A molecular marker for head and neck squamous cell carcinoma and its application

Abstract

The present invention discloses a molecular marker for head and neck squamous cell carcinoma and its application. The molecular marker contains SMG6 protein. The present invention also provides the application of the molecular marker for head and neck squamous cell carcinoma in auxiliary diagnosis products, prognosis prediction models, as a target in screening anti-head and neck squamous cell carcinoma drugs, and as a head and neck squamous cell carcinoma tumor inhibitor. The present invention has developed a group of molecular markers for predictive prognosis diagnosis of HNSCC. The present invention analyzes the prognostic significance of SMG6 protein in HNSCC and finds that increased expression of SMG6 protein is positively correlated with a good prognosis of HNSCC patients. The present invention confirms through in vivo and in vitro experiments that SMG6 protein plays a role in inhibiting tumors in HNSCC.

Description

Technical Field

[0001] The present invention belongs to the technical field of biomedicine, and in particular relates to a molecular marker for head and neck squamous cell carcinoma and an application thereof. Background Art

[0002] Head and neck squamous cell carcinoma (HNSCC) accounts for the majority of head and neck cancers, causing a large number of deaths worldwide each year. Since the head and neck are home to many key organs that control important physiological functions, a large number of tissues such as muscles, bones, blood vessels and nerves are concentrated in this small space and are intertwined. Traditional treatments such as surgery, chemotherapy and radiotherapy are difficult to completely cure the disease. Compared with traditional treatments, NK immune cells have more precise targeting effects, which can achieve the effects of clearing cancer cells, preventing recurrence and inhibiting metastasis. However, due to the high invasiveness and heterogeneity of HNSCC, the prognosis of patients is still poor, and the disease morbidity and mortality rates are increasing year by year. TNM staging and histological grading are closely related to the prognosis of HNSCC, and are also the main basis and foundation for the development of treatment plans such as prognostic evaluation, immunotherapy, radiotherapy and chemotherapy. However, HNSCC patients may show different clinical pathological characteristics, indicating that traditional clinical pathological staging may not be completely accurate. Therefore, the discovery of new prognostic biomarkers is crucial to improving the quality of life of HNSCC patients. Summary of the invention

[0003] The purpose of the present invention is to solve at least one of the technical problems existing in the prior art. The technical problem to be solved by the present invention is that there is a certain lag in the means of prognostic diagnosis of head and neck squamous cell carcinoma in the prior art, thereby proposing a molecular marker for the diagnosis and treatment of head and neck squamous cell carcinoma and its application. The present invention comprehensively expounds the important role of SMG6 protein in HNSCC, that is, it is a biomarker closely related to prognostic diagnosis. The present invention analyzes the prognostic significance of SMG6 protein in HNSCC and finds that increased expression of SMG6 protein is positively correlated with a good prognosis of HNSCC patients. The present invention confirms through in vivo and in vitro experiments that SMG6 protein plays a role in inhibiting tumors in HNSCC.

[0004] The technical solution of the present invention is as follows:

[0005] A molecular marker for head and neck squamous cell carcinoma, wherein the molecular marker is SMG6 protein.

[0006] Preferably, the sequence of the SMG6 protein is as shown in SEQ ID NO:1.

[0007] The second aspect of the present invention provides an application of a head and neck squamous cell carcinoma molecular marker in a head and neck squamous cell carcinoma auxiliary diagnosis product.

[0008] Specifically, the auxiliary diagnostic product is a test kit or a test paper.

[0009] The above-mentioned molecular markers of head and neck squamous cell carcinoma are made into auxiliary diagnostic products such as kits or test strips for auxiliary diagnosis of head and neck squamous cell carcinoma.

[0010] The third aspect of the present invention provides an application of a molecular marker for head and neck squamous cell carcinoma in constructing a prognosis prediction model for head and neck squamous cell carcinoma.

[0011] Specifically, the molecular markers were made into a prognostic prediction model for the prognosis prediction of head and neck squamous cell carcinoma.

[0012] A fourth aspect of the present invention provides a use of a head and neck squamous cell carcinoma molecular marker as a head and neck squamous cell carcinoma tumor suppressor.

[0013] Specifically, targeted therapeutic drugs can be designed for specific tumor suppressor genes such as SMG6 protein. Therapeutic drugs targeting SMG6 can be designed in the following ways:

[0014] mRNA vaccine: By designing an mRNA vaccine targeting the SMG6 protein, the patient's immune system is stimulated to produce SMG6 protein, thereby increasing its content.

[0015] Small molecule inducers: Study the regulatory mechanism of SMG6 protein expression, discover small molecule substances that can induce SMG6 protein expression, and design drugs that can activate SMG6 protein expression through drug screening and optimization.

[0016] The fifth aspect of the present invention provides a head and neck squamous cell carcinoma molecular marker as a head and neck squamous cell carcinoma tumor inhibitor application

[0017] The present invention has at least one of the following beneficial effects:

[0018] 1. The present invention develops molecular markers for predictive prognosis diagnosis of HNSCC. The present invention comprehensively explains the important role of SMG6 protein in HNSCC, that is, it is a biomarker closely related to prognosis.

[0019] 2. Through analysis of the prognostic significance of SMG6 protein in HNSCC, the present invention found that increased expression of SMG6 protein was positively correlated with a good prognosis of HNSCC patients.

[0020] 3. The present invention confirms through in vivo and in vitro experiments that SMG6 protein plays a tumor-suppressing role in HNSCC. BRIEF DESCRIPTION OF THE DRAWINGS

[0021] Figure 1 Figure 2 is the correlation between SMG6 protein expression and the survival curve of HNSCC patients.

[0022] Figure 2 This is a diagram showing that SMG6 protein inhibits the proliferation, invasion and migration of HNSCC cells. Figure 2 A in the figure is a Western blot experiment to verify the effect of overexpressing SMG6 in FaDu cells; Figure 2 B in the figure is a clone formation experiment; Figure 2 C in the figure is the CCK8 experiment to detect cell proliferation; Figure 2 D in the figure is an invasion and migration experiment to detect the invasion and migration ability of cells.

[0023] Figure 3 This is a photo of SMG6 protein inhibiting HNSCC tumor growth in a nude mouse subcutaneous tumor formation experiment. DETAILED DESCRIPTION

[0024] In order to make the technical problems, technical solutions and beneficial effects solved by the present invention more clearly understood, the present invention is further described in detail below in conjunction with the accompanying drawings and embodiments. It should be understood that the specific embodiments described herein are only used to explain the present invention and are not used to limit the present invention.

[0025] Example 1

[0026] This embodiment provides a molecular marker for head and neck squamous cell carcinoma, specifically SMG6 protein, namely telomerase binding protein EST1A, the sequence of SMG6 protein is shown in SEQ ID NO: 1:

[0027]

[0028] Nonsense-mediated mRNA decay (NMD) is a cytoplasmic RNA degradation mechanism that detects and degrades mRNAs containing premature termination codons, thereby preventing these abnormal mRNAs from being translated into harmful proteins. Studies have shown that NMD may play a dual role in tumor development. The effect of NMD on tumors depends on the specific context and cell type, and further research is needed to reveal its mechanism of action in tumor development.

[0029] SMG6 protein is a major member of the NMD complex and plays a key role in the NMD process. Specifically, SMG6 protein is involved in cellular transcriptional regulation and RNA degradation ribozymes, and plays an important role in regulating RNA stability and quality control. It is a protein closely related to biological processes such as apoptosis, cell cycle regulation, and RNA degradation pathways. Given the important role of NMD in tumors, it is speculated that SMG6 protein may play an important role in tumors.

[0030] In this example, RNAseq data of the STAR process of the TCGA-HNSC (head and neck squamous cell carcinoma) project were downloaded and sorted from the TCGA database (https: / / portal.gdc.cancer.gov) and data in TPM format were extracted. Statistical analysis was performed using the statistical analysis and visualization software R (4.2.1), including the following R packages: survival[3.3.1], survminer[0.4.9], and ggplot2[3.3.6]. The processing process was to use the survival package to perform a proportional hazard hypothesis test and fit survival regression, and the results were visualized using the survminer package and the ggplot2 package.

[0031] The results are as follows Figure 1 As shown, the blue curve is the overall survival curve of HNSCC patients with low SMG6 protein expression, and the red curve is the survival curve of HNSCC patients with high SMG6 protein expression. It can be seen that HNSCC patients with high SMG6 protein expression have a higher survival rate than HNSCC patients with low SMG6 protein expression. Figure 1 It can be seen that increased SMG6 protein expression is positively correlated with a good prognosis of HNSCC patients.

[0032] Therefore, SMG6 protein can be used as a marker to assist in the diagnosis of HNSCC, and thus can be used in products for assisting the diagnosis of HNSCC.

[0033] Example 2

[0034] The "FaDu cells overexpressing SMG6 in the logarithmic growth phase" used in the following examples were cultured by the following method:

[0035] Human pharyngeal squamous cell carcinoma cells (FaDu) were obtained from the cell bank of the Chinese Academy of Sciences. After receiving the cells, they were cultured and passaged. The specific steps are as follows: Cell medium replacement: Open the biosafety cabinet, disinfect the countertop with 75% ethanol, place the culture flask / dish, pipette, gun tip, etc. on the work surface, and irradiate with ultraviolet light for 30 minutes. Place the DMEM medium containing 10% high-quality fetal bovine serum (GIBCO catalog number: 10566016) in a 37°C water bath to rewarm. After the ultraviolet irradiation, start the experiment, use the gun tip to absorb the old culture medium, add PBS to gently rinse twice, slowly add 5mL10% high-quality fetal bovine serum DMEM medium, and then place the culture dish in the cell culture incubator for continued culture. At the end of the experiment, tidy up the work surface, close the biosafety cabinet, start the ultraviolet disinfection program, and put the reagents back to their original places.

[0036] Cell passaging: Observe the cells under a microscope. If the cell density reaches 90%, the cells need to be passed to a new culture dish. Prepare the required reagents and consumables and place them in a biosafety cabinet for UV disinfection. Reheat the culture medium and trypsin in a 37°C water bath. After UV disinfection, disinfect with alcohol and place in a biosafety cabinet. Remove the old culture medium from the culture dish, add phosphate buffered saline (PBS) to gently rinse twice, add 1mL of trypsin to cover all cells, gently mix and place in a cell culture incubator; after 2 minutes of culture, when the cells in the culture dish begin to become smaller and round, add 2mL of fresh complete culture medium containing serum to terminate the trypsin digestion process; gently blow the cells in the dish with a pipette tip, transfer the cells in the culture dish to a new 15mL centrifuge tube, and centrifuge at 1000rpm for 3 minutes at room temperature; after centrifugation, aspirate the supernatant, add 1mL of fresh complete culture medium to the centrifuge tube, mix and resuspend thoroughly, transfer to a new culture dish with a pipette tip, and slowly add 4mL of fresh complete culture medium, shake the cells using the "8-shaped method", and place the culture dish in a cell culture incubator for continued culture. Clean up the work surface, close the biosafety cabinet, start the ultraviolet disinfection program, and put the reagents back to their original places.

[0037] Infect FaDu cells with lentivirus to construct a cell line overexpressing SMG6: Infect FaDu cells with SMG6 overexpression lentivirus (purchased from GeneCare) to establish a stable cell line overexpressing SMG6. The specific steps are as follows:

[0038] 1. Before cells are infected with lentivirus, screen the appropriate working concentration of puromycin in FaDu cells. The specific operation is as follows: FaDu cells to be passaged are plated in 24-well plates, and the density is controlled at about 30%-50%. After the cells adhere to the wall, different concentrations of puromycin are added to the culture medium, and the cell death is observed under a microscope. By continuously refining the puromycin concentration gradient, the lowest concentration at which all cells die is selected as the most suitable concentration for subsequent experiments.

[0039] 2. One day before the cells are prepared to be infected with lentivirus, FaDu cells are digested with trypsin, centrifuged, resuspended in fresh culture medium, and plated on 6-well plates. Culture continues and the cells are infected with lentivirus when the cell density reaches about 30% the next day.

[0040] 3. Replace the medium in the 6-well plate. Add 1 mL of complete medium to the wells, and add 0.5 μL of 20 μg / mL polybrene. After gently mixing, add SMG6 lentivirus. The required amount of lentivirus is: 2.5 μL for the overexpression control group and 5 μL for the overexpression group. Gently shake the 6-well plate, shake well, and continue to culture in the incubator. Collect the used tips, add 84 disinfectant, and seal for storage.

[0041] 4. After 12 hours of culture, observe the cell status under a microscope and add 1 mL of fresh complete culture medium to the 6-well plate.

[0042] 5. After 72 hours of lentivirus infection, observe the lentivirus infection efficiency under a fluorescence microscope. At this time, digest the cells in the 6-well plate and transfer them to the culture flask for further culture. After all the cells are attached to the wall, add the most suitable concentration of puromycin to remove the cells that are not infected with the lentivirus.

[0043] 6. After the cells are treated with puromycin, they are subcultured and expanded. During this period, the cells are frozen for seed preservation, and the remaining cells are used for subsequent experiments.

[0044] (1) Extraction of proteins from FaDu cells overexpressing SMG6 in the logarithmic growth phase

[0045] 1. Take out the FaDu cells from the incubator and rinse them with pre-cooled phosphate buffered saline (PBS). Repeat this process 3 times.

[0046] 2. After rinsing with PBS, aspirate all the liquid in the dish, add an appropriate amount of protein lysis buffer, place on ice for about 1 minute, use a cell scraper to scrape all the cells from the culture dish as much as possible, and transfer them to a clean 1.5mL EP tube using a pipette tip.

[0047] 3. After vortex mixing, transfer the EP tube to the corresponding hole in the vertical rotating mixer and place it in a 4°C refrigerator for 30 minutes to fully lyse the protein.

[0048] 4. After the rotation mixing is completed, centrifuge at 4°C and 13,000 rpm for 15 minutes.

[0049] 5. After centrifugation, use a pipette tip to transfer the supernatant to a clean EP tube, add loading buffer, boil at 100℃ for 10 min, and store in a -80℃ refrigerator for later use.

[0050] (2) Western Blotting

[0051] 1. Prepare the lower gel solution of electrophoresis gel (New Cyme Color Gel Rapid Kit) according to the ratio of lower gel solution: lower gel buffer: improved coagulant = 2.5mL: 2.5mL: 50μL.

[0052] 2. After inversion and mixing, use a 5mL pipette tip to draw the lower layer of glue solution into the glue plate, and immediately add 1mL of anhydrous ethanol on top of the lower layer of glue solution to flatten it.

[0053] 3. Prepare the upper gel solution according to the ratio of upper gel solution: upper gel color buffer = 0.75mL: 0.75mL. Do not add coagulant at this time.

[0054] 4. At room temperature for about 30 minutes, observe whether the lower layer of gel in the centrifuge tube has solidified. If so, pour out the upper layer of anhydrous ethanol, gently rinse with double distilled water, and then absorb the liquid with filter paper.

[0055] 5. Add 15 μL of improved coagulant to the mixed solution in step 3, invert and mix thoroughly, use a 1 mL pipette tip to draw the upper layer of gel solution into the gel plate, and immediately and slowly insert a 1.5 mm 10-hole comb.

[0056] 6. At room temperature for about 30 minutes, observe whether the upper layer of gel in the centrifuge tube has solidified. If so, electrophoresis can be performed.

[0057] 7. Prepare the electrophoresis solution, install the gel plate, add the electrophoresis solution, pull out the comb, load the samples in the order of protein loading, set the upper gel voltage to 80 volts, run the electrophoresis for 30 minutes, then change to 135 volts, run the electrophoresis for 60 minutes. Observe the markers at this time, and stop the electrophoresis if the protein position to be detected has appeared.

[0058] 8. Determine the cutting range according to the marked position and place the cut gel into the pre-prepared transfer solution.

[0059] 9. Cut 0.22μm PVDF membrane according to the size of the gel, and place it in methanol for activation.

[0060] 10. Place the transfer pad and filter paper on the cathode first, gently transfer the gel to the filter paper, cover the PVDF membrane, remove all bubbles, and cover the filter paper and transfer pad.

[0061] 11. After installation, place it in the transfer tank, add the pre-cooled transfer solution into it, and add ice water around the transfer tank to cool it down.

[0062] 12.200mA constant current electroporation for 2h.

[0063] 13. After the transfer is completed, turn off the power, take out the PVDF membrane, soak it in TBST, and dispose of the gel safely and discard it into the hazardous reagent waste bin.

[0064] 14. Prepare 5% skim milk with TBST and place the PVDF membrane in it. Shake slowly on a shaker at room temperature for 1 h.

[0065] 15. Take out the PVDF membrane, soak it in TBST, and cut the membrane according to the position of the protein to be measured.

[0066] 16. Place the cut PVDF membrane into the prepared primary antibody (prepared according to the antibody: primary antibody dilution ratio of 1:1000) and shake gently in a 4°C refrigerator overnight.

[0067] 17. Remove the PVDF membrane and recover the primary antibody.

[0068] 18. Add TBST and shake rapidly to wash the membrane for 10 min each time, repeat 3 times.

[0069] 19. Discard the TBST, add the corresponding secondary antibody (prepared according to the secondary antibody: TBST solution 1:1000), and shake slowly on a shaker at room temperature for 1.5 h.

[0070] 20. Discard the secondary antibody, add TBST and wash the membrane with rapid shaking for 10 minutes each time, repeat 3 times.

[0071] 21. Prepare chemiluminescent solution in the ratio of A solution: B solution = 1:1, and use the American BIO-RAD multicolor fluorescence and chemiluminescence gel imaging system to detect the results.

[0072] (3) CCK8 proliferation assay

[0073] 1. Digest the FaDu cells overexpressing SMG6 in the logarithmic growth phase, centrifuge at 1000 rpm for 3 min at room temperature, remove the supernatant, and resuspend in fresh complete medium.

[0074] 2. Cell counting: Use a pipette tip to draw 10 μL of cell resuspension into a cell counting plate and insert it into a cell counter for counting.

[0075] 3. After the cells are fully mixed, they are plated in a 96-well plate at a density of 2000 cells / well. 100 μL of culture medium is added to each well. There are 5 replicate wells in each group, and the first, second, third and fourth days are marked.

[0076] 4. Add 150 μL PBS around the outside of the 96-well plate and place it in the incubator.

[0077] 5. At 1, 2, 3, and 4 days of cell culture, add 10 μL of CCK8 reagent to each well marked as the first, second, third, and fourth days, respectively. Gently shake the 96-well plate to mix the culture medium and CCK8 reagent, then place the plate in a cell culture incubator for continued culture.

[0078] 6. After reacting in the incubator for 3 hours, set the multifunctional microplate reader to 450 nm wavelength to detect the OD value and record the data.

[0079] (4) Clone formation experiment

[0080] 1. After digesting the FaDu cells overexpressing SMG6 in the logarithmic growth phase, set the centrifuge speed to 1000 rpm at room temperature for 3 minutes. After centrifugation, use a pipette to remove the supernatant as much as possible, add 1 mL of fresh complete culture medium and mix by pipetting.

[0081] 2. Cell counting: Use a pipette tip to draw 10 μL of cell resuspension into a cell counting plate and insert it into a cell counter for counting.

[0082] 3. Use a pipette to blow the cells thoroughly to mix them, then plate them in a 6-well plate at a density of 1000 cells / well. Add 2 mL of fresh complete culture medium to each well of the 6-well plate, plate 3 replicate wells for each group, shake the cells using the "figure 8 method" and transfer them to a cell culture incubator.

[0083] 4. Change the cell medium every 2 days and observe the cell status under a microscope.

[0084] 5. When the number of single clone cells in the vast majority of wells is observed to be greater than 50 under a microscope, stop culturing and collect samples.

[0085] 6. Aspirate the original culture medium in the 6-well plate, gently rinse with PBS twice, add 4% paraformaldehyde after absorbing the liquid, add 700μL to each well, and place it at room temperature for fixation for 30 minutes.

[0086] 7. Aspirate the fixative, rinse twice with PBS, add clean, impurity-free crystal violet staining solution, add 700 μL to each well, place on a shaker and mix slowly for 20 minutes.

[0087] 8. Aspirate the crystal violet stain, transfer to a 50mL centrifuge tube and seal for storage. Slowly place the 6-well plate vertically into tap water and soak for 10 seconds. Take out the plate and repeat this process several times. After the background in the 6-well plate is clean, invert it on absorbent paper to dry and take pictures under a stereo microscope.

[0088] (5) Migration experiment

[0089] 1. Digest and centrifuge the FaDu cells overexpressing SMG6 in the logarithmic growth phase, remove the supernatant, resuspend in serum-free medium, mix thoroughly and count the cells.

[0090] 2. Add 700 μL / well of culture medium containing 20% ​​FBS to a 24-well plate.

[0091] 3. After the cells are mixed, they are added into the Transwell chamber at a density of 20,000 cells / well. 200 μL of serum-free culture medium is added to each well, with 3 replicates per group.

[0092] 4. Use tweezers to carefully transfer the chamber to a 24-well plate containing 20% ​​FBS medium and place it in an incubator for 24 hours.

[0093] 5. Aspirate the culture medium in the Transwell chamber and the 24-well plate, gently rinse twice with PBS, and aspirate all the liquid.

[0094] 6. Add 700 μL / well of 4% paraformaldehyde and fix at room temperature for 30 minutes.

[0095] 7. Aspirate the fixative, rinse twice with PBS, add 700 μL of clean, impurity-free crystal violet stain to stain the cells, and shake slowly on a shaker for 20 minutes.

[0096] 8. Recover the crystal violet stain, slowly place the chamber into tap water, wet a cotton swab, gently wipe off the cells in the chamber with the cotton swab, and let it dry.

[0097] 9. Observe the cells under a microscope, randomly select 5 different fields of view to take pictures and collect data.

[0098] (6) Invasion assay

[0099] 1. Melt the Matrigel in an ice bath.

[0100] 2. Dilute the matrix gel by adding serum-free culture medium at a ratio of 1:7 and spread 40 μL / well in the upper chamber of the Transwell chamber.

[0101] 3. Place in the incubator for 2 h until gelation occurs, then hydrate with serum-free medium for 30 min.

[0102] 4. Subsequent operations are the same as the migration experiment steps.

[0103] The results of the above experiments are as follows Figure 2 As shown, where:

[0104] Figure 2 A in the figure is a Western blot experiment to detect the effect of overexpression of SMG6 in head and neck squamous cell carcinoma FaDu cells. Figure 2 As can be seen in A, compared with GAPDH, the SMG6 protein level in the experimental group was significantly higher than that in the control group.

[0105] Figure 2 B in the figure is a clone formation experiment. Figure 2 As can be seen from B, compared with the control group, the cells in the experimental group formed clone colonies that were smaller in size and fewer in number.

[0106] Figure 2 C in the figure is the cell proliferation detected by CCK8 experiment; Figure 2 As can be seen from C, the cell proliferation ability of the experimental group is weaker than that of the control group.

[0107] Figure 2 D in the figure is the invasion and migration assay to detect the cell invasion and migration abilities; Figure 2 As can be seen from D, compared with the control group, the number of invasion and migration cells in the experimental group is less, indicating that its invasion and migration ability is weaker.

[0108] In summary, Figure 2 The results showed that SMG6 protein could inhibit the proliferation, invasion and migration of HNSCC cells.

[0109] Example 3

[0110] Nude mouse subcutaneous tumor formation experiment

[0111] 1. The FaDu cells of SMG6 in the logarithmic growth phase extracted in Example 2 were digested with trypsin, centrifuged after digestion was terminated, and the supernatant was sucked out as much as possible with a pipette tip, and then an appropriate amount of serum-free culture medium was added and mixed by pipetting, and the cells were counted after sufficient mixing.

[0112] 2. Add an appropriate amount of serum-free culture medium according to the counting results to make the SMG6 cell density reach 3×10 7 / mL, transfer to a clean 1.5mL EP tube, and immediately put the EP tube on ice for storage.

[0113] 3. On the clean bench, select the upper and middle groin area of ​​the nude mouse with rich blood supply, and disinfect the area to be injected with 75% alcohol.

[0114] 4. Mix the cell suspension thoroughly, draw up the cell suspension with a syringe, and inoculate it subcutaneously at the injection site with an inoculation volume of 0.1 mL.

[0115] 5. After the inoculation is completed, the inoculated nude mice are raised normally under a sterile environment, and the body weight of the nude mice and the longest and shortest diameters of the tumor are measured every 4 days.

[0116] 6. After 4 weeks, the subcutaneous tumors were removed, weighed and recorded, and photographed according to the groups.

[0117] The results are as follows Figure 3 As shown in Figure 2, HNSCC cells overexpressing SMG6 protein and control were subjected to subcutaneous tumor formation experiments in nude mice, and it was found that HNSCC cells overexpressing SMG6 protein had weaker subcutaneous tumor formation ability. Figure 3 The results showed that SMG6 protein could inhibit the growth of HNSCC cells.

[0118] Although the description of the present invention has been quite detailed and specifically describes several described embodiments, it is not intended to be limited to any of these details or embodiments or any particular embodiment, but should be regarded as providing a broad possible interpretation of these claims in view of the prior art by reference to the appended claims, thereby effectively covering the intended scope of the present invention. In addition, the above description of the present invention is based on the embodiments foreseeable by the inventor, and its purpose is to provide a useful description, and those non-substantial changes to the present invention that have not yet been foreseen may still represent equivalent changes to the present invention.

Claims

1. Application of a molecular marker in constructing a prognosis prediction model for head and neck squamous cell carcinoma, characterized in that: The molecular marker is SMG6 protein, and the amino acid sequence of the SMG6 protein is shown in SEQ ID NO:

1.

2. Use of a molecular marker as a target in screening drugs against head and neck squamous cell carcinoma, characterized in that: The molecular marker is SMG6 protein, the amino acid sequence of the SMG6 protein is shown in SEQ ID NO: 1, and the anti-head and neck squamous cell carcinoma drug is used to promote the high expression of the SMG6 protein.

3. Use of a molecular marker in the preparation of a tumor suppressor for head and neck squamous cell carcinoma, characterized in that: The molecular marker is SMG6 protein, and the amino acid sequence of the SMG6 protein is shown in SEQ ID NO:1.

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