Stability of the recombinant anti‑erbB2 scFv‑Fc‑interleukin‑2 fusion protein and its inhibition of HER2‑overexpressing tumor cells. 2013

Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
Norman Bethune College of Medicine, Jilin University, Changchun 130021, P.R. China.

The anti‑erbB2 scFv‑Fc‑IL‑2 fusion protein (HFI) is the basis for development of a novel targeted anticancer drug, in particular for the treatment of HER2‑positive cancer patients. HFI was fused with the anti‑erbB2 antibody and human IL‑2 by genetic engineering technology and by antibody targeting characteristics of HFI. IL‑2 was recruited to target cells to block HER2 signaling, inhibit or kill tumor cells, improve the immune capacity, reduce the dose of antibody and IL‑2 synergy. In order to analyse HFI drug ability, HFI plasmid stability was verified by HFI expression of the trend of volume changes. Additionally, HFI could easily precipitate and had progressive characteristics and thus, the buffer system of the additive phosphate‑citric acid buffer, arginine, Triton X‑100 or Tween‑80, the establishment of a microfiltration, ion exchange, affinity chromatography and gel filtration chromatography‑based purification process were explored. HFI samples were obtained according to the requirements of purity, activity and homogeneity. In vivo, HFI significantly delayed HER2 overexpression of non‑small cell lung cancer (Calu‑3) in human non‑small cell lung cancer xenografts in nude mice, and the inhibition rate was more than 60% (P<0.05) in the group treated with 1 mg/kg the HFI dose; HFI significantly inhibited HER2 expression of breast cancer (FVB/neu) transgenic mouse tumor growth in 1 mg/kg of the HFI dose group, and in the following treatment the 400 mm3 tumors disappeared completely. Combined with other HFI test data analysis, HFI not only has good prospects, but also laid the foundation for the development of antibody‑cytokine fusion protein‑like drugs.

UI MeSH Term Description Entries
D007135 Immunoglobulin Variable Region That region of the immunoglobulin molecule that varies in its amino acid sequence and composition, and comprises the binding site for a specific antigen. It is located at the N-terminus of the Fab fragment of the immunoglobulin. It includes hypervariable regions (COMPLEMENTARITY DETERMINING REGIONS) and framework regions. Variable Region, Ig,Variable Region, Immunoglobulin,Framework Region, Immunoglobulin,Fv Antibody Fragments,Fv Fragments,Ig Framework Region,Ig Variable Region,Immunoglobulin Framework Region,Immunoglobulin Fv Fragments,Immunoglobulin V,Antibody Fragment, Fv,Antibody Fragments, Fv,Fragment, Fv,Fragment, Fv Antibody,Fragment, Immunoglobulin Fv,Fragments, Fv,Fragments, Fv Antibody,Fragments, Immunoglobulin Fv,Framework Region, Ig,Framework Regions, Ig,Framework Regions, Immunoglobulin,Fv Antibody Fragment,Fv Fragment,Fv Fragment, Immunoglobulin,Fv Fragments, Immunoglobulin,Ig Framework Regions,Ig Variable Regions,Immunoglobulin Framework Regions,Immunoglobulin Fv Fragment,Immunoglobulin Variable Regions,Regions, Immunoglobulin Variable,Variable Regions, Ig,Variable Regions, Immunoglobulin
D007141 Immunoglobulin Fc Fragments Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN. Fc Fragment,Fc Fragments,Fc Immunoglobulin,Fc Immunoglobulins,Ig Fc Fragments,Immunoglobulin Fc Fragment,Immunoglobulins, Fc,Immunoglobulins, Fc Fragment,Fc Fragment Immunoglobulins,Fc Fragment, Immunoglobulin,Fc Fragments, Ig,Fc Fragments, Immunoglobulin,Fragment Immunoglobulins, Fc,Fragment, Fc,Fragments, Ig Fc,Immunoglobulin, Fc
D007376 Interleukin-2 A soluble substance elaborated by antigen- or mitogen-stimulated T-LYMPHOCYTES which induces DNA synthesis in naive lymphocytes. IL-2,Lymphocyte Mitogenic Factor,T-Cell Growth Factor,TCGF,IL2,Interleukin II,Interleukine 2,RU 49637,RU-49637,Ro-23-6019,Ro-236019,T-Cell Stimulating Factor,Thymocyte Stimulating Factor,Interleukin 2,Mitogenic Factor, Lymphocyte,RU49637,Ro 23 6019,Ro 236019,Ro236019,T Cell Growth Factor,T Cell Stimulating Factor
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D001943 Breast Neoplasms Tumors or cancer of the human BREAST. Breast Cancer,Breast Tumors,Cancer of Breast,Breast Carcinoma,Cancer of the Breast,Human Mammary Carcinoma,Malignant Neoplasm of Breast,Malignant Tumor of Breast,Mammary Cancer,Mammary Carcinoma, Human,Mammary Neoplasm, Human,Mammary Neoplasms, Human,Neoplasms, Breast,Tumors, Breast,Breast Carcinomas,Breast Malignant Neoplasm,Breast Malignant Neoplasms,Breast Malignant Tumor,Breast Malignant Tumors,Breast Neoplasm,Breast Tumor,Cancer, Breast,Cancer, Mammary,Cancers, Mammary,Carcinoma, Breast,Carcinoma, Human Mammary,Carcinomas, Breast,Carcinomas, Human Mammary,Human Mammary Carcinomas,Human Mammary Neoplasm,Human Mammary Neoplasms,Mammary Cancers,Mammary Carcinomas, Human,Neoplasm, Breast,Neoplasm, Human Mammary,Neoplasms, Human Mammary,Tumor, Breast
D002289 Carcinoma, Non-Small-Cell Lung A heterogeneous aggregate of at least three distinct histological types of lung cancer, including SQUAMOUS CELL CARCINOMA; ADENOCARCINOMA; and LARGE CELL CARCINOMA. They are dealt with collectively because of their shared treatment strategy. Carcinoma, Non-Small Cell Lung,Non-Small Cell Lung Cancer,Non-Small Cell Lung Carcinoma,Non-Small-Cell Lung Carcinoma,Nonsmall Cell Lung Cancer,Carcinoma, Non Small Cell Lung,Carcinomas, Non-Small-Cell Lung,Lung Carcinoma, Non-Small-Cell,Lung Carcinomas, Non-Small-Cell,Non Small Cell Lung Carcinoma,Non-Small-Cell Lung Carcinomas
D005260 Female Females
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000906 Antibodies Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).

Related Publications

Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
October 2007, Acta pharmacologica Sinica,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
May 2003, Biotechnology letters,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
January 2003, Journal of bioscience and bioengineering,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
August 2012, Sheng wu gong cheng xue bao = Chinese journal of biotechnology,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
June 2022, Scientific reports,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
February 2018, Oncotarget,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
November 2011, Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
March 2005, Journal of molecular biology,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
May 2004, The Journal of biological chemistry,
Yu-Jia Du, and Ze-Min Lin, and Ying-Hua Zhao, and Xiu-Ping Feng, and Chang-Qing Wang, and Gang Wang, and Chun-Di Wang, and Wei Shi, and Jian-Ping Zuo, and Fan Li, and Cheng-Zhong Wang
May 2015, EBioMedicine,
Copied contents to your clipboard!