- https://doi.org/10.1080/17435889.2026.2621728
Self-assembling dendrimer nanoparticles in cancer therapy.
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Take Notes Malignant cancer remains the leading cause of mortality globally, and advancements in nanotechnology-driven nanomedicine are expected to yield promising alternative therapeutic strategies. Dendrimers, as synthetic polymers, possess a broad potential for biomedical applications. In this respect, self-assembling dendrimer nanoparticles derived from amphiphilic dendrimers represent a promising platform for drug delivery in cancer therapy. This potential stems from precise structural characteristics, ease of synthesis, cooperative multivalency, and adaptable assembly behavior. These nanoparticles can encapsulate therapeutic agents, enhance selective accumulation in tumor tissues, facilitate deep penetration, and enable stimulus-responsive drug release, thereby improving therapeutic efficacy while minimizing side effects. In this review, we briefly introduce the self-organizing strategies of self-assembling dendrimers and present representative examples of their applications in cancer chemotherapy, gene therapy, and combination therapy. We also discuss future perspectives for self-assembling dendrimers in personalized and effective cancer nanomedicine. Our goal is to provide valuable insights and inspire further development of self-assembling dendrimers for precision oncology. [Databases searched: Web of Science, PubMed, and Google Scholar; Inclusive dates: 2011-2025].
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Recently, we have described a novel gene, DD3, which is one of the most prostate cancer-specific genes described to date (Bussemakers, M. J. G., van Bokhoven, A., Verhaegh, G. W., Smit, F. P., Karthaus, H. F. M., Schalken, J. A., Debruyne, F. M. J., Ru, N., and Isaacs, W. B. (1999) Cancer Res. 59, 5975-5979). The prostate cancer-specific expression of DD3 indicates that the DD3 gene promoter is a promising tool for the treatment of prostate cancer. To identify the promoter elements that are responsible for the prostate cancer-specific expression of DD3, we have isolated and characterized the DD3 promoter. Sequence analysis of the DD3 5'-flanking region was performed and several promoter-human growth hormone reporter constructs were prepared, which were transiently transfected in the DD3-positive cell line LNCaP and several DD3-negative cell lines. Using a 500-base pair DD3 promoter construct, we could detect promoter activity in LNCaP cells, which was not affected by increasing the size of the constructs. Truncated constructs, however, showed an increased transcriptional activity, suggesting the presence of a silencer that negatively regulates the expression of DD3. DNase-I footprint analysis, using nuclear extracts from LNCaP cells, revealed the presence of three DNase-I-protected areas within the DD3 proximal promoter. We show that the high mobility group I(Y) protein binds to one of the DNase-I-protected areas and recruits another, yet unidentified, protein to the DD3 promoter in LNCaP cells.
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