RESUMO
The rapid development of bioengineering technology has introduced Fc-fusion proteins, representing a novel kind of recombinant protein, as promising biopharmaceutical products in tumor therapy. Numerous related anti-tumor Fc-fusion proteins have been investigated and are in different stages of development. Fc-fusion proteins are constructed by fusing the Fc-region of the antibody with functional proteins or peptides. They retain the bioactivity of the latter and partial properties of the former. This structural and functional advantage makes Fc-fusion proteins an effective tool in tumor immunotherapy, especially for the recruitment and activation of natural killer (NK) cells, which play a critical role in tumor immunotherapy. Even though tumor cells have developed mechanisms to circumvent the cytotoxic effect of NK cells or induce defective NK cells, Fc-fusion proteins have been proven to effectively activate NK cells to kill tumor cells in different ways, such as antibody-dependent cell-mediated cytotoxicity (ADCC), activate NK cells in different ways in order to promote killing of tumor cells. In this review, we focus on NK cell-based immunity for cancers and current research progress of the Fc-fusion proteins for anti-tumor therapy by activating NK cells.
Assuntos
Fragmentos Fc das Imunoglobulinas , Células Matadoras Naturais , Citotoxicidade Celular Dependente de Anticorpos , Fragmentos Fc das Imunoglobulinas/genética , Imunoterapia , Proteínas Recombinantes de Fusão/genéticaRESUMO
The asymmetric unit of the title compound, C(16)H(14)F(3)N(3)OS·H(2)O, contains two independent mol-ecules (A and B) and two water mol-ecules, one of which is disordered over two positions in a 0.790â (8):0.210â (8) ratio. The mol-ecular conformations are close, the benzimidazole mean plane and pyridine ring forming dihedral angles of 1.8â (3) and 0.1â (2)° in mol-ecules A and B, respectively. The water mol-ecules are involved in formation of two independent hydrogen-bonded chains via N-Hâ¯O and O-Hâ¯N hydrogen bonds. Chains propagating along the a axis are formed by mol-ecule A and one independent water mol-ecule, while chains propagating along the b axis are formed by mol-ecule B and the other independent water mol-ecule. The crystal packing exhibits π-π inter-actions, as indicated by short distances of 3.607â (3) and 3.701â (3)â Å between the centroids of the imidazole and pyridine rings of neighbouring mol-ecules.
RESUMO
OBJECTIVE: Routine semen parameters have limited clinical diagnostic value for predicting male infertility. The aim of this study was to investigate the association between sperm DNA fragmentation index (DFI) and semen quality, and between DFI and clinical pregnancy rate of in vitro fertilization (IVF) and intracytoplasmic sperm injection (ICSI). METHODS AND MATERIALS: A total of 390 couples undergoing sperm fragmentation prior to receiving conventional IVF (n = 238) or ICSI (n = 152) were evaluated. RESULTS: We found that there were no significant differences in fertilization rate, good embryo rate, or pregnancy rate between high (≥30%) and low (<30%) DFI groups after IVF or ICSI. However, statistically different decreasing motility trends under higher DFI values in the IVF and ICSI groups were detected. Comparison of ROC curve of motility and DFI scores for achieved pregnancy revealed that the best DFI cut-off value was 20%. Also, no significant change was found when 20% DFI level was taken in IVF and ICSI outcomes. CONCLUSION: DFI scores did not provide independent information regarding fertilization, embryo quality, or pregnancy for infertile patients who received IVF or ICSI, but were consistent with semen analysis for infertile couples, regardless of IVF or ICSI outcome.