CD137 (4-1BB) is a costimulatory molecule that can be manipulated for the treatment of cancer and autoimmune disease. Although it is known that agonistic antibodies (mAbs) against CD137 enhance the rejection of murine tumors in a natural killer (NK) cell-and T celldependent fashion, the mechanism for NK dependence is poorly understood. In this study, we evaluated the ability of 2 different glycoforms of a chimerized antihuman CD137 mAb, an aglycosylated (GA) and a low fucose form (GG), to react with human NK cells. Both mAbs bound similarly to CD137 and partially blocked the interaction between CD137 and CD137 ligand. However, unlike GA mAb, immobilized GG mAb activated NK cells and enhanced CD137 expression. These effects were seemingly dependent on
These data have both prognostic and therapeutic relevance and support the design of a prospective trial to determine the influence of FcgammaRIIIa polymorphisms on the clinical outcome of patients with SCCHN treated with alpha-EGFR mAbs.
The diamagnetic iron(II) complexes of the hydrazone ligand pyridinecarboxaldehyde-2‘-pyridylhydrazone (papyH)
have been characterized by NMR, IR, UV−vis, and electrochemistry. The dication Fe(papyH)2
2+ undergoes reversible
one-electron oxidation at 0.66 V vs internal ferrocene and shows a strong metal−ligand charge-transfer band in the
visible region at 524 nm. Deprotonation with NaOH gives diamagnetic, neutral Fe(papy)2 with an oxidation potential
of −0.25 V vs internal ferrocene and a charge-transfer band at 603 nm. Fe(papy)2 reacts with active alkylating
agents to give dialkyl complexes Fe(papyR)2
2+ with spectroscopic properties similar to those of Fe(papyH)2
2+.
Monitoring the alkylation by UV−vis reveals the intermediacy of a monoalkylated species.
Immunity to previously encountered diseases is provided in large part by memory T lymphocytes, which may be subdivided based on phenotypic and functional differences, as well as the specific cellular compartments in which these cells reside. The bone marrow (BM) is a unique microenvironment that supports robust proliferation and recall responses of both "central" and "effector" memory T cells, particularly within the CD8+ T cell subset. The recent identification within human BM of a population of CD8+ effector memory T cells with hybrid phenotype and enhanced cytotoxic function has important implications for the development of future immunotherapies. Using activated BM CD8+ memory T cells for adoptive transfer or targeting such cells with tailored vaccines may improve the ability of these classic modalities to produce potent and long-lasting antigen-specific responses, ultimately leading to clinically significant control of viral and malignant diseases.
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