation. Here, we studied the role of p38 MAPK in PMCA4b degradation and its effect on melanoma metastasis. We found that activation of p38 MAPK induces internalization and subsequent degradation of PMCA4b through the endo/lysosomal system that contributes to the low PMCA4b steady-state protein level of BRAF mutant melanoma cells. Moreover, BRAF wild type cell models including a doxycycline-inducible HEK cell system revealed that p38 MAPK is a universal modulator of PMCA4b endocytosis. Inhibition of the p38 MAPK pathway markedly reduced migration, colony formation and metastatic activity of BRAF mutant cells in vitro partially through an increase in PMCA4b and a decrease in β4 integrin abundance. In conclusion, our data suggest that the p38 MAPK pathway plays a key role in PMCA4b degradation and inhibition of this pathway-by increasing the stability of PMCA4b-may provide a potential therapeutic target for inhibition of melanoma progression and metastasis.


AAPS is an open source app for people living with insulin-dependent diabetes that acts as an artificial pancreas system (APS) on Google Android smartphones. The main components are different openAPS software algorithms which aim to do what a living pancreas does: keeping blood sugar levels within healthy limits by using automated insulin dosing (AID). Additionally, you need at least a supported and FDA/CE approved insulin pump and continuous glucose meter.


The subsection What do I need? specifies the CGMs (Continuous Glucose Monitors) and insulin pumps which are are available for use with AAPS. This subsection is important to understand so that your AAPS system can be assembled and built correctly the first time around and will function well in real world situations.


The subsection Component Setup explains how to properly integrate each of the various different separate component parts into AAPS, as well as how to set them up to work as seamlessly as possible together. All components are listed under the separate sections: CGM/FGM, xDrip Settings, Pumps, Phones, Nightscout setup, and Smartwatches. The sensor (BG) values and control of the insulin pump are particularly important information to understand. The subsection Configuration describes the best pump configurations to use in AAPS.


Finally, we assessed the metabolic consequences of infusing BNP. BNP is more commonly measured than ANP in clinical settings (53, 54), and it is administered in the clinic. Mini-pumps containing saline or BNP were implanted into 10-week-old mice, as detailed in Methods. As shown in Figure 11A, plasma levels of BNP were significantly higher in the mice receiving BNP, while within relevant physiological range (55). Although there was a trend for mice receiving BNP to consume more food, there were no significant differences in food intake or physical activity between the 2 groups (data not shown). Mice treated with BNP exhibited greater oxygen consumption (Figure 11B) and energy expenditure (Figure 11C) during both the light and dark periods than the saline control group. Respiratory exchange ratio (RER) was modestly decreased only during the light period (saline, 0.845 0.004 kcal/l; BNP, 0.805 0.006 kcal/l; P


BNP infusion increased oxygen consumption, energy expenditure, and expression of brown adipocyte markers. C57BL/6 mice were treated for 7 days with saline (0.9% NaCl) or with BNP (2 ng/kg/ml) via Mini-pump. Food intake, physical activity, and respiration were measured by the Oxymax Comprehensive Lab Animal Monitoring System. (A) Plasma BNP levels measured on day 7. (B) Oxygen consumption and (C) energy expenditure (EE) during the light and dark periods. *P P P D) iBAT (BAT) and (E) inguinal WAT for UCP1, PGC-1α, and cytochrome c protein levels. GAPDH was used as internal standard.


LPS has been widely used both in vitro and in vivo to evaluate the anti-inflammatory potential of many agents [42], and long-term administration of LPS can mimic chronic inflammation diseases [43]. In addition, exploring the low-dose influx of LPS to illustrate the etiology of chronic inflammatory conditions has been justified by the plentiful presence of LPS in the surrounding [8]. Therefore, many experimental studies have used LPS to induce chronic subclinical inflammation either by intermittent injection or by using osmotic pump release [44, 45]. In line with these reports, the current study demonstrated that the selected dose and administration frequency of LPS have successfully produced the typical features of CSSI, including partial suppression of food intake and body weight gain, leukocytosis and elevated pro-inflammatory mediators in the peripheral circulation. The daily consumption of SBH ameliorated the impact of CSSI on animal performance through improving food intake and maintaining a normal body weight gain. Consuming functional foods rich in bioactive compounds such as polyphenols has been well-documented to preserve hemostasis during low-grade chronic inflammation [46]. In addition, the long-term consumption of SBH has been proven previously to maintain normal food intake and body weight gain [47].


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On days 23, 25 and 27, conscious mice were exposed to ozone [1.0 parts/million (ppm) for 3 h] or filtered air. Ozone was generated by directing an air stream with a micro air pump (SC3601PM, Shenzhen, China) into a AQUA MEDIC O3 generator (model 300, AB Aqua Medic GmbH, Bissendorf, Germany). Ozone concentration in the chamber was monitored continuously by an Ozone Switch (OS-4, Newark, USA), which also controlled the operation of the ozone generator in response to the instantaneous value. The target O3 concentration range was set as 0.77 ppm 1.32 ppm, which has been proved by our preliminary experiment to be able to maintain a comparatively stable O3 concentration averaged as 1.01 0.02 ppm (data not shown). This methodology of O3 exposure has been adapted by previous study which had documented that, such level of ozone inhalation can induced the airway inflammation but not influence the body weight of mice [17], which means less toxic effect. One hour before and 4 hrs after the O3 exposure, mice were injected through tail vein SB239063 (Sigma Aldrich, St. Louis, MO) dissolved in 3% DMSO (0.1 ml, Sigma Aldrich, St. Louis, MO) or DMSO only, respectively. The dosages of SB239063 were titrated in a preliminary experiment, where the final dosage of 4.0 mg/kg was selected. The present experimental protocol was outlined in Figure 1.


rolled/MAPK EVOLUTIONARY HOMOLOGS Table of contents Miscellaneous targets of MAP kinaseSon of sevenless-1 and -2 (Sos-1 and -2) (Drosophila homolog SOS) are guanosine nucleotide exchange factors implicated in theactivation of Ras (See Drosophila Ras) by both the insulin and epidermal growth factor signal transduction pathways. Ras initiates the activation of cellular protein kinases including mitogen-activated protein (MAP)kinases. Sos proteins contain numerous sequences in their carboxyl-terminal regions that correspond toconsensus sites for MAP kinase phosphorylation. To examine whether these sites are substrates for MAPkinases, the cDNA encoding Drosophila Sos (dSos) was tagged with sequences encoding the majorantigenic epitope of the influenza virus hemagglutinin (HA) to create a dSosHA fusion construct. dSosHAis transiently expressed in COS-1 cells and immunoprecipitated with anti-HA antibodies. When immunecomplexes are incubated with purified MAP kinase and radioactive ATP, a phosphorylated band of 180kDa is observed. This band is not present inimmunoprecipitations from cells transfected with vector alone. No phosphorylation of the 180 kDa band isseen when immunoprecipitates are incubated with ATP in the absence of MAP kinase. There are twomajor phosphorylated species that are also found in dSosHA isolated from COS-1 cells.This supports the hypothesis that a feedback loop exists wherein growth factor-activatedMAP kinases phosphorylate and regulate Sos proteins (Cherniack, 1994). Mitogen-activated protein (MAP) kinases bind tightly to many of their physiologically relevant substrates. A new subfamily of murineserine/threonine kinases has been identified, whose members, MAP kinase-interacting kinase 1 (Mnk1) and Mnk2, bind tightly to the growth factor-regulated MAP kinases: Erk1 andErk2. MNK1, but not Mnk2, also binds strongly to the stress-activated kinase, p38. MNK1 complexes more strongly with inactive than active Erk, implying thatMnk and Erk may dissociate after mitogen stimulation. Erk and p38 phosphorylate MNK1 and Mnk2, which stimulates Mnk in vitro kinase activity toward asubstrate, eukaryotic initiation factor-4E (eIF-4E). Initiation factor eIF-4E is a regulatory phosphoprotein whose phosphorylation is increased by insulin in anErk-dependent manner. In vitro, MNK1 rapidly phosphorylates eIF-4E at the physiologically relevant site, Ser209. In cells, Mnk1 is post-translationally modifiedand enzymatically activated in response to treatment with either peptide growth factors, phorbol esters, anisomycin or UV. Mitogen- and stress-mediated MNK1activation is blocked by inhibitors of MAP kinase kinase 1 (Mkk1) and p38, demonstrating that Mnk1 is downstream of multiple MAP kinases. MNK1 may definea convergence point between the growth factor-activated and one of the stress-activated protein kinase cascades and is a candidate to phosphorylate eIF-4E incells (Waskiewicz, 1997). A novel expression screening method has been developed for identifying protein kinase substrates. In this method, a lambda phage cDNA expression library isscreened by in situ, solid-phase phosphorylation using purified protein kinase and [gamma-32P]ATP. Screening a HeLa cDNA library with ERK1 MAP kinaseyields cDNAs of previously characterized ERK substrates, c-Myc and p90RSK (see Drosophila S6kII), demonstrating the utility of this method for identifying physiological protein kinasesubstrates. A novel clone isolated in this screen, designated MNK1, encodes a protein-serine/threonine kinase, which is most similar to MAP kinase-activatedprotein kinase 2 (MAPKAP-K2), 3pK/MAPKAP-K3 and p90RSK. Bacterially expressed MNK1 is phosphorylated and activated in vitro by ERK1 and p38MAP kinases but not by JNK/SAPK. Further, MNK1 is activated upon stimulation of HeLa cells with 12-O-tetradecanoylphorbol-13-acetate, fetal calf serum,anisomycin, UV irradiation, tumor necrosis factor-alpha, interleukin-1beta, or osmotic shock, and the activation by these stimuli is differentially inhibited by the MEK inhibitor PD098059 or the p38 MAP kinase inhibitor SB202190. Together, these results indicate that MNK1 is a novel class of protein kinase that isactivated through both the ERK and p38 MAP kinase signaling pathways (Fukunaga, 1997). Xenopus laevis oogenesis is characterized by an active transcription that ceasesabruptly upon maturation. To survey changes in the characteristics of thetranscriptional machinery that might contribute to this transcriptional arrest, thephosphorylation status of the RNA polymerase II largest subunit (RPB1 subunit) wasanalyzed during oocyte maturation. The RPB1 subunit accumulates inlarge quantities from previtellogenic early diplotene oocytes up to fully grown oocytes.The C-terminal domain (CTD) of the RPB1 subunit is essentiallyhypophosphorylated in growing oocytes from Dumont stage IV to stage VI. Uponmaturation, the proportion of hyperphosphorylated RPB1 subunits increasesdramatically and abruptly. The hyperphosphorylated RPB1 subunits are dephosphorylated within 1 h after fertilization or heat shock of the matured oocytes. Extracts from metaphase II-arrested oocytes show a much stronger CTD kinaseactivity than extracts from prophase stage VI oocytes. Most of this kinase activity can be attributed to the activated Xp42 mitogen-activated protein (MAP) kinase, a MAPkinase of the ERK type. Making use of artificial maturation of the stage VI oocytethrough microinjection of a recombinant stable cyclin B1, a parallelactivation of Xp42 MAP kinase and phosphorylation of RPB1 is observed. Both events requiredprotein synthesis, which demonstrated that activation of p34cdc2 kinase isinsufficient to phosphorylate RPB1 ex vivo and is consistent with a contribution ofthe Xp42 MAP kinase to RPB1 subunit phosphorylation. These results further supportthe possibility that the largest RNA polymerase II subunit is a substrate of theERK-type MAP kinases during oocyte maturation (Bellier, 1997).While most untransformed cells require substrate attachment for growth (anchorage dependence), the oncogenically transformedcells lack this requirement (anchorage independence) and are often tumorigenic. However, the mechanism of loss of anchoragedependence is not fully understood. When normal rat fibroblasts are cultured in suspension without substrate attachment, thecell cycle arrests in G1 phase and the cyclin-dependent kinase inhibitor p27Kip1 protein and its mRNA accumulate.Conditional expression of oncogenic Ras induces the G1-S transition of the cell cycle and significantly shortens the half-life ofp27Kip1 protein without altering its mRNA level. Inhibition of the activation of mitogen-activated protein (MAP) kinase bycyclic AMP-elevating agents and a MEK inhibitor prevents the oncogenic Ras-induced degradation of p27Kip1 (See Drosophila Dacapo). Theseresults suggest that the loss of substrate attachment induces cell cycle arrest through the up-regulation of p27Kip1 mRNA,but the oncogenic Ras confers anchorage independence by accelerating p27Kip1 degradation through the activation of theMAP kinase signaling pathway. It appears that p27Kip1 is phosphorylated by MAP kinase in vitro and thephosphorylated p27Kip1 cannot bind to and inhibit cdk2 (Kawada, 1997). During mitosis, chromatin is condensed into mitotic chromosomes and transcription is inhibited. These are two processes that might be thwarted by the chromatin remodeling activity of the SWI/SNF complexes. Brg1and hBrm (see Drosophila Brahma), two components of human SWI/SNF (hSWI/SNF) complexes, have recently been shown tobe phosphorylated during mitosis. This suggests that phosphorylation might be used as a switch tomodulate SWI/SNF activity. Using an epitope-tag strategy, hSWI/SNF complexes were purified atdifferent stages of the cell cycle: hSWI/SNF was found to be inactive in cells blocked in G2-M.Mitotic hSWI/SNF contains Brg1 but not hBrm, and is phosphorylated on at least two subunits,hSWI3 (Drosophila homolog: Moira) and Brg1 (Sif, 1998). To test whether phosphorylation is the only modification required to inactivate the hSWI/SNF complex, a kinase was sought, capable of phosphorylating hSWI/SNF and altering its activity. Brg1 is known to be phosphorylated in unfertilized Xenopus eggs, which are naturally blocked in metaphase.Fractionation of Xenopus egg extracts revealed that a single peak of activity, which can perfectly phosphorylate Brg1, cofractionates with ERK1. To determine whether ERK1 can phosphorylate human SWI/SNF subunits, MEK1-activated ERK1 was tested for its abilityto phosphorylate the hSWI/SNF complex. Wild-type GST-ERK1 can phosphorylate SWI/SNF subunits,whereas a kinase-deficient form of GST-ERK1 cannot. Other well-characterized mitoticki


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