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Collection of stem cells in (autologous) donors by apheresis
Published in Cut Adeya Adella, Stem Cell Oncology, 2018
As discussed, in the bone cavity, HPCs are bound to stromal cells and various extracellular proteins. Administration of G-CSF leads to the release of a variety of serine proteases from granulocytes. This takes days. These proteases disrupt the binding between stromal cells and stem cells and with it the release of the HPCs in the peripheral circulation. Unfortunately, G-CSF mobilization has a 5-30% failure rate among healthy donors and patients. Risk factors for a sub-optimal HPC mobilization are ages above 60 years, disease status, duration of the previous chemo- and radiotherapy. Mobilization in patients is preferably achieved with chemotherapy followed with G-CSF (“chemo mobilization”). Usually, a higher number of stem cells are available in the peripheral blood stream for harvesting than after G-CSF only. Since some years, plerixafor became available for autologous HPC mobilization. Plerixafor leads direct antibody mediated interference with the CXCR4 receptor binding leading to peak levels of CD34-positive cells in the peripheral circulation 6-9 hours after administration. Plerixafor is used in combination with G-CSF when G-CSF mobilization shows to be insufficient.
Peptide-enabled receptor-binding-quantum dots for enhanced detection and migration inhibition of cancer cells
Published in Journal of Biomaterials Science, Polymer Edition, 2020
Ruijuan Zu, Xiaocui Fang, Yuchen Lin, Shilin Xu, Jie Meng, Haiyan Xu, Yanlian Yang, Chen Wang
Dedicated efforts have been reported on studying chemokine receptor CXCR4 as a potential therapeutic target for cancer diagnosis and treatment [10]. One small molecule antagonist named as plerixafor (also termed as AMD3100) has been approved by the U.S. Food and Drug Administration (FDA) for non-Hodgkin’s lymphoma and multiple myeloma treatment [11,12]. Several other CXCR4 antagonist candidates are currently being evaluated in various stages of clinical development. In our previous study, we selected a series of potential peptide antagonists with designated sequences in our original experiments according to the extracellular domain of CXCR4. The binding strengths between peptide antagonists and CXCR4 were examined using flow cytometry, surface plasmon resonance (SPR), and confocal microscopy methods. Our results demonstrated that, peptide E5 (GGRSFFLLRRIQGCRFRNTVDD) shows high binding affinity and selectivity towards CXCR4-overexpressed cancer cells [13]. E5 was observed to inhibit the migration and adhesion of cancer cells, and increase the sensitivity of cancer cells to chemotherapeutic agents by antagonizing CXCR4/CXCL12 chemokine axis [13–15].