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Image Search Results
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: CD44s forms both trans- and cis- dimers. A, CD44s mainly forms trans-dimers in MDA-MB-231 breast cancer cells. Immunoblots of CD44 and β-actin from MDA-MB-231 single cells and cell clusters, treated with DMSO vehicle control or protein crosslinking agent DSS are shown. The small size, medium size, and big size CD44s monomers are marked as blue (*), pink (#), and black (∧), respectively. Their dimers are labeled as blue (**), pink (##), and black (∧∧) accordingly. B, left panel, immunoblots of anti-FLAG (CD44s) of HEK-293 cell lysates transfected with vector control (V), WT CD44s (WT), and mutant CD44 (M = 6Ns/Q) with six Asn residues converted to Gln for depleted glycosylation. Right panel, immunoblots of CD44s showing its lower molecular mass after PNGase F treatment (PN) which partially cleaves the N-glycans from the glycosylated CD44s. NT, no treatment. C, CD44fl forms both trans- and cis-dimers in ectopic CD44fl-overexpressed single HEK-293 cells and clustered HEK-293 cells. @ indicates the main glycosylated monomer CD44fl band. @@ indicate cis- and trans-dimers. D, CD44 intercellular trans-homophilic interactions in clustered HEK-293 cells detected by co-IP. Left panel, diagram of a two-cell cluster, separately transfected with C-terminal FLAG-tagged and HA-tagged CD44, respectively. Right panel, immunoblots for the CD44-FLAG and CD44-HA proteins upon co-IP with anti-FLAG antibodies using lysates from clustered HEK-293 cells after 48-h transfection. The small size, medium size, and big size CD44s monomers are marked as blue (*), pink (#), and black (∧), respectively. E, CD44 intracellular cis-homophilic interactions in single cells detected by co-IP. Left panel, diagram of single HEK-293 cells co-transfected with both FLAG-tagged and HA-tagged CD44. Right panel, immunoblots for the CD44-FLAG and CD44-HA proteins upon co-IP with anti-FLAG antibodies using lysates from single HEK-293 cells after 48 h transfection. The small size, medium size, and big size CD44s monomers are marked as blue (*), pink (#), and black (∧), respectively.
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques: Western Blot, Labeling, Transfection, Plasmid Preparation, Mutagenesis, Co-Immunoprecipitation Assay
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: Prediction of CD44s extracellular binding sites for homophilic interactions. A, diagram of the CD44fl and CD44s polypeptide chains encoded by shared and distinct exons and the predicted four-domain structure of CD44s. Human CD44fl is encoded by 19 exons, without exon 5a that is mouse specific, and the exons 5a–14 can also generate CD44 variants (v1 to v10) through alternative splicing. CD44s is the smallest CD44 molecule lacking the entire variable region. EX, extracellular domain; TM, transmembrane domain; CT, cytoplasmic domain. B, representative CD44s dimer structure model derived from dimerization predictions. C, top panel, structure model of CD44s monomer with the predicted hot spots in pointed labeling shown in the Domains I and II responsible for dimerization. Red color residues indicate the hot spots within Domain I and the blue color residues in Domain II mutated to alanine. His-92 and Pro-93 are also predicted hot spots in Domain I; however, they are necessary to maintain a turn, so remain intact without mutagenic conversions. Bottom panel lists the amino acid sequences of CD44s-FLAG, dN21–97(ΔN), Domain I mutant (DI), and Domain II mutant (DII).
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques: Binding Assay, Derivative Assay, Labeling, Mutagenesis
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: Mutant CD44 disrupts trans-dimerization and homophilic interactions. A, mutant CD44 (ΔN, DI, and DII) disrupted CD44 trans-dimerization in clustered HEK-293 cells. Top panel, diagram of a cluster of two HEK-293 cells transfected with C-terminal FLAG-tagged wide-type CD44 or CD44 mutants. Bottom panel, immunoblots for the FLAG-tagged CD44 (CD44s, ΔN, DI, and DII) and β-actin, using the lysates of cells treated with DMSO vehicle control or protein crosslinking agent DSS. Blue (*), pink (#), and black (∧) indicate small size, medium size, and big size CD44s monomers, respectively. Pink (##) marks the dominant dimer of CD44s which is absent in CD44 mutant-transfected cells. B, mutant CD44 disrupts trans-homophilic interactions in clustered HEK-293 cells. Top panels, diagram of a cluster of one cell transfected with C-terminal FLAG-tagged CD44 with one cell transfected with HA-tagged CD44. Bottom panels, immunoblots for the FLAG-tagged CD44 and HA-tagged CD44 proteins upon co-IP with anti-HA and anti-FLAG antibodies, respectively. Pink (#) indicates the medium-size CD44s. @ indicates the main monomer band of CD44fl-HA.* indicates a nonspecific band which comes from the lysate or magnetic beads.
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques: Mutagenesis, Transfection, Western Blot, Co-Immunoprecipitation Assay, Magnetic Beads
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: Probabilities of cross-chain interactions for 15 amino acids in Domains I and II Predicted cross-chain interactions (notables besides C97-C97 disulfide bond: **, opposite charges; *, aromatic; ∧ , polar-polar; ∼ , charge-polar; the unlabeled hydrophobic-hydrophobic).
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques:
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: CD44 trans-homophilic interactions are required for PAK2 activation. A, mutant CD44 (ΔN, DI, and DII) decreased PAK2 phosphorylation upon ectopic expression in HEK-293 cells. Immunoblots against HA (ectopic PAK2), p-PAK2 (Ser-20), FLAG (ectopic CD44s WT, ΔN, DI, and DII), and β-actin with HEK-293 cell lysates. B, mutant CD44 (ΔN, DI, and DII) remained in the protein complex with PAK2 detected by immunoblotting of HA (PAK2) and FLAG (CD44) upon co-IP using anti-FLAG (CD44) to pull down clustered HEK-293 cell lysates at 48 h post co-transfection with FLAG-tagged CD44 and HA-tagged PAK2. The small size, medium size, and big size CD44s monomers are marked as blue (*), pink (#), and black (∧), respectively. C, immunoblots of CD44, total PAK2, p-PAK2 (Ser-20), and β-actin expression in MDA-MB-231 cells after 48 h post transfection with siControl (siCon) and siCD44.
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques: Activation Assay, Mutagenesis, Expressing, Western Blot, Co-Immunoprecipitation Assay, Cotransfection, Transfection
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: CD44 mutants disrupt cell-cell aggregation in vitro. A, mutant CD44-transfected HEK-293 cells failed to aggregate. Representative images of aggregation of HEK-293 cells for 0 and 2 h at 48 h post transfection with FLAG-tagged CD44s and FLAG-tagged CD44s mutants (ΔN, DI, and DII). Scale bars, 100 μm. B, quantitative counts of aggregated HEK-293 cells, transfected with FLAG-tagged CD44s, ΔN2, DI, and DII CD44s mutants, in cluster sizes of 2–5, 6–10 and >10 cells. t test; *, p < 0.05.
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques: In Vitro, Mutagenesis, Transfection
Journal: The Journal of Biological Chemistry
Article Title: Extracellular Domains I and II of cell-surface glycoprotein CD44 mediate its trans -homophilic dimerization and tumor cluster aggregation
doi: 10.1074/jbc.RA119.010252
Figure Lengend Snippet: CD44 mutant decreases colonization and cluster formation in the lungs. A, bioluminescence images on day 0 and day 1 post tail vein infusion of L2G-labeled 231-CD44KO cells transfected with vehicle control, FLAG-tagged CD44s, DI, and DII CD44s mutants (left panels) and normalized quantitative images (right panel). t test; *, p < 0.05. B, representative fluorescence images of the dissected lungs ex vivo on day 2 (left panels) and quantitative counts of aggregated big clusters (≥4 cells) (right panel). t test; ***, p < 0.0001.
Article Snippet: For plasmid-cDNA overexpression experiments, pCMV3-C-GFP Spark Control Vector (Sino Biological, CV026), pCMV3-HA-PAK2 (Sino Biological, HG10085-NY),
Techniques: Mutagenesis, Labeling, Transfection, Fluorescence, Ex Vivo
Journal: Cancer discovery
Article Title: Homophilic CD44 interactions mediate tumor cell aggregation and polyclonal metastasis in patient-derived breast cancer models
doi: 10.1158/2159-8290.CD-18-0065
Figure Lengend Snippet: A. Time lapse aggregation images at 0, 4, 8, and 24 h incubation with PDX-derived 1:1 mixtures of tdTomato+ and eGFP+ primary tumor cells. Left column: sorted CD44+; middle column, CD44-; right column, mixed CD44+/CD44- cells in two colors. For details see the Supplementary Videos S6-S8.
Article Snippet: For overexpression experiments in HEK-293 cells, pCMV6-Flag-CD44 (OriGene),
Techniques: Incubation, Derivative Assay
Journal: Cancer discovery
Article Title: Homophilic CD44 interactions mediate tumor cell aggregation and polyclonal metastasis in patient-derived breast cancer models
doi: 10.1158/2159-8290.CD-18-0065
Figure Lengend Snippet: A. The number of proteins with a >2-fold change in CD44+ versus CD44- and siCD44 versus control comparisons: 535 out of 1377, and 382 out of 1523, respectively, with 38 proteins in common. The graph shows the canonical pathways of the 38 overlapped proteins.
Article Snippet: For overexpression experiments in HEK-293 cells, pCMV6-Flag-CD44 (OriGene),
Techniques:
Journal: Cancer discovery
Article Title: Homophilic CD44 interactions mediate tumor cell aggregation and polyclonal metastasis in patient-derived breast cancer models
doi: 10.1158/2159-8290.CD-18-0065
Figure Lengend Snippet: A-C. Kaplan-Meier plot of OS (A), RFS (B), and DMFS (C) for patients with high (red) and low (blue) CD44 (probes 31615_i or 210916_s) expression in breast tumors. Expression was dichotomized at the optimal cut point plotted in GSE3143 (n=158, left panel) and GSE7390 (n=198, right two panels). 95% confidence intervals for each group are indicated by dotted lines. Cox p=0.006, 0.026 and 0.008 as indicated.
Article Snippet: For overexpression experiments in HEK-293 cells, pCMV6-Flag-CD44 (OriGene),
Techniques: Expressing