CN116270982A - Use of recombinant type XVII humanized collagen in the treatment of breast cancer - Google Patents

Abstract

The invention belongs to the field of biomedicine, and in particular relates to the application of recombinant type XVII humanized collagen in the treatment of breast cancer. The present invention provides the use of recombinant type XVII humanized collagen in the preparation of medicaments for preventing and/or treating breast diseases; the recombinant type XVII humanized collagen comprises the sequence shown in (A)m or consists of (A) The sequence composition shown in m, wherein each A is selected from the amino acid sequence shown in any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3; m is an integer between 1-10 . The research results show that the recombinant type XVII humanized collagen can significantly inhibit the growth, proliferation and migration characteristics of breast cancer cells, and can also promote the dormancy of breast cancer cells, thus laying the foundation for the preparation of drugs for the treatment of breast cancer.

Description

Use of recombinant type XVII humanized collagen in breast cancer treatment

technical field

The invention belongs to the field of biomedicine, and in particular relates to the application of recombinant type XVII humanized collagen in the treatment of breast cancer.

Background technique

Currently, breast cancer (BC) ranks first in the incidence of cancer in the world. There are limited treatment options for breast cancer, mainly including surgical resection, radiation therapy, chemotherapy and hormone therapy.

Triple negative breast cancer (TNBC) is a subtype of breast cancer. , PR) and human epidermal growth factor receptor (epidermal growth factor receptor 2, HER2) negative breast cancer. It has the characteristics of easy recurrence and high metastasis rate, and due to the lack of effective therapeutic targets, its treatment method is relatively single. At present, chemotherapy is the main treatment method, so more effective and safe treatment methods are urgently needed.

Collagen is the most abundant protein in animals, accounting for about 30% of the total protein, and plays an important role in physiological processes such as cell adhesion. Because collagen has good biocompatibility and biodegradation safety, it has been widely used in the field of medicine. Until now, most of the collagen used in various researches comes from animal tissue and skin extracts. Collagen extracted from animal bodies has poor water solubility and weak processability, which directly limits the development of many potential uses. The collagen produced by genetic engineering technology can effectively overcome the above shortcomings.

The Chinese patent application with the application number 201911051106.3 and the invention title "Human Collagen Type 17 Polypeptide, Its Production Method and Use" records a recombinant type XVII humanized collagen, which has the characteristics of high water solubility and high biological activity . No reports have suggested a link between recombinant type XVII humanized collagen and breast cancer treatment.

Contents of the invention

The problem to be solved by the invention

This invention intends to use the recombinant humanized collagen type XVII in the Chinese patent application with application number 201911051106.3 as a raw material to evaluate its effectiveness in the treatment of breast cancer and other breast diseases. Specifically, the present invention intends to use recombinant type XVII humanized collagen to inhibit the proliferation activity and/or migration ability of breast cancer cells, and promote the dormancy of breast cancer cells so as to achieve the effect of preventing and/or treating breast cancer.

solutions to problems

The present invention provides the use of recombinant type XVII humanized collagen in the preparation of medicines for preventing and/or treating breast diseases;

Wherein, the recombinant type XVII humanized collagen comprises the sequence shown in (A)m or consists of the sequence shown in (A)m, wherein each A is selected from SEQ ID No.1, SEQ ID No. 2 and the amino acid sequence shown in any one of SEQ ID No.3 or any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3 is substituted, added, inserted or deleted with 1 or more amino acid residues sequence or a sequence having at least 83% sequence identity with the amino acid sequence shown in any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3; m is an integer between 1-10; wherein each The A's are the same or different, and two adjacent A's are directly linked by a peptide bond or linked by more than one amino acid residue.

Further, the recombinant type XVII humanized collagen comprises or consists of the amino acid sequence shown in SEQ ID No.1, SEQ ID No.2, SEQ ID No.3, SEQ ID No.4 or SEQ ID No.5 .

Further, the breast disease is breast cancer.

Further, the breast cancer includes luminal A breast cancer, luminal B breast cancer, HER-2 overexpression breast cancer, basal cell-like breast cancer, triple-negative breast cancer and normal breast-like breast cancer.

Further, the breast cancer is luminal A breast cancer, HER-2 overexpression breast cancer, basal cell-like breast cancer or triple negative breast cancer.

Further, the recombinant type XVII humanized collagen prevents and/or treats breast cancer by inhibiting the proliferation ability of breast cancer cells, inhibiting the migration ability of breast cancer cells and/or promoting the breast cancer cells to enter dormancy.

Further, said inhibiting the proliferation ability of breast cancer cells includes inhibiting the DNA replication activity of breast cancer cells.

The effect of the invention

The research results of the present invention show that the recombinant type XVII humanized collagen can significantly inhibit the growth and proliferation ability (including DNA replication activity) of breast cancer cells (including non-triple-negative breast cancer cells and triple-negative breast cancer cells), And it can inhibit the migration characteristics of tumor cells (including both non-triple-negative breast cancer cells and triple-negative breast cancer cells), and can also promote the dormancy of breast cancer cells, thereby laying the foundation for the preparation of drugs for the treatment of breast cancer, and also for the The safety and effectiveness of recombinant type XVII humanized collagen in breast cancer patients provide a certain theoretical basis.

Description of drawings

Figure 1 is the statistical result of the effect of different concentrations of recombinant humanized collagen type XVII on the proliferation activity of MCF-7 cells at different times.

Figure 2 is the statistical result of the effect of different concentrations of recombinant XVII humanized collagen on the proliferation activity of MDA-MB-231 cells at different times.

Figure 3 is the statistical results of the effects of different concentrations of recombinant XVII humanized collagen on the proliferation activity of SK-BR-3 cells at different times.

Fig. 4 is the statistical result of the effect of recombinant type XVII humanized collagen provided by the present invention on the migration ability of MCF-7 cells at different times.

Fig. 5 is the statistical result of the effect of recombinant type XVII humanized collagen provided by the present invention on the migration ability of MDA-MB-231 cells at different times.

Fig. 6 is the statistical result of the effect of recombinant type XVII humanized collagen provided by the present invention on the migration ability of SK-BR-3 cells at different times.

Fig. 7 is the detection result of the effect of the recombinant type XVII humanized collagen provided by the present invention on the DNA replication activity of MCF-7 cells in the EDU cell proliferation experiment.

Fig. 8 is the detection result of the effect of the recombinant type XVII humanized collagen provided by the present invention on the DNA replication activity of MDA-MB-231 cells in the EDU cell proliferation experiment.

Fig. 9 is the detection result of the effect of the recombinant type XVII humanized collagen provided by the present invention on the DNA replication activity of SK-BR-3 cells in the EDU cell proliferation experiment.

Fig. 10 is the detection result of the effect of recombinant type XVII humanized collagen provided by the present invention on the cell cycle of MDA-MB-231 cells.

Detailed ways

Embodiments of the present invention will be described below, but the present invention is not limited thereto.

In the present invention, the meaning expressed by "may" includes both meanings of performing certain processing and not performing certain processing.

In the present invention, "optional" or "optionally" means that the next described event or circumstance may or may not occur, and that the description includes instances where the event occurs and instances where it does not.

In the present invention, the terms "comprising", "having", "comprising" or "containing" may mean inclusive or open-ended and do not exclude additional, unrecited elements or method steps. At the same time, "comprising", "having", "including" or "comprising" can also mean enclosing, excluding additional, unrecited elements or method steps.

In the present invention, references to "some specific/preferred embodiments", "other specific/preferred embodiments", "embodiments" and the like refer to specific elements described in relation to the embodiments (such as , feature, structure, property and/or characteristic) are included in at least one embodiment described herein and may or may not be present in other embodiments. In addition, it is to be understood that the described elements may be combined in any suitable manner in the various embodiments.

In the present invention, the numerical range represented by "numerical value A - numerical value B" or "numerical value A-numerical value B" refers to a range including numerical values A and B at the endpoints.

In the present invention, the term "one (a)" or "one (an)" or "one (the)" may refer to "one", and may also refer to "one or more", "at least one" and "one or more than one".

In the present invention, the term "individual", "patient" or "subject" includes mammals. Mammals include, but are not limited to, domesticated animals (e.g., cattle, sheep, cats, dogs, and horses), primates (e.g., humans and non-human primates such as monkeys), rabbits, and rodents (e.g., , mice and rats).

In the present invention, "treatment" refers to: after suffering from a disease, subject is contacted (for example, administered) with the recombinant type XVII humanized collagen described in the present invention, thereby reducing the Alleviation of disease symptoms does not necessarily mean complete suppression of disease symptoms. Suffering from a disease means that the body has symptoms of a disease.

In the present invention, "prevention" refers to: before suffering from a disease, by exposing the subject to the recombinant type XVII humanized collagen described in the present invention, thereby reducing the probability of suffering from the disease and the And/or alleviating the symptoms of a disease does not necessarily mean completely suppressing the disease.

In the present invention, the recombinant type XVII humanized collagen is described in a Chinese patent application with the application number 201911051106.3 and the title of the invention "Human Collagen Type 17 Polypeptide, Its Production Method and Use".

In some embodiments, the recombinant type XVII humanized collagen of the present invention comprises or consists of the sequence shown in (A)m, wherein each A is selected from SEQ ID No. 1. The amino acid sequence shown in any one of SEQ ID No.2 and SEQ ID No.3 or any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3 has 1 or more substitutions, additions, or deletions Amino acid sequence of amino acid residues or a sequence having at least 83% sequence identity with the amino acid sequence shown in any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3; m is between 1-10 Integer; where each A is the same or different, and two adjacent A are directly linked by a peptide bond or linked by more than one amino acid residue.

The SEQ ID No.1, SEQ ID No.2 or SEQ ID No.3 of the present invention is derived from the human type 17 collagen COL17A1 sequence, and the human type 17 collagen COL17A1 sequence can be found at https://www.ncbi.nlm. nih.gov/protein/Q9UMD9.3.

SEQ ID No. 1: GSPGPKGDMGSPGPKGDRGFPGTPPGIPGPLGHPGPQGPKGQKGSVGDPPGMEGPMGQRGREGPMGPRGEA.

SEQ ID No. 2: GLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPA.

SEQ ID No. 3: GADFAGDLDYNELAVRVSESMQRQGLLQGMAYTVQGPPGQPGPQGPPGISKVFSAYSNVTADLMDFFQTYGAIQGPPGQKGEMGTPGPKGDRGPAGPGPGHPGPPGPRGHKGEKGDKGDQ.

In some preferred embodiments, the recombinant type XVII humanized collagen of the present invention comprises or consists of the sequence shown in SEQ ID No.4, which is represented by SEQ ID No. 1 was used as a repeating unit and was repeated 3 times.

SEQ ID No. 4: GSPGPKGDMGSPGPKGDRGFPGTPPGIPGPLGHPGPQG PKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGSPGPKGDMGSPGPKGDRGFPGTPPGIPGPLGHPGPQGPKGQKGSVGDPGMEGPMGQRGREGPMGPRGEAGSPGPKGDMGSPGPKGDRGFPGTPPGIPGPLGHPGPQGPKG QKGSVGDPGMEGPMGQRGREGPMGPRGEA.

In some other preferred embodiments, the recombinant type XVII humanized collagen of the present invention comprises or consists of the sequence shown in SEQ ID No.5, which is represented by SEQ ID No.2 was repeated 3 times as a repeating unit.

SEQ ID No. 5: GLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGLPGAVGEPGAKGAMGPAGLQGLRGEVGLPGVKGDKGPMGPPGPKGDQGEKGPRGLTGEPGMRGL PGAVGEPGAKGAMGPA.

In the present invention, amino acid addition refers to adding amino acids to the amino acid sequence, such as the C-terminal or N-terminal of SEQ ID No.4, as long as the recombinant type XVII humanized collagen of the present invention retains the activity of the amino acid sequence of SEQ ID No.4 .

In the present invention, amino acid substitution refers to the substitution of an amino acid residue at a certain position in an amino acid sequence, such as a sequence of SEQ ID No.4, by other amino acid residues, as long as the recombinant humanized collagen type XVII of the present invention remains Activity of the amino acid sequence of SEQ ID No.4.

In the present invention, the amino acid substitution can be a conservative amino acid substitution, which means that compared with the amino acid sequence of SEQ ID No.4, there are 3, more preferably 2 amino acids or 1 amino acid are replaced by amino acids with similar or similar properties. form peptides. These conservative variant peptides can be produced according to the following amino acid substitutions: substitution of Val, Leu or Ile for Ala, substitution of Lys, Gln, Asn or His for Arg, substitution of Gln, His, Lys or Arg for Asn, Glu or Asn Substitution of Asp, substitution of Cys by Ser or Ala, substitution of Gln by Asn or Glu, substitution of Glu by Asp or Gln, substitution of Gly by Ala, substitution of His by Asn, Lys, Gln or Arg, Leu, Met , Ala, Val, Phe or Norleucine for Ile, Ile, Met, Ala, Val, Phe or Norleucine for Leu, Asn, Gln or Arg for Lys, Ile, Leu or Phe Substitution of Met, substitution of Leu, Val, Ile, Ala or Tyr to Phe, substitution of Ala to Pro, substitution of Thr to Ser, substitution of Ser or Val to Thr, substitution of Phe or Tyr to Trp, Trp, Phe , Thr or Ser for Tyr substitution, and Phe, Ala, Met, Ile, Leu or norleucine for Val substitution. Amino acid substitutions can also be non-conservative amino acid substitutions.

In the present invention, amino acid insertion refers to the insertion of amino acid residues at an appropriate position in an amino acid sequence, such as the sequence of SEQ ID No.4, and the inserted amino acid residues can also be all or partly adjacent to each other, or there is no gap between the inserted amino acids. adjacent to each other as long as the recombinant type XVII humanized collagen of the present invention retains the activity of the amino acid sequence of SEQ ID No.4. The insertion position of the amino acid here is not between the individual repeat sequences.

In the present invention, amino acid deletion means that 1, 2 or more than 3 amino acids can be deleted from the amino acid sequence, such as the sequence of SEQ ID No.4, as long as the recombinant type XVII humanized collagen of the present invention retains SEQ ID No.4 activity of the amino acid sequence.

Unless otherwise defined, other technical and scientific terms used in the present invention have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs.

Example

The present invention is further illustrated by the following examples, but any example or combination thereof should not be construed as limiting the scope or implementation of the present invention. The scope of the present invention is defined by the appended claims, and those skilled in the art can clearly understand the scope defined by the claims in combination with the description and common knowledge in the field. Without departing from the spirit and scope of the present invention, those skilled in the art may make any modifications or changes to the technical solutions of the present invention, and such modifications and changes are also included in the scope of the present invention.

Those who do not indicate the specific conditions in the examples are carried out according to the conventional conditions or the conditions suggested by the manufacturer. All reagents or instruments that did not indicate the manufacturer are all conventional products that can be purchased from the market. In order to better illustrate the present invention, numerous specific details are given in the following specific embodiments. It will be understood by those skilled in the art that the present invention may be practiced without certain of the specific details. In some other embodiments, methods, means, devices and steps well known to those skilled in the art are not described in detail in order to highlight the gist of the present invention.

Experimental Materials:

Breast cancer cells: MCF-7 cells, MDA-MB-231 cells, SK-BR-3 cells are from ATCC;

FBS source: Sigma;

Serum-free medium was sourced from: Sigma;

The amino acid sequence of the recombinant type XVII humanized collagen is shown in SEQ ID No.4;

CCK-8 kit comes from: GLPbio;

EDU and cell cycle detection kits are from: Biyuntian.

Example 1: Effect of Recombinant Type XVII Humanized Collagen on Cell Proliferation

experimental method:

Experimental group: breast cancer cells + 10% FBS medium + recombinant type XVII humanized collagen co-cultured.

Negative control group: breast cancer cells + 10% FBS medium, co-cultured without collagen.

Blank control group: no cells, 10% FBS medium, co-culture without collagen.

After setting up the experimental groups, inoculate three kinds of breast cancer cells (MCF-7 cells, MDA-MB-231 cells and SK-BR-3 cells) at the appropriate density in a 96-well plate according to the needs, with a volume of 100 μL/well. Recombinant type XVII humanized collagen was added behind the wall, and the final concentrations were 0.01mg/mL, 0.1mg/mL, 1mg/mL, and 10mg/mL (marked as 0.01mg/mL, 0.1mg/mL, and 1mg/mL in the figure). mL _, 10mg/mL), the negative control group did not add collagen (marked as 0mg/mL in the figure); after 24h and 48h of co-culture of cells and collagen, the 96-well plate was transferred to the ultra-clean bench of the cell room, and the culture was discarded. Add 100 μL serum-free medium and 10 μL CCK-8 to each well in the dark, and add PBS to the periphery of the 96-well plate to prevent reagent volatilization; place the 96-well plate in a 37°C incubator to avoid light After incubation for 1 hour, the absorbance value OD _450nm was measured with a microplate reader, and the measurement was repeated three times to obtain the average value. Calculated according to the formula in the CCK-8 kit manual: cell survival rate = (OD value of the experimental group - OD value of the blank control group) / (OD value of the negative control group - OD value of the blank control group) × 100%.

Experimental results:

The results are shown in Figures 1-3, the recombinant type XVII humanized collagen can inhibit the proliferative activity of breast cancer cells.

After group culture, compared with the control group, the proliferation activities of the three types of breast cancer cells treated with recombinant XVII humanized collagen were significantly reduced, indicating that recombinant XVII humanized collagen has an effect on the proliferation ability of breast cancer cells. inhibition.

Example 2: Effect of Recombinant Type XVII Humanized Collagen on Cell Migration

experimental method:

The experimental grouping is the same as in Example 1.

Breast cancer cells were inoculated in six-well plates with a volume of 2 mL/well. After the cells adhered to the wall, the recombinant XVII humanized collagen prepared with 10% FBS medium was added to the experimental group for co-culture (marked in the figure as experimental group), the final concentration of collagen was 10 mg/mL, and 10% FBS medium was added to the control group (marked as the control group in the figure). When the cells in each well are 95% full and form a single layer of cells, use a 200 μL pipette tip to make a "one" scratch on the monolayer of cells, wash with PBS for 3 times, and continue to add serum-free medium to the experimental group The prepared recombinant type XVII humanized collagen was cultured, the final concentration of collagen was 10 mg/mL, and the control group was added with serum-free medium. After incubation in the incubator for 24 hours, the culture medium was sucked off, washed with PBS for 3 times, and then placed in an inverted fluorescent tube. Observe and take pictures under a microscope, and count the relative migration rate of cells at the same time.

Experimental results:

The results are shown in Figures 4-6, the recombinant type XVII humanized collagen can inhibit the migration ability of breast cancer cells.

After group culture, compared with the control group, the migration rates of the three types of breast cancer cells treated with recombinant XVII humanized collagen decreased significantly, indicating that recombinant XVII humanized collagen has an effect on the migration ability of breast cancer cells. inhibition.

Example 3: Effect of recombinant type XVII humanized collagen on cellular DNA replication activity Experimental method:

The experimental grouping was the same as in Example 1, and the final concentration of collagen co-culture was 10 mg/mL.

Breast cancer cells in the logarithmic growth phase were seeded in 96-well plates at 8×10 ³ cells per well. After adherent culture to the normal growth stage on the second day, the EDU kit was used for staining. First, add an equal volume of 1× EdU working solution (10 μM) preheated at 37°C to a 6-well plate, and incubate in a 37°C incubator for 2 hours; after EdU labeling of cells, remove the culture medium and add 0.1mL 4 % (W/V) paraformaldehyde for fixation. After fixing at room temperature for 15 minutes, remove the fixative, and wash the cells with 0.1 mL washing solution for each well 3 times, 3-5 minutes each time. After removing the washing solution, each well was incubated with 0.1 mL permeabilization solution (0.3% (V/V) Triton X-100 in PBS) at room temperature for 10-15 minutes. Next, remove the permeabilization solution, wash the cells 1-2 times with 0.1mL washing solution per well, 3-5 minutes each time, then add 0.05mL Click reaction solution to each well, incubate at room temperature in the dark for 30 minutes, then aspirate the Click reaction solution , Wash 3 times with washing solution, 3-5 minutes each time. Subsequently, the nuclei were stained with Hoechst 33342 and incubated at room temperature for 10 minutes in the dark. Fluorescence detection can then be performed.

Experimental results:

The results are shown in Figures 7-9, the recombinant type XVII humanized collagen can inhibit the proliferation ability of breast cancer cells such as DNA replication activity.

After group culture, compared with the control group, the proportion of breast cancer cells with proliferative activity (red fluorescence) decreased significantly after the treatment with recombinant XVII humanized collagen, indicating that the recombinant XVII humanized collagen has an effect on the proliferation of breast cancer cells. Has an inhibitory effect.

Example 4: Effect of Recombinant Type XVII Humanized Collagen on Cell Cycle

experimental method:

The experimental grouping was the same as in Example 1, and the final concentration of collagen co-culture was 10 mg/mL.

MDA-MB-231 breast cancer cells were digested with trypsin, added to 1ml ice-bath pre-cooled 70% ethanol, mixed gently by pipetting, and fixed at 4°C for 30 minutes. Centrifuge at 1000g for 3-5 minutes to pellet the cells. Add 1ml ice-bath pre-cooled PBS to resuspend the cells. Centrifuge again to pellet the cells, aspirate the supernatant, add 0.5mL propidium iodide staining solution to each tube of cell samples, slowly and fully resuspend the cell pellet, and incubate at 37°C for 30 minutes in the dark to complete the flow detection.

Experimental results:

The results are shown in FIG. 10 , the recombinant type XVII humanized collagen can affect the division cycle of breast cancer cells.

After group culture, compared with the control group, the proportion of breast cancer cells in the dormant cycle (G1/G0 phase) increased significantly after treatment with recombinant XVII humanized collagen, and the breast cancer cells in the proliferative active cycle (G2/M phase) The proportion of cancer cells decreased significantly, indicating that the recombinant type XVII humanized collagen can promote breast cancer cells to enter the dormant cycle (G1/G0 phase).

Summarize:

Breast cancer currently ranks first in the incidence of cancer in the world. There are limited treatment options, especially for triple-negative breast cancer. The treatment method is single, and the recurrence and metastasis rate is high. More effective and safe treatment methods are urgently needed. Recombinant type XVII humanized collagen has the characteristics of high water solubility and high biological activity. Existing experiments have confirmed that recombinant type XVII humanized collagen can inhibit the growth and proliferation of breast cancer cells, and can inhibit the migration characteristics of tumor cells, and its mechanism may depend on promoting tumor cells to enter the dormant cycle. This will provide a certain theoretical basis for the safety and effectiveness of recombinant XVII humanized collagen in clinical application to breast cancer patients.

Claims (7)

1. The use of recombinant type XVII humanized collagen in the preparation of medicines for preventing and/or treating breast diseases; Wherein, the recombinant type XVII humanized collagen comprises the sequence shown in (A)m or consists of the sequence shown in (A)m, wherein each A is selected from SEQ ID No.1, SEQ ID No. 2 and the amino acid sequence shown in any one of SEQ ID No.3 or any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3 is substituted, added, inserted or deleted with 1 or more amino acid residues sequence or a sequence having at least 83% sequence identity with the amino acid sequence shown in any one of SEQ ID No.1, SEQ ID No.2 and SEQ ID No.3; m is an integer between 1-10; wherein each The A's are the same or different, and two adjacent A's are directly linked by a peptide bond or linked by more than one amino acid residue. 2. The use according to claim 1, characterized in that the recombinant XVII type humanized collagen comprises SEQ ID No.1, SEQ ID No.2, SEQ ID No.3, SEQ ID No.4 or SEQ ID No. The amino acid sequence shown in ID No.5 or consists of it. 3. The use according to claim 1 or 2, characterized in that the breast disease is breast cancer. 4. The use according to claim 3, wherein the breast cancer includes luminal A breast cancer, luminal B breast cancer, HER-2 overexpression breast cancer, basal cell-like breast cancer, Triple-negative breast cancer and normal mammary-like breast cancer. 5. The use according to claim 3 or 4, wherein the breast cancer is luminal A breast cancer, HER-2 overexpression breast cancer, basal cell-like breast cancer or triple negative breast cancer. 6. The use according to any one of claims 3 to 5, characterized in that the recombinant type XVII humanized collagen inhibits the proliferation ability of breast cancer cells, inhibits the migration ability of breast cancer cells and/or Promoting breast cancer cell dormancy to prevent and/or treat breast cancer. 7. The use according to claim 6, characterized in that said inhibiting the proliferation ability of breast cancer cells comprises inhibiting the DNA replication activity of breast cancer cells.

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