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Dec 24, 2013 · In accordance with these results, previous studies indicate that Rac activates the RAF/MEK/ERK pathway (16, 17) and that Rac/PAK regulation of ERK is essential for HER2-induced transformation of breast epithelial cancer cells.

However, the regulation of ERK signaling in a PI3K-dependent manner via P-Rex1 has not been previously described.


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Радиатор стальной ELSEN ERK 21 600 2600

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For example, two negative feedback loops composed of ERK→SOS→Ras→ERK and ERK→GAB1→SOS→Ras→ERK compensate the upstream signals of the ERK pathway when MEK is suppressed by its specific inhibitor, which means that such feedback loops are one important mechanism of maintaining the robustness of signal flow.

Радиатор стальной ELSEN ERK 21 600 2600


The Ras-extracellular signal-regulated kinase (Ras-ERK) and phosphatidylinositol 3-kinase-mammalian target of rapamycin (PI3K-mTOR) signaling pathways are the chief for controlling survival, differentiation, proliferation, metabolism, and motility in response to extracellular cues.


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Phosphorylation of Ser 235/236 was found to require extracellular signal-regulated (ERK) signaling, suggesting that Здесь or other kinases downstream of ERK, such as the mitogen- and stress-activated (MSK1/2), contribute to rpS6 phosphorylation upon mitogen stimulation.

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Радиатор стальной ELSEN ERK 21 600 2600

Hiromichi Ebi aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and bDivision of Medical Oncology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan Carlotta Costa aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Anthony C.
Faber aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Madhuri Nishtala aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Hiroshi Kotani bDivision of Medical Oncology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan Dejan Juric aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Patricia Della Pelle aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Youngchul Song aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Seiji Yano bDivision of Medical Oncology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan Mari Mino-Kenudson aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Cyril H.
Benes aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and Jeffrey A.
Engelman aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and aMassachusetts General Hospital Cancer Center and Harvard Medical School, Charlestown, MA, 02129; and bDivision of Medical Oncology, Cancer Research Institute, Kanazawa University, Kanazawa, Ishikawa 920-0934, Japan Edited by Peter K.
Vogt, The Scripps Research Institute, La Jolla, CA, and approved November 8, 2013 received for review July 25, 2013 Author contributions: H.
Genetic alterations targeting the PI3K pathway are highly prevalent in breast cancers.
Although breast cancers harboring PIK3CA mutation and HER2 amplification have enhanced sensitivity to PI3K inhibitors, the mechanism underlying this sensitivity is unknown.
Importantly, expression levels of the Rac-GEF, P-Rex1, correlate with sensitivity to PI3K inhibitors among these breast cancer cell lines, indicating its potential utility as a biomarker to identify cancers that will respond to inhibitors.
The PI3K pathway is genetically altered in excess of 70% of breast cancers, largely through PIK3CA mutation and HER2 amplification.
Preclinical studies have suggested that these subsets of breast cancers are particularly sensitive to PI3K inhibitors; however, the reasons for this heightened sensitivity are mainly unknown.
We investigated the signaling effects of PI3K inhibition in PIK3CA mutant and HER2 amplified breast cancers using PI3K inhibitors currently in clinical trials.
Furthermore, PI3K inhibition led to an ERK-dependent up-regulation of the proapoptotic protein, BIM, followed by induction of apoptosis.
Expression of a constitutively active form of Rac1 in these breast cancer models blocked PI3Ki-induced down-regulation of ERK phosphorylation, apoptosis, and mitigated PI3K inhibitor sensitivity in vivo.
The expression level of P-Rex1 correlates with sensitivity to PI3K inhibitors in these breast cancer cell lines.
In addition, P-Rex1 may serve as a biomarker to predict response to single-agent PI3K inhibitors within this subset of breast cancers.
The phosphoinositide 3-kinase PI3K family of lipid plays a prominent role in the growth and survival of several types of cancer.
The PI3K pathway is aberrantly activated by a number of different mechanisms in cancers.
PI 3,4,5 P3 directly binds to the pleckstrin homology PH domains of certain proteins, such as AKT, leading to their activation, which in turn transmit growth and survival signals.
These findings have encouraged the development of several different PI3K inhibitors, many of which are either in or approaching clinical trial testing.
Genotype-driven patient selection has been investigated to uncover patient populations that will be particularly susceptible to PI3K inhibitors.
Cancers harboring mutations in the PIK3CA gene have emerged as among the most sensitive to single-agent PI3K inhibitors in several preclinical studies, although clinical activity to date has been mixed —.
These gain-of-function mutations in the PI3KCA gene are found in a broad range of cancers, and they are highly enriched in breast cancer, where they are observed in 20—25% of cases.
However, even among patients whose cancers harbor PIK3CA mutations, a significant heterogeneity of responses has been observed to PI3K inhibitors currently being tested in clinical studies —.
There have been some patients with bona fide response evaluation criteria in solid tumors RECIST criteria responses, but the majority has not had similarly impressive outcomes.
These early clinical results highlight the potential utility of a biomarker of sensitivity to single-agent PI3K inhibitors.
Importantly, the expression levels of the Rac guanine exchange factor Rac-GEFP-Rex1, correlate with sensitivity to PI3K inhibitors in these breast cancer cell lines.
This result was recapitulated with additional PI3K inhibitors, including the p110α-specific inhibitor, BYL719, and another pan-PI3K inhibitor, BKM120.
Of note, in PIK3CA and HER2 amplified breast cancers that harbor concurrent RAS mutations, PI3K inhibitors did not suppress ERK signaling.
PI3K inhibition down-regulates both AKT and ERK signaling in HER2 amplified and PIK3CA mutant breast cancer cells.
A Cells were treated with 1 μM GDC-0941 for the indicated times, and lysates were probed with the indicated antibodies.
Although BT474 has a K111N amino жмите сюда substitution, this mutation was found to have no effect on AKT phosphorylation.
Independent experiments were performed three times, and a representative result is shown.
B Cells were treated with 1 μM GDC-0941, 1 μM BYL719, and 1 μM BKM120 for 30 min, and lysates were probed with the indicated antibodies.
Independent experiments were performed three times, and a representative result is shown.
C Cells were treated with 1 μM GDC-0941 for the indicated times, and lysates were probed with the indicated antibodies.
Independent experiments were performed three times, and a representative result is shown.
However, to our surprise, we observed that RAS activity was not suppressed but rather was induced after GDC-0941 treatment in PIK3CA mutant and HER2 amplified breast cancer cells.
Indeed, we observed that knockdown of small GTPase K-RAS K-RAS or small GTPase H-RAS H-RAS failed to suppress ERK phosphorylation in T47D cells, in contrast to a K-RAS mutant pancreatic cancer cell line.
Previous research has identified alternative mechanisms for activating ERK signaling, and thus we turned our attention to Rac, the small GTPase that is a key downstream effector of PI3K signaling.
We observed that GDC-0941 treatment significantly inhibited Rac1 activity as well as phosphorylation of PAK, C-RAF, MEK, and ERK.
Among the three isoforms of PAK, only siRNA against PAK1 and PAK3 suppressed ERK phosphorylation after PI3K inhibition.
Interestingly PAK2 down-regulation paradoxically caused activation of ERK for reasons unknown at this time.
Taken together, these results are consistent with PI3K activating the ERK signaling как сообщается здесь via Rac, independent of RAS.
PI3K inhibition suppresses Rac but not RAS activation.
A RAS activity assays were completed after 30 min of GDC-0941 treatment.
Representative detection of active RAS RAS-GTP, determined by читать больше Raf-1 pull-down assay; is shown.
The corresponding whole-cell extracts were probed with the indicated antibodies.
Independent experiments were performed at least three times, and a representative result is shown.
B Cells were transfected with control, K-RAS, or H-RAS—targeted siRNA for 72 h.
Lysates were prepared and probed with the indicated antibodies.
Results were confirmed by two independent experiments.
Cells were lysed after 30 min, and Rac-GTP levels were determined with a PAK1-binding domain pull-down assay.
Independent experiments were performed more than three times for T47D and twice for other cell lines, and a representative result is shown.
D Cells were treated with 1 μM Детальнее на этой странице for the indicated times, and lysates were probed with the indicated antibodies.
Independent experiments were performed at least three times, and a representative result is shown.
E Schematic representation of how PI3K is proposed to regulate ERK pathway.
To determine whether down-regulation of Rac is essential for PI3K inhibitors to suppress ERK phosphorylation, we expressed a constitutively activated version of Rac1 in T47D and MCF7 cells.
Expression of constitutively active Rac1 G12V Rac1 abrogated PI3K-dependent down-regulation of C-RAF and ERK phosphorylation, although suppression of AKT phosphorylation was preserved and.
Importantly, G12V Rac1 expression mitigated apoptosis induced by PI3K inhibition even though AKT activity remained suppressed.
Consistent with these results, GDC-0941 treatment blocked growth of MCF7 tumor xenografts in vivo, but efficacy of the PI3K inhibitor was substantially mitigated in the MCF7 tumors expressing constitutively active Rac1.
Thus, down-regulation of Rac1 is necessary for PI3K inhibitors to suppress ERK signaling and for full efficacy in vivo.
Constitutive Rac1 activation abrogates the efficacy of PI3K inhibitors in vivo.
A Cells expressing the empty vector VC or constitutive form of Rac1 Rac1 G12V were treated with 1 μM GDC-0941 for 30 min, and lysates were evaluated by Western blot with the indicated antibodies.
Independent experiments were performed three times, and a representative result is shown.
B MCF7 cells expressing the empty vector VC or constitutive form of Rac1 Rac1 G12V were treated with 1 μM GDC-0941 Консоль с опорой ml для пров.

лотка облег. осн. 100 дкс fc34105 72 h.
The percentage of cells undergoing apoptosis, as measured by annexin V positivity, is shown relative to untreated cells.
The average tumor sizes are shown.
Lysates were prepared and blotted with the indicated antibodies.
Accordingly, AKT inhibition did not suppress Rac1 activity.
These results were verified with a second AKT inhibitor, MK-2206.
Consistent with the differential effects on ERK signaling, we observed that PI3K inhibition led to greater up-regulation of the proapoptotic protein BIM BIMa critical inducer of apoptosis whose protein expression is normally suppressed by ERK-mediated phosphorylation and degradation.
AKT inhibitors fail to down-regulate ERK signaling and induce apoptosis.
Lysates were prepared and blotted with the indicated antibodies.
Independent experiments were performed at least three times, and a representative result is shown.
After 30 min cells were lysed, and Rac-GTP levels were determined with a PAK1-binding domain pull-down assay.
Independent experiments were performed twice for BT474 cells and three times for T47D />The percentage of cells undergoing apoptosis, as measured by annexin V positivity, is shown relative to untreated cells.
Lysates were prepared and probed with the indicated antibodies.
Independent experiments were performed three times, and a representative result is shown.
Thus, we endeavored to identify which other PI3K effector likely containing a PH domain regulated Rac activation.
Rac activation is directly mediated by Rac-GEFs, a class of molecules that promote the exchange of GDP for GTP.
A recent study indicated that the PH domain-containing GEF, P-Rex1, is overexpressed in numerous breast cancers, particularly in primary tumors or cell lines of luminal origin, compared with normal mammary cells.
Moreover, in these cells P-Rex1 is responsible for PI3K-dependent Rac activation, although its role in regulating ERK had not been evaluated.
Thus, we hypothesized that P-Rex1—dependent activation of Rac may be dependent on PI 3,4,5 P3 levels on the membrane and thus would be sensitive to PI3K inhibitors but not AKT inhibitors.
To determine the role of P-Rex1 in the regulation of ERK signaling, we used RNA interference to deplete P-Rex1 levels.
As expected, tetracycline-induced depletion of P-Rex1 inhibited Rac1 activity.
Consistent with our results above, depletion of P-Rex1 by either siRNA or shRNA suppressed MAPK signaling, including c-RAF, MEK, and ERK.
P-Rex1 expression levels correlate with sensitivity to PI3K inhibition.
After 30 min cells were lysed, and Rac-GTP levels were determined with a PAK1-binding domain pull-down assay.
Independent experiments were performed twice, and a representative result is shown.
Lysates were prepared and probed with the indicated antibodies.
Results were confirmed by three independent experiments, and a representative result is shown.
C Cells were transfected with control or P-Rex1-targeted siRNA for 48 and 72 h.
Lysates were prepared and probed with the indicated antibodies.
Independent experiments were performed at least 3 times for T47D and twice for MCF7, and a representative result is shown.
D Cells were lysed, and lysates were probed with P-Rex1 antibody; GAPDH served as loading control.
Results were confirmed by independent lysates, and a representative result is shown.
E Cells were treated with 1 μM GDC-0941 for the indicated times, and lysates were probed with the indicated antibodies.
Independent experiments were performed at least three times, and https://chmall.ru/100/dar-al-hae-100-ml.html result is shown.
Cells were lysed after 30 min, and Rac-GTP levels were determined with a PAK1-binding domain Карта памяти Pretec SDC assay.
The average tumor sizes are shown.
H CAL-51 tumors were harvested 2 h after the last treatment as indicatedand lysates were prepared and blotted with the indicated antibodies.
As previously reportedthere is a spectrum of expression of levels of P-Rex1 across breast cancer cell lines.
Interestingly, P-Rex1 was expressed in all of the cell lines in which PI3K inhibition led to suppression of the ERK pathway.
Conversely, in three breast cancer cell lines—MDA-MB-453 HER2 amplified and PIK3CA mutantBT-20 PIK3CA mutantand CAL-51 PIK3CA mutant —that had undetectable levels of P-Rex1PI3K inhibition did not suppress Rac1 activation or ERK phosphorylation.
Indeed, there was no correlation between Rac-GTP and P-Rex1 levelsunderscoring the finding that PI3K-dependent activation of Rac, not absolute Rac-GTP levels, correlate with PI3K-dependent regulation of ERK signaling.
Unlike the MCF7 xenograft tumors, the growth of CAL-51 tumors was minimally impacted by PI3K inhibitionand as expected, the PI3K inhibitor did not impair ERK signaling in low P-Rex1 tumors in vivo.
However, the combination of PI3K inhibitor and MEK inhibitor induces down-regulation of both AKT and ERK pathways and tumor regression.
Notably, examination of P-Rex1 expression levels among a panel of HER2 amplified and PIK3CA mutant breast cancer cells revealed that those cell lines that express low levels of P-Rex1 were less sensitive to the antiproliferative effects of GDC-0941 than high P-Rex1—expressing cells.
Taken together, these data demonstrate that PI3K-dependent regulation of ERK signaling is mediated through P-Rex1.
Consequently, P-Rex1 expression levels may serve as a biomarker to predict which HER2 amplified and PIK3CA mutant breast cancers have ERK signaling under the regulation of PI3K and accordingly may help identify those cancers that will be most susceptible to single-agent PI3K inhibitors in the clinic.
Interestingly, ERK down-regulation had been observed also in patients treated with XL147, a potent inhibitor of the class I PI3K family memberssupporting the observation that in some cancers PI3K signaling controls ERK signaling.
However, the regulation of ERK signaling in a PI3K-dependent manner via P-Rex1 has not been previously described.
Although our data suggest that ERK is one key downstream effector of PI3K-dependent Rac1 activity in these tumors, we cannot exclude the possibility that Rac1 may also regulate signaling pathways in addition to Https://chmall.ru/100/kronshteyn-na-stenu-vlk-trento-36.html that contribute to the survival of these cells.
In this study we identified P-Rex1 as the Rac-GEF that regulates PI3K-mediated ERK pathway activation.
We think it is unlikely that other Rac-GEFs with a PH domain, such as P-Rex2a, exert a redundant role in activating the ERK pathway in these cells for several reasons: i P-Rex1 is the only Rac-GEF controlling Rac activity when overexpressed ; ii P-Rex2a is almost undetectable in cells overexpressing P-Rex1 ; and iii P-Rex2a regulates PI3K pathway through inhibition of PTEN independently of its Rac-GEF activity.
Our finding that expression levels of P-Rex1 correlate with sensitivity to GDC-0941 suggests that P-Rex1 expression may serve as a clinical biomarker predicting clinical benefit from PI3K inhibitors.
Analysis of patient specimens from ongoing clinical trials of PI3K inhibitors will be needed to assess this hypothesis.
Although these data demonstrate that ERK activation is controlled by PI3K in breast cancers that express high levels of P-Rex1, we do not have data to determine whether ERK activation is under control of Rac in breast cancers that low levels of P-Rex1.
It is quite possible that low P-Rex1 breast cancers use Rac-independent pathways to control ERK activation.
To по этому сообщению initial surprise, PI3K inhibitor-induced suppression of the ERK pathway seems to be largely independent of RAS.
In fact, whereas GDC-0941 treatment results in inhibition of both ERK and AKT activation, RAS activity was modestly increased.
Additionally, other regulators of RAS activation may be regulated by PI3K, such as a RAS-GAP that contains a PH domain.
Our data support the notion that inhibition of PI3K is qualitatively different from AKT inhibition in some cancers.
Our finding that AKT inhibitors do not suppress ERK and are inferior to PI3K inhibitors in terms of induction of the proapoptotic molecule BIM and apoptosis suggests that PI3K inhibitors may have superior antitumor activity compared with AKT inhibitors for certain cancers.
However, the functional differences between PI3K and AKT inhibitors may extend beyond the regulation of P-Rex1 and ERK signaling.
Previously, others reported that the PI 3,4,5 P3 produced by PI3K can activate AKT-independent signaling pathways that are critical for cancer growth.
For example, it has been shown that the PDK1 substrate SGK3 can play a role in promoting PI3K-dependent viability in some breast cancers harboring PIK3CA mutations.
In early clinical trials, BTK inhibitors are yielding promising activity in lymphoid malignancies .
Thus, in several cancers, PI3K seems to control oncogenic pathways other than just AKT.
Interestingly, in contrast to our findings, previous studies revealed activation of ERK signaling after more prolonged treatment with PI3K inhibitors in HER2 amplified breast cancers .
In the PIK3CA mutant T47D and MCF7 breast cancer cells, both Rac and ERK signaling remained suppressed for up to 24 h.
In contrast, both Rac and ERK signaling recovered after 24 h of treatment with GDC-0941 in BT474 cells.
Although these findings do not explain why BT474 cells recover Rac activation, these results continue to support a tight relationship between Rac and ERK activation among all of these breast cancer cell lines.
Thus, it seems that potent inhibition of mTOR may have a greater capacity than PI3K inhibitors to activate ERK in HER2 amplified breast cancers.
However, the clinical significance of this distinction remains to be determined.
Our findings raise the question of why ERK signaling is regulated by a PI3K-dependent mechanism in many breast cancer cell lines, particularly those without RAS mutations.
In these cancers, there may be less input into ERK by RTKs, especially because PI3K activation normally suppresses RTK activation.
In this scenario, those clones that effectively used PI 3,4,5 P3 to also activate the ERK signaling pathway i.
This may explain the relatively high expression levels of P-Rex1 observed in many luminal breast cancers.
Furthermore, these results provide a rationale for assessing P-Rex1 as a biomarker in clinical trials of breast cancers treated with PI3K inhibitors.
Lysates were prepared as previously described.
Antibodies against AKT and RAF-1 were purchased from Santa Cruz Biotechnology.
Total RAS and Rac were from Millipore.
RAS and Rac Activity Assay.
RAS and Rac1 activation assays Декоративное покрытие Бирсс №31 Белая, 25 кг performed using RAS and Rac Activity Assay kit Millipore.
Briefly, cell lysates were immunoprecipitated with a GST fusion protein corresponding to the RAS-binding domain of Raf-1 bound to glutathione-agarose to identify RAS-GTP or the p21-binding domain of human PAK1 bound to glutathione-agarose to identify Rac1-GTP.
GTPγS and GDP protein loading were used for positive and negative controls, respectively.
For xenograft experiments, a suspension of 5—10 × 10 6 cells was inoculated s.
The mice were maintained in laminar airflow units under aseptic conditions, and the care and treatment of experimental animals were in accordance with institutional guidelines.
GDC-0941 was dissolved in 0.
AZD6244 was dissolved in 0.
PIK3CA mutation and HER2 amplification status for cell lines was obtained from the Sanger Institute COSMIC database, drug sensitivity data, represented as IC 50, were obtained from Supplementary Data 1 of Garnett et al.
Cell lines were classified into two groups—high and low—depending on the levels of P-Rex1 they expressed, and a two-tailed Student t test was Крем регенерирующий Deb-Stoko Classic, 100 мл on the IC 50.
The authors declare no conflict of interest.
This article is a PNAS Direct Submission.
This article contains supporting information online at.
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Радиатор стальной ELSEN ERK 21 600 2600

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