CN110734920A - lung cancer detection, treatment and prognosis targets and application - Google Patents
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Abstract
lung cancer cell drug targets, the drug targets are peroxiredoxin 2, the sequence of the drug targets is shown in a sequence table SEQ ID NO 1. the invention defines the molecular mechanism of the non-small cell lung cancer and a plurality of regulation targets Akt, p-Akt, mTOR, p-mTOR, Cyclin D1 and P70S6k. the invention provides a new treatment target PRDX2 for treating the non-small cell lung cancer, defines the relationship between the change of the new target PRDX2 and the non-small cell lung cancer, has the prediction function of , defines the relationship between the change of the new target PRDX2 and the metastasis and invasion of the non-small cell lung cancer, and has the prognosis function of .
Description
Technical Field
The invention belongs to the technical field of biomedicine, and relates to lung cancer (NSCLC) detection, treatment and prognosis targets and application.
Background
Although NSCLC has made major progress in the last 20 years, its 5-year survival rate has been as low as 15%, and local recurrence, metastasis and drug resistance are important factors affecting the prognosis of NSCLC patients, it has been reported that about 79% of NSCLC patients have developed secondary metastases, such as brain metastases, and even metastatic disease at the time of diagnosis, and therefore, it is necessary to explore the molecular mechanisms of non-small cell lung cancer and to find new therapeutic targets for treating non-small cell lung cancer.
Disclosure of Invention
The invention provides novel lung cancer (NSCLC) detection, treatment and prognosis targets and application aiming at the problems in the traditional lung cancer treatment process.
Peroxidases (PRDXs) are -class thiol-specific antioxidant enzymes with H-scavenging activity2O2Among the common types of cancer diseases, carcinogenic mechanisms are activation of various signaling pathways and alteration of transcription factors caused by oxidative stress.
Peroxiredoxin 2 (PRDX 2) is an important member of the PRDXs family, can scavenge superoxide and Reactive Oxygen Species (ROS) in cells, regulate redox states and participate in various cell biological functions.
The research of the invention proves that PRDX2 has abnormal expression in lung cancer and proves that PRDX2 plays an important role in cell proliferation, death and drug sensitivity of the lung cancer.
The invention provides that PRDX2 has biological effect in the development of non-small cell lung cancer (NSCLC), and PRDX2 can be used as a biological marker for lung cancer. The sequence is as follows:
ggcgctgaga acgcgggtcc acgcgtgtga tcgtccgtgc gtctagcctt tgcccacgcagctttcagtc atggcctccg gtaacgcgcg catcggaaag ccagcccctg acttcaaggc cacagcggtggttgatggcg ccttcaaaga ggtgaagctg tcggactaca aagggaagta cgtggtcctc tttttctaccctctggactt cacttttgtg tgccccaccg agatcatcgc gttcagcaac cgtgcagagg acttccgcaagctgggctgt gaagtgctgg gcgtctcggt ggactctcag ttcacccacc tggcttggat caacaccccccggaaagagg gaggcttggg ccccctgaac atccccctgc ttgctgacgt gaccagacgc ttgtctgaggattacggcgt gctgaaaaca gatgagggca ttgcctacag gggcctcttt atcatcgatg gcaagggtgtccttcgccag atcactgtta atgatttgcc tgtgggacgc tccgtggatg aggctctgcg gctggtccaggccttccagt acacagacga gcatggggaa gtttgtcccg ctggctggaa gcctggcagt gacacgattaagcccaacgt ggatgacagc aaggaatatt tctccaaaca caattaggct ggctaacgga tagtgagcttgtgcccctgc ctaggtgcct gtgctgggtg tccacctgtg cccccacctg ggtgccctat gctgacccaggaaaggccag acctgcccct ccaaactcca cagtatggga ccctggaggg ctaggccaag gccttctcatgcctccacct agaagctgaa tagtgacgcc ctcccccaag cccacccagc cgcacacagg cctagaggtaaccaataaag tattagggaa aggtg。
the siRNA interference for down-regulating PRDX2 can obviously inhibit the proliferation, migration and invasion of A549 and H1299 cells and reduce the activity of MMP 9.
Silencing PRDX2 can obviously reduce phosphorylation of Akt and mTOR and expression of downstream proteins Cyclin D1 and p70S6 k.
PRDX2 plays a role in promoting cancer in the development process of NSCLC and is a potential therapeutic target for NSCLC treatment.
After siRNA interferes PRDX2, the primer sequence for detecting PRDX2 RNA level is
Forward direction: 5'-CCTTCAAAGAGGTGAAGCTG-3' the flow of the air in the air conditioner,
and (3) reversing: 5'-GTTGCTGAACGCGATGAT-3' are provided.
The invention provides a specific role of PRDX2 in the growth and invasion of non-small cell lung cancer. The down-regulation of PRDX2 can obviously inhibit the proliferation, migration and invasion of NSCLC cells and promote the apoptosis. In addition, silencing of PRDX2 decreased activation of the Akt/mTOR signaling pathway in NSCLC cells. PRDX2 has carcinogenic effect in the development process of NSCLC, and PRDX2 can be used as a potential target for NSCLC treatment.
Compared with the prior art, the invention has the advantages and positive effects that:
1. the molecular mechanism and a plurality of regulation targets Akt, P-Akt, mTOR, P-mTOR, CyclinD1 and P70S6k of the non-small cell lung cancer are determined.
2. Provides a new therapeutic target PRDX2 for treating the non-small cell lung cancer.
3. The relation between the change of the new target PRDX2 and the non-small cell lung cancer is determined, and the prediction effect of is realized.
4. The relation between the change of a new target PRDX2 and the metastasis and invasion of the non-small cell lung cancer is determined, and the prognostic effect of is achieved.
Drawings
Figure 1 shows that in vitro knockout of PRDX2 inhibits NSCLC cell proliferation.
A549 and H1299 cells were transfected with siRNA-PRDX2 (si-PRDX2) and siRNA negative controls (si-NC) were used as negative controls. A. After 24h of transfection, the expression of PRDX2 mRNA was detected by RT-PCR. B. Western blot was used to examine the relative expression of PRDX2 protein in sirna 48 h transfected NSCLC cells. Two sets of cell viability CCK8 assays were performed C, D on a549 (C), H1299 (D) cells. Cell proliferation was detected by colony formation. P < 0.05.
Figure 2 shows that silencing PRDX2 inhibits migration and invasion of NSCLC cells.
A. Cell migration of sirna-transfected a549 and H1299 cells was assessed using a scratch assay. The cells were assayed for migration (C) and invasion (D) 24h after transfection of sirna by the Transwell method. MMP9 activity was measured in a549 and H1299 cells after sirna transfection. P <0.05
FIG. 3 shows that down-regulation of PRDX2 promotes apoptosis by modulating the Bcl-2/Bax axis and Caspase cascade.
A. And detecting the apoptosis of A549 and H1299 cells after silencing PRDX2 by using a Hoechst33342/PI staining method. B. Western blot is used for detecting the expression conditions of apoptosis-related proteins Bcl-2, Bax, cleared-Caspase 3 and cleared-Caspase 9. P < 0.05.
FIG. 4 shows that down-regulation of PRDX2 inhibits activation of Akt/mTOR signaling pathway in NSCLC cells.
48H after transfection, expression of Akt, P-Akt, mTOR, P-mTOR, Cyclin D1 and P70S6k proteins in A549 and H1299 cells after transfection of si-PRDX2 or si-NC. P < 0.05.
Detailed Description
In order to provide a clearer understanding of the above-mentioned objects, features and advantages of the present invention, the present invention will be described below in with reference to specific embodiments.
In the following description, numerous specific details are set forth in order to provide a thorough understanding of the present invention, however, the present invention may be practiced in other ways than those specifically described herein, and thus the present invention is not limited to the specific embodiments of the present disclosure.
Example 1
Materials and methods
Cell culture and transfection
Human non-small cell lung cancer cell lines A549 and H1299 were obtained from the cell bank of Chinese academy of sciences (Shanghai, China), and cultured in a mixed medium of DMEM medium (Hyclone) and 10% serum (Gibco), 100U/ml penicillin (sigma) and 100 mg/ml streptomycin (sigma) at 37 ℃ and 5% carbon dioxide. After reaching 80% fusion, siRNAs were transfected into A549 and H1299 cells using Lipofectamine 2000 (Invitrogen, Carlsbad, CA, USA) as described in the instructions, inhibiting PRDX2 synthesis, and siR-Ribo Negative Control (Ribobio) as Negative Control (si-NC).
Real-time quantitative polymerase chain reaction (qRT-PCR)
Total RNA was extracted from siRNAs transfected NSCLC cells using an ultrapure RNA kit (CWBIO, Beijing, China) and reverse-transcribed to cDNA by a HiFiScript cDNA Synthesis kit (CWBIO). PCR was performed with FastSYBR Cocktail (CWBIO) on ABI 7500 Rapid systems (applied biosystems, Foster, CA). The present study used the following primers PRDX2, 5'-CCTTCAAAGAGGTGAAGCTG-3' (forward) and 5'-GTTGCTGAACGCGATGAT-3' (reverse), β -actin was used as an internal reference, 5-CCCGAGCCGTGTTTCCT-3 (forward) and 5-GTCCCAGTTGGTGACGATGC-3 (reverse). 2-ΔΔCtThe method was used to calculate the relative expression of PRDX 2.
Immunoblot analysis
After 48 h of sirna transfection, 6-well plates were placed on ice and cells were lysed in RIPA lysate (CWBIO), protein concentration was determined using BCA protein kit (CWBIO), 20 μ g of protein isolated from each sample was WB detected using 10% SDS PAGE gel and polyvinylidene fluoride membrane (PVDF;5% skim milk was blocked for 1 h, incubated with anti-4 ℃ overnight, and then incubated with the corresponding hrp-conjugated secondary antibody; ECL kit (Millipore) showed protein bands, which were quantitated using Image Lab software (Bio-Rad, USA).
The main antibodies (reagents for detecting the expression of each substance) used in this example were anti-prdx 2 (dilution 1:1000; cat No. 10545-2-AP, anti-bcl-2 (dilution 1:1000; cat No. 12789-1-AP), anti-bax (dilution 1:1000; cat No. 50599-2-Ig), anti-Akt (dilution 1:1000; cat No. 10176-2-AP, anti-p-Akt (dilution 1:1000; cat No. 66444-1-Ig), anti-mtor (dilution 1:1000; cat No. 20657-1-AP) and GAPDH (dilution 1:1000; cat No. 60004-1-Ig), anti-clear caspase3 (dilution 1:1000; cat No. 9661), anti-clear caspase 9 (diluted 1:1000; cat No. 9505) and anti-p-mtor (dilution 1:1000; cat No. 2971).
CCK8 experiment
NSCLC cells synthesized by PRDX2 were transfected with siRNAs and plated for 24 hours in 96-well plates at a cell density of 3000 cells per well. Incubate at 37 ℃ for various times (0, 24, 48 and 72 h). CCK8 reagent (10. mu.l/well) was incubated at 37 ℃ for 1 h and absorbance was measured at 450 nm.
Colony formation assay
24h after transfection with interfering siRNA, the cells were digested with 0.25% trypsin to prepare a cell suspension, and then the cells were transferred to a 35mm petri dish containing 5ml of medium at a concentration of 300 cells/dish. After incubation for 1-2 weeks at 37 ℃, cells were washed with PBS, fixed for 30min with 4% paraformaldehyde, stained for 30min with 0.1% crystal violet, rinsed slowly with tap water, and air dried. Colonies were counted and photographed under an optical microscope.
Scratch test
Cells were seeded in 6-well plates 24h after transfection of interfering sirnas. When the density of the fused cells reached 100%, a 200. mu.l pipette tip was used to scratch out the cells, and the scratched-out cells were washed out with PBS. After the addition of the medium, the cells were incubated at 37 ℃ for 24 hours, and the Image of the cells was taken with an optical microscope and the scratch closure rate was analyzed with Image J software.
Transwell experiment
Cell invasion or migration assays were performed with Transwell chambers (microwells) pre-coated or uncoated with matrix gel, respectively. Non-small cell lung cancer cell transfection interfering siRNA was collected and suspended in serum-free medium 24 hours later, 100. mu.l cell suspension cells (1X 10)5) Added to the upper chamber, and 500. mu.l of DMEM medium containing 10% serum was added to the lower chamber. After incubation at 37 ℃ for 24h, the upper chamber was wiped free of residual cells with a cotton swab. Migrated or invaded cells were fixed with 4% paraformaldehyde for 30min and stained with 0.1% crystal violet for 20 min. 5 microscope-photographed views of migration or invasion were randomly selected for cell counting (magnification x 100).
Gelatin zymogram detection analysis
Sirna 24H transfected a549 and H1299 cells were washed 3 times with serum free DMEM and cultured with serum free DMEM at 37 ℃ for 24H. The supernatant was collected and electrophoresed on a 10% SDS-PAGE gel containing 0.5mg/ml gelatin. After electrophoresis, the gel was stained with 0.25% Coomassie Brilliant blue R250 for 4h at room temperature. After decolorization at room temperature, the gel was scanned by an image scanner (Ahmad Sohm, USA) and analyzed by IMAGISOANT TL V2003 software
Hoechst33342/PI staining experiment
24h after transfection of siRNAs, non-small cell lung cancer cells were collected, stained with Hoechst33342 (10. mu.l; Beyotime, Shanghai, China) for 5-15 min at 37 ℃, stained with PI (5. mu.l; Beyotime) for 10 min at room temperature in the dark, observed with a fluorescence microscope and counted.
Statistical analysis
Experimental data are presented as mean ± standard deviation of at least three independent experiments. Statistical analysis was performed in this study using GraphPad software 7.0(GraphPad inc., USA). Differences between the two groups were analyzed by t-test, and differences between the three or more groups were compared by one-way anova. P <0.05 was considered statistically significant for the differences.
Results
Down-regulation of PRDX2 inhibits proliferation of NSCLC cells
To investigate the biological role of PRDX2 in NSCLC progression, we used siRNA-PRDX2 to interfere with NSCLC cell lines a549 and H1299 to silence their expression as shown in fig. 1A and B, siRNA-PRDX2 significantly inhibited PRDX2 expression at both the mRNA and protein levels CCK8 experiments showed that silencing PRDX2 inhibited survival of a549 cells compared to the NC group (fig. 1C), as well as H1299 cells transfected with siRNA-PRDX2 had significantly reduced survival (fig. 1D), compared to these results , siRNA-PRDX2 also reduced the colony forming ability of a549 and H1299 cells compared to the control group (fig. 1E), which showed that deletion of PRDX2 inhibited proliferation of non-small cell lung cancer cells in vitro.
Silencing PRDX2 expression can inhibit migration and invasion of NSCLC cells
The influence of PRDX2 on the transfer capacity of the non-small cell lung cancer cells is researched by adopting a scratch test. As shown in fig. 2A, down-regulation of PRDX2 significantly inhibited the ability of a549 and H1299 cells to migrate to blank spaces. Similar to the above, the transwell experiment also found that in a549 and H1299 cells, siRNA-PRDX2 induced cell migration significantly decreased (fig. 2B). The invasive capacity of a549 and H1299 cells transfected with siRNA-PRDX2 was significantly reduced compared to the control group (fig. 2C).
Given the critical role of MMP9 in cell adhesion and invasion, we examined MMP9 activity using gelatinase profiling. As shown in fig. 2D, down-regulation of PRDX2 significantly reduced MMP9 activity in a549 and H1299 cells. Taken together, our data indicate that deletion of PRDX2 may inhibit the migration and invasive capacity of NSCLC cells by down-regulating the activity of MMP 9.
Down-regulation of PRDX2 promotes apoptosis of NSCLC cells
It is generally believed that escape of death is the major feature of tumor cells, therefore, we proceeded to step studies on the effect of PRDX2 on NSCLC cell apoptosis as shown in fig. 3A, silencing PRDX2 promoted apoptosis of NSCLC cells, and knocking down the apoptosis rate of PRDX2 cells significantly higher than that of the NC control group, therefore, step studies on the mechanism of siRNA-PRDX2 induced apoptosis of NSCLC cells our data showed that silencing PRDX2 significantly down-regulated the expression of the anti-apoptotic protein Bcl-2 in a549 and H1299 cells, up-regulated the expression of the pro-apoptotic protein Bax (fig. 3B). furthermore, the activation of Caspase3 and Caspase 9, which play a critical role in the process of apoptosis, was activated by siRNA-PRDX2 in both a549 and H1299 cells (fig. 3B).
Silencing of PRDX2 inhibits activation of Akt/mTOR signaling pathway in NSCLC cells
The Akt/mTOR signaling pathway plays an important role in physiological processes such as cell proliferation, differentiation, invasion and survival. The Akt/mTOR signaling pathway is overactivated in tumors and is involved in tumor progression, including NSCLC. Therefore, we used a western blot analysis to assess the effect of PRDX2 on the NSCLC Akt/mTOR signaling pathway. As shown in figure 4, silencing PRDX2 significantly reduced the protein levels of phosphorylated Akt in a549 and H1299 cells without affecting total Akt expression. In addition, the expression of Cyclin D1 and p70S6k, downstream proteins that regulate cell proliferation, were examined. Compared with the control group, the cell of the siRNA-PRDX2 obviously inhibits the activation of the cell signaling pathway (FIG. 4). In conclusion, the results of our research show that the silencing PRDX2 can inhibit the activation of the mTOR/Akt signaling pathway of the non-small cell lung cancer cell.
Conclusion
Besides having a proliferation effect, the apoptosis also plays a crucial role in the occurrence and development of tumors, the apoptosis disorder is which is a main characteristic of tumor cells, PRDX2 has the effect of regulating the apoptosis of the tumor cells, and the reduction of the expression of PRDX2 leads to the increase of the apoptosis of NSCLC cells.
In addition, activated caspase 9 participates in initiation of series apoptosis events, and activated caspase3 is a key executor of apoptosis, PRDX2 is inhibited to down-regulate Bcl-2 expression and up-regulate Bax expression, and clear caspase3 and clear caspase 9 expression in NSCLC cells, which shows that PRDX2 regulates apoptosis of NSCLC cells by regulating Bcl-2/Bax axis and caspase cascade reaction.
Akt/mTOR signaling pathway is used as an important mechanism participating in cell physiological process and tumor progression and is hot spots in tumor treatment strategy, activation of Akt/mTOR signaling pathway can regulate and control expression of downstream effector factors such as Cyclin D1, p70S6k and the like participating in cell function, more importantly, PRDX2 regulates and controls drug resistance of colon cancer cells to 5-FU by regulating and controlling Akt signaling pathway.
In the development process of NSCLC, PRDX2 has cancer promoting effect, and the down regulation of PRDX2 can obviously inhibit the proliferation, migration and invasion of NSCLC cells and promote the apoptosis. More importantly, silencing PRDX2 can inhibit activation of Akt/mTOR signaling pathway in NSCLC cells. Therefore, PRDX2 can be a potential therapeutic target for NSCLC treatment.
The above description is only a preferred embodiment of the present invention, and not intended to limit the present invention in other forms, and any person skilled in the art may apply the above modifications or changes to the equivalent embodiments with equivalent changes, without departing from the technical spirit of the present invention, and any simple modification, equivalent change and change made to the above embodiments according to the technical spirit of the present invention still belong to the protection scope of the technical spirit of the present invention.
SEQUENCE LISTING
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cacagcggtg gttgatggcg ccttcaaaga ggtgaagctg tcggactaca aagggaagta 180
cgtggtcctc tttttctacc ctctggactt cacttttgtg tgccccaccg agatcatcgc 240
gttcagcaac cgtgcagagg acttccgcaa gctgggctgt gaagtgctgg gcgtctcggt 300
ggactctcag ttcacccacc tggcttggat caacaccccc cggaaagagg gaggcttggg 360
ccccctgaac atccccctgc ttgctgacgt gaccagacgc ttgtctgagg attacggcgt 420
gctgaaaaca gatgagggca ttgcctacag gggcctcttt atcatcgatg gcaagggtgt 480
ccttcgccag atcactgtta atgatttgcc tgtgggacgc tccgtggatg aggctctgcg 540
gctggtccag gccttccagt acacagacga gcatggggaa gtttgtcccg ctggctggaa 600
gcctggcagt gacacgatta agcccaacgt ggatgacagc aaggaatatt tctccaaaca 660
caattaggct ggctaacgga tagtgagctt gtgcccctgc ctaggtgcct gtgctgggtg 720
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Claims (7)
1, lung cancer cell drug targets, characterized in that, the drug target is peroxiredoxin 2, the sequence is shown in sequence table SEQ ID NO. 1.
2. The lung cancer cell drug target of claim 1, wherein the peroxoredoxin 2 is inhibited by a siRNA having the sequence 5 '-CCTTCGCCAGATCACTGTTAA-3'.
3. The lung cancer cell drug target according to claim 2, wherein the detection primer sequence used after siRNA inhibits peroxiredoxin 2 is
Forward direction: 5'-CCTTCAAAGAGGTGAAGCTG-3' the flow of the air in the air conditioner,
and (3) reversing: 5'-GTTGCTGAACGCGATGAT-3' are provided.
4. The application of siRNA for inhibiting redox protein 2 in preparing a medicine for treating lung cancer is characterized in that the siRNA has a sequence of 5 '-CCTTCGCCAGATCACTGTTAA-3'.
5. The application of the inhibitor of the peroxoredoxin 2 in the preparation of the agent for inhibiting the proliferation, migration and/or invasion of lung cancer cell strains A549 and H1299 is characterized in that the inhibitor is siRNA with the sequence of 5 '-CCTTCGCCAGATCACTGTTAA-3'.
6. Use of a reagent for detecting the amount of peroxiredoxin 2 secretion in an individual for the preparation of a diagnostic reagent or kit for diagnosing whether the individual to be tested has lung cancer.
7. The application of siRNA gene or protein for inhibiting redox protein 2 or synergist thereof in preparing medicine is characterized in that the medicine is used for preventing and treating lung cancer.
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