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ATCC
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Journal: bioRxiv
Article Title: Myeloid Lectin Profiling Identifies SYK as a Targetable Signaling Node for Remodeling Immunosuppressive Tumor-Associated Macrophages in Breast Cancer
doi: 10.64898/2026.09.04.749378
Figure Lengend Snippet: 3D IS-TME prioritizes surface-expressed myeloid lectins. Experimental design of the 3D IS-TME model, comprising aggregated tumor spheroids, fibroblasts and PBMC-derived monocytes, encapsulated in an alginate polymer (A). Percentage of positive cells (relative to live or CD45+ cells) for CD163, CD204 and CD206 (B) or selected lectins (C) from monocytes (Day 0) and recovered macrophages (Day 7) in co-culture with HCC1806, MDA-MB-231 and BT474 cells in the 3D IS-TME. Fold-change in the MFI of CD45+ cells at Day 7 vs Day 0 for each selected lectin in monocytes/macrophages across 3D IS-TME with three different cell lines (D). Statistical significance was determined using one-way ANOVA with Tukeýs multiple comparisons test (B and C) or one sample ratio t-test (D), with p < 0.05 (*), p < 0.01 (**), p < 0.001 (***) and p < 0.0001 (****). N=3 independent biological donors for each cell line.
Article Snippet:
Techniques: Derivative Assay, Polymer, Co-Culture Assay
Journal: Polymers
Article Title: Amylopectin- g -Poly(Acrylic Acid): Synthesis and Application as Reduction Agent for In Situ Formation of Gold Nanoparticles
doi: 10.3390/polym18131636
Figure Lengend Snippet: Cytotoxicity assessment of AMP- g -PAA and AMP- g -PAA/AuNPs in human dermal fibroblasts (HDF) after 48 h exposure. Relative cell viability (%) of HDF cells treated with increasing concentrations (0.125, 0.25, 0.5, and 1 µg/mL) of AMP- g -PAA (dotted light grey bars) and AMP- g -PAA/AuNPs (solid dark grey bars), as determined by the CellTiter-Glo ® Luminescent Cell Viability Assay. Cell viability was normalized to the untreated negative control and measured by ATP-dependent bioluminescence. Numerical values inside each bar indicate mean relative cell viability (%). Data are expressed as mean ± standard deviation from three independent experiments performed in duplicate. Statistical significance was assessed by two-way ANOVA, followed by Dunnett’s multiple comparisons test against the untreated control. ns = not significant ( p > 0.05).
Article Snippet: The cytotoxicity of both the AMP- g -PAA copolymer and the AMP- g -PAA/AuNPs composites was evaluated using a
Techniques: Cell Viability Assay, Negative Control, Standard Deviation, Control
Journal: Bioactive Materials
Article Title: Glycosaminoglycan-functionalized hydrogels for sustained delivery of tissue inhibitor of metalloproteinase-3 mediating matrix metalloprotease inhibition and extracellular matrix stabilization
doi: 10.1016/j.bioactmat.2026.02.010
Figure Lengend Snippet: Biocompatibility of hydrogels. (A-C) Hydrogels were incubated in the respective cell culture media for 72 h, and the obtained extracts were used to assess their effects on the metabolic activity of huMECs (A), vSMCs (B), and NHDFs (C) after 48 h of culture. (D, E) Hydrogel extracts were added to primary human monocytes obtained from five independent donors. The differentiation efficiency of these immune cells into M1 (D) or M2 (E) macrophages was analyzed by flow cytometry using specific markers. (F) Anti-factor Xa activity of HA c and sHA c was determined in comparison with Hep using a chromogenic assay. (A-F) One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. (G) In-vivo assessment of GelMA and GelMA/sHA c hydrogels loaded with TIMP-3. Experimental overview: TIMP-3-loaded GelMA and GelMA/sHA c hydrogels were implanted subcutaneously into BALB/c mice for 14 days. (H) Representative histological images of explanted gels stained for MPO (neutrophils), CD68 (macrophages), CD31 (microvessels), and Sirius red (collagen deposition). The granulation tissue between the muscle tissue and the implant is highlighted by dotted yellow lines. (I-L) Quantification of MPO + and CD68 + cells, CD31 + events, and Sirius red intensity (three ROIs per sample). Statistical analysis was performed using an unpaired t -test with Welch's correction: ∗p < 0.05, ∗∗p < 0.01.
Article Snippet:
Techniques: Incubation, Cell Culture, Activity Assay, Flow Cytometry, Comparison, Chromogenic Assay, In Vivo, Staining
Journal: Bioactive Materials
Article Title: Glycosaminoglycan-functionalized hydrogels for sustained delivery of tissue inhibitor of metalloproteinase-3 mediating matrix metalloprotease inhibition and extracellular matrix stabilization
doi: 10.1016/j.bioactmat.2026.02.010
Figure Lengend Snippet: TIMP-3 maintains protease inhibitory activity in the presence of sHA c and hydrogels release bioactive TIMP-3. (A-D) Influence of soluble GAGs and hydrogel extracts on TIMP-3-mediated inhibition of protease activity in TNF-α-stimulated NHDFs. (A) Schematic of the experimental design. Inflammation was modeled by stimulating NHDFs with TNF-α, inducing increased protease secretion. Gelatinase/collagenase activity in supernatants was quantified using the EnzChek assay with a fluorogenic gelatin substrate in the presence or absence of soluble TIMP-3, soluble GAGs or hydrogel extracts. (B) Protease activity in the supernatants after TNF-α treatment relative to unstimulated controls. (C) Protease activity of TNF-α-stimulated supernatants incubated with soluble GAGs (HA c , sHA c ) with or without TIMP-3. (D) Protease activity of TNF-α-stimulated supernatants incubated with hydrogel extracts (prepared by 72 h hydrogel incubation in medium) in the absence or presence of TIMP-3. One-way ANOVA: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. Only significant differences relative to the Ctrl without TIMP-3 or relative to TIMP-3 alone are shown in C/D. (E) The inhibitory potential of TIMP-3 released from the hydrogels was measured using a MMP-9 activity assay. (F) The ratio of bioactive TIMP-3 to the total amount of released TIMP-3 was calculated and expressed as a fold change relative to GelMA hydrogels without GAGs. (G) Collagen-based ECMs were incubated with collagenase (CHC) for 20 or 60 min with TIMP-3 released from the hydrogels after 24 or 168 h. The remaining collagen was detected after Sirius red staining and elution. Two-way ANOVA for A, B: ∗p < 0.05, ∗∗p < 0.01, ∗∗∗p < 0.001. One-way ANOVA for C: ∗p < 0.05. (H) Molecular rationale for the regulatory role of sHA c on TIMP-3-mediated protease inhibition. The MD-refined complex of TIMP-3 (in grey) with HA6_3AC1 (atom-colored brown sticks, color gradient as in D) is shown superimposed with the TIMP-3/ADAM complex (PDB ID 3CKI ). ADAM is shown in green, and the corresponding TIMP-3 structure has been omitted for clarity.
Article Snippet:
Techniques: Activity Assay, Inhibition, Incubation, Staining