Recently, chimeric antigen receptors T cells (CAR T) have made a breakthrough in the treatment of lymphoma and leukemia, open a new path for the tumor cellular immunetherapy. It is the key for CAR T to take the gene which can identify the CD19 antigen of lymphoblastic leukemia into lymphocytes, enable it to kill leukemia cells with specific cell-surface loci. The same principle also applies to other aspects, if we find specific target genes of lymphocytes. Recent studies have found that high mobility group protein N2 (high mobility group chromosal protein N2, HMGN2) is the excellent target of tumor-associated antigen in lymphocytes, is the antitumor effector molecule of CD8(+) T cells, which has the ability of trends and specific identify/binding in myeloid leukemia, breast cancer, cervical cancer and other tumor cells. HMGN2 is expected to be used for the preparation of specific identification of tumor lymphocytes and to treat more leukemia and tumors. This article focuses on the strucure and function of HMGN and the chemotaxis and antitumor effect of HMGN2 in leukemia and tumors.
Antigens, CD19 ; Antigens, Neoplasm ; CD8-Positive T-Lymphocytes ; HMGN2 Protein ; Humans ; Immunotherapy ; Leukemia ; Neoplasms ; Receptors, Antigen, T-Cell

This study sought to clarify the distribution of HMGN2 in HeLa cells. The recombinant eukaryotic expression vectors pcDNA3. 1-myc-his-HMGN2 and pEGFP-N1-HMGN2 were constructed, and then were transfected into HeLa cells. immunocytochemistry staining indicated that HMGN2 were present not only in HeLa nucleus but also in the cytoplasm. The presence of HMGN2 was also detected in the culture supernatant by ELISA with rabbit anti-serum against HMGN2 and mouse anti-His6 monoclonal antibodies. The confocal microscope observation showed the same subcellular localization as that of immunocytochemistry staining. There results suggested that HMGN2 could be present in the nucleus and cytoplasm of HeLa cell as well as in the extracellular environment.
Animals ; Antibodies, Monoclonal ; HMGN2 Protein ; immunology ; metabolism ; pharmacology ; HeLa Cells ; Humans ; Mice ; Rabbits ; Recombinant Fusion Proteins ; biosynthesis ; pharmacology ; Transfection

This study was conducted to isolate and purify antimicrobial polypeptides HMGN2 (high mobility group nucleosomal-binding domain2) from human lymph node, to detect the antimicrobial activity of HMGN2, and to determine the subcellular location of HMGN2 in human lymph node. The antimicrobial polypeptides were purified by the Reverse Phase HPLC and identified by Tricine-SDS-PAGE. The antimicrobial activity was detected by agar diffusion test. Mass spectrum and Western-blot analysis indicated the individual character of protein. HMGN2 was isolated and purified from human lymph node, and it showed antimicrobial potency against the pathogenic strain E. coli 54,080. The immunocytochemistry staining indicated that HMGN2 was present both in human lymph node cells' nucleus and cytoplasm. In conclusion, HMGN2 protein is of antimicrobial activity and it is probably involved in the defence of innate immunity in vivo.
Antimicrobial Cationic Peptides ; isolation & purification ; metabolism ; Escherichia coli ; drug effects ; HMGN2 Protein ; isolation & purification ; metabolism ; Humans ; Lymph Nodes ; chemistry ; metabolism ; Tissue Distribution

Total RNA was extracted from human LAK cell, and a cDNA encoding mature peptide HMG-17 and its alpha helix domain was amplified by RT-PCR. The recombinant prokaryotic expression vector pGEX-1lambdaT-HMG-17 and pGEX-1lambdaT HMG-17alpha helix was constructed. Using affinity chromatography, thrombin cleaving and AU-PAGE elution, we obtained the purified HMG-17. Analyses of MIC, MEC and MBC indicated that HMG-17 and HMG-17alpha had strong antibacterial activity. MIC of the alpha-helic domain was almost the same as that of HMG17, suggesting that the alpha-helic structure would be essential for the antibacterial activity of HMG-17.
Anti-Bacterial Agents ; biosynthesis ; pharmacology ; Escherichia coli ; genetics ; metabolism ; HMGN2 Protein ; biosynthesis ; genetics ; pharmacology ; Humans ; Killer Cells, Lymphokine-Activated ; chemistry ; Peptides ; genetics ; pharmacology ; Prokaryotic Cells ; metabolism ; Recombinant Proteins ; biosynthesis ; genetics ; pharmacology

ADP Ribose Transferases ; chemistry ; pharmacology ; Animals ; Antineoplastic Agents ; pharmacology ; Bacterial Toxins ; chemistry ; pharmacology ; Exotoxins ; chemistry ; pharmacology ; Female ; HMGN2 Protein ; chemistry ; pharmacology ; HeLa Cells ; Humans ; Immunotoxins ; pharmacology ; Mice ; Mice, Inbred BALB C ; Protein Structure, Tertiary ; Recombinant Fusion Proteins ; biosynthesis ; pharmacology ; Virulence Factors ; chemistry ; pharmacology