Publications by authors named "S Yonkovich"
Article Synopsis
- The Wnt coreceptor LRP6 is crucial for activating canonical Wnt signaling and is influenced by specific monoclonal antibodies to regulate its function.
- mAb135, a high-affinity antibody, enhances Wnt signaling while blocking the inhibitory effects of DKK1, indicating its potential role in modulating LRP6.
- Research identified Ser 243 in LRP6's first propeller domain as key for mAb135 binding, revealing this domain's significance in the interaction between LRP6 and DKK1, and suggesting that mAb135 can effectively prevent DKK1 from internalizing LRP6.
IREM-1 is an inhibitory cell surface receptor with an unknown function and is expressed on myeloid cell lineages, including cell lines derived from acute myeloid leukemia (AML) patients. We have generated a series of monoclonal antibodies (mAbs) against the extracellular domain of IREM-1 and further assessed its expression in normal and AML cells. IREM-1 was restricted to cells from myeloid origin and extensive expression analysis in primary cells obtained from AML patients showed IREM-1 expression in leukemic blasts of 72% (39/54) of samples.
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- The R-Spondin (RSpo) family of proteins plays a crucial role in activating the Wnt signaling pathway, although the four members show notable differences in their expression and effects in knockout mice.
- All RSpo proteins can activate the canonical Wnt pathway, with RSpo2 and RSpo3 being more effective than RSpo1, while RSpo4 shows little activity.
- RSpo proteins enhance Wnt signaling by requiring Wnt ligands and LRP6 for function and inhibiting DKK1, which is crucial for their role in amplifying Wnt signaling in biological contexts.
NTB-A is a CD2-related cell surface protein expressed primarily on lymphoid cells including B-lymphocytes from chronic lymphocytic leukaemia (CLL) and lymphoma patients. We have generated a series of monoclonal antibodies (mAbs) against NTB-A and assessed their therapeutic potential for CLL. Selective mAbs to NTB-A were further tested in functional complement-dependent cytotoxicity (CDC) and antibody-dependent cellular cytotoxicty (ADCC) assays in cell lines and B lymphocytes freshly isolated from CLL patients.
View Article and Find Full Text PDFObjective: The platelet-derived growth factor (PDGF) family consists of four members, PDGF A, PDGF B, and 2 new members, PDGF C and PDGF D, which signal through the alpha and beta PDGF receptor (PDGFR) tyrosine kinases. This study was performed to determine the receptor specificity and cellular expression profile of PDGF C.
Methods And Results: PDGF C growth factor domain (GFD) was shown to preferentially bind and activate alpha PDGFR and activate beta PDGFR when it is co-expressed with alpha PDGFR through heterodimer formation.