biotinylated lectins  (Vector Laboratories)

Journal: Neural Regeneration Research

Article Title: Complement-dependent neuroinflammation in spinal cord injury: from pathology to therapeutic implications

doi: 10.4103/NRR.NRR-D-24-00116

Figure Lengend Snippet: Overview of complement activation pathways. Created with BioRender.com. C: Complement; DAMPs: damage-associated molecular patterns; MBL: mannose-binding lectins; PAMPs: pathogen associated molecular patterns.

Article Snippet: The pattern of activation of the lectin pathway is similar and is initiated when soluble defense proteins like ficolins and mannose-binding lectins (MBL) bind to mannose-containing carbohydrate residues on pathogenic or stressed cellular surfaces (Alawieh et al., 2015a).

Techniques: Activation Assay, Binding Assay

Journal: Neural Regeneration Research

Article Title: Complement-dependent neuroinflammation in spinal cord injury: from pathology to therapeutic implications

doi: 10.4103/NRR.NRR-D-24-00116

Figure Lengend Snippet: Triggers of complement activation after spinal cord injury. Complement pathways are activated by either the direct binding of opsonins to stressed and degenerating cells, or by antibodies that recognize DAMPs. An alternative mechanism also involves binding to CRP (an acute phase reactant). These mechanisms involve the classical and alternative pathways of C. The lectin pathway has not yet been investigated. Created with BioRender.com. C: Complement; CRP: C-reactive protein; DAMPs: damage-associated molecular patterns; MBL: mannose-binding lectins.

Article Snippet: The pattern of activation of the lectin pathway is similar and is initiated when soluble defense proteins like ficolins and mannose-binding lectins (MBL) bind to mannose-containing carbohydrate residues on pathogenic or stressed cellular surfaces (Alawieh et al., 2015a).

Techniques: Activation Assay, Binding Assay

Journal: Neural Regeneration Research

Article Title: Complement-dependent neuroinflammation in spinal cord injury: from pathology to therapeutic implications

doi: 10.4103/NRR.NRR-D-24-00116

Figure Lengend Snippet: Inhibitors of complement activation after spinal cord injury. The figure shows the different pathways of C activation and the sites of action of different endogenous and exogenous inhibitors. (1) Inhibitors of the antibody-complement axis include genetic models of Rag1 deficiency, B-cell depletion, and Fc-gamma receptor in addition to the fusion protein B4-Crry that inhibits the bind of B4IgM to modified annexin IV. (2) Inhibitors of the classical pathway include genetic deficiency in C1q or use of C1-inhibitor (C1-INH). (3) Inhibitors of C3 convertase from all pathways include the fusion proteins B4-Crry and CR2-Crry, soluble CR1 (sCR1), and C3 deficiency. (4) Inhibition of the alternative pathway C3 convertase via factor B deficiency. (5) Inhibition of C3a-C3aR1 interaction via C3aR1 deficiency. (6) Inhibition of C5a-C5aR interaction using C5aR1 antagonist (PMX-205), C5aR1 deficiency or C5aR2 deficiency. (7) Inhibition of membrane attack complex includes C5 deficiency and C6 deficiency. Created with BioRender.com. C: Complement; DAMPs: damage-associated molecular patterns; MBL: mannose-binding lectins; PAMPs: pathogen associated molecular patterns.

Article Snippet: The pattern of activation of the lectin pathway is similar and is initiated when soluble defense proteins like ficolins and mannose-binding lectins (MBL) bind to mannose-containing carbohydrate residues on pathogenic or stressed cellular surfaces (Alawieh et al., 2015a).

Techniques: Activation Assay, Modification, Inhibition, Membrane, Binding Assay

Journal: Biomedical Reports

Article Title: Black rice bran‑derived anthocyanins attenuate cholangiocarcinoma cell migration via the alteration of epithelial‑mesenchymal transition and sialylation

doi: 10.3892/br.2024.1906

Figure Lengend Snippet: Glycan expression in CCA cell lines evaluated by staining with a panel of 16 lectins.

Article Snippet: A total of 16 biotinylated lectins and ABC-peroxidase solution (cat. no. PK-4000) were purchased from Vector Laboratories, Inc. (Maravai LifeSciences).

Techniques: Expressing, Staining

Journal: Cell & Bioscience

Article Title: Maladaptive changes in the homeostasis of AEA-TRPV1/CB1R induces pain-related hyperactivity of nociceptors after spinal cord injury

doi: 10.1186/s13578-025-01345-6

Figure Lengend Snippet: TRPV1 and CB1R are upregulated in nociceptors following SCI. A Schematic of the experimental design (top) and representative Western blots (bottom) showing the TRPV1 and CB1R levels in DRGs from the sham group or at different time points after SCI. B Statistics for the TRPV1 and CB1R levels from ( A ) using a one-way ANOVA with Dunnett’s post hoc test. *p < 0.05, **p < 0.01. C Immunofluorescence of TRPV1 (red) with CGRP (green, top), IB4 (green, middle), and NF200 (green, below) in DRG neurons in the sham and 28 days post-SCI groups. Scale bar, 50 μm. Scale bar of the enlarged view, 12.5 μm. D Statistics of co-localization of TRPV1 with CGRP, IB4, and NF200 in DRG neurons in the sham and 28 days post-SCI groups using a Fisher’s exact test. *p < 0.05, **p < 0.01. n.s., not significant. E Immunofluorescence of CB1R (red) with CGRP (green, top), IB4 (green, middle), and NF200 (green, below) in DRG neurons in the sham and 28 days post-SCI groups. Scale bar, 50 μm. Scale bar of the enlarged view, 12.5 μm. F Statistics of co-localization of CB1R with CGRP, IB4, and NF200 in DRG neurons in the sham and 28 days post-SCI groups using a Fisher’s exact test. **p < 0.01

Article Snippet: DRG neurons (L4-L5) were fixed in 4% paraformaldehyde (PFA) for 12 h and then dehydrated in a 30% sucrose solution for over 2 nights at 4 °C for 36–48 h. Longitudinal sections of DRG (14 μm) were made using a cryostat (CM1950, Leica, GER), and then incubated with primary antibodies for TRPV1 (1:100, Alomone, IL) and CB1R (1:100, Alomone, IL) in combination with antibodies for neurofilament-200 (NF200, 1:500, Abcam, UK), calcitonin gene-related peptide (CGRP, 1:200, Abcam, UK), and isolectin B4 (IB4, 1:100, Sigma, USA).

Techniques: Western Blot, Immunofluorescence