Journal: Cell and Tissue Research

Article Title: Filamin-A-interacting protein 1 (FILIP1) is a dual compartment protein linking myofibrils and microtubules during myogenic differentiation and upon mechanical stress

doi: 10.1007/s00441-023-03776-4

Figure Lengend Snippet: List of primary antibodies used in this work

Article Snippet: EB3 , EB3 , rabbit pAb , 1:2,000 , Proteintech.

Techniques: Immunofluorescence, Microscopy, Western Blot

Journal: Cell and Tissue Research

Article Title: Filamin-A-interacting protein 1 (FILIP1) is a dual compartment protein linking myofibrils and microtubules during myogenic differentiation and upon mechanical stress

doi: 10.1007/s00441-023-03776-4

Figure Lengend Snippet: FILIP1 expression and localization in differentiating cultured C2C12 myotubes. a , a' Representative western blots showing the levels of FLNc, FILIP1, EB3, tyrosylated tubulin (Tyr-tub) and acetylated tubulin (Ac-tub) in proliferating C2C12 myoblasts (0 days) and myotubes differentiated for the indicated time (1–8 days). GAPDH was used as loading control and for normalization. b – b'''' Quantification of the data presented in ( a – a' ), expressed as mean ± SD. n = 3. In all individual experiments maximum relative expression of each protein was set to 1.0. c – e''' Immunolocalization of FLNc, FILIP1 and EB3 in C2C12 myotubes differentiated for 2 ( c – c''' ), 4 ( d – d''' ) and 6 ( e – e''' ) days. c – c''' FILIP1 and EB3 partially colocalize (arrows), which becomes more evident later in differentiation ( d – d''' , arrows). This is still evident in mature myotubes 6 days after the start of differentiation ( e – e''' , arrows), when FILIP1 and FLNc are mainly present in Z-discs ( e – e''' and f – f''' , arrowheads). A magnification of the boxed area in ( e – e''' ) is shown in ( f – f''' ). Bars: 10 μm

Article Snippet: EB3 , EB3 , rabbit pAb , 1:2,000 , Proteintech.

Techniques: Expressing, Cell Culture, Western Blot, Control

Journal: Cell and Tissue Research

Article Title: Filamin-A-interacting protein 1 (FILIP1) is a dual compartment protein linking myofibrils and microtubules during myogenic differentiation and upon mechanical stress

doi: 10.1007/s00441-023-03776-4

Figure Lengend Snippet: Tyrosylated microtubules flank EPS-induced sarcomeric lesions. a–a''''' Microtubules stained for beta-tubulin show the typical longitudinal orientation in mechanoadapted (mech. adapt.) myotubes ( a – a'' ) while in twitch-paced myotubes many sarcomeric lesions are flanked by microtubules ( a''' – a''''' , arrowheads). b – b'' Immunolocalization of FLNc and EB3 in a C2C12 myotube treated with twitch EPS. The arrowheads indicate sarcomeric lesions marked by FLNc. EB3 is widely expressed throughout the myotube, and appears concentrated in the proximity of these lesions. c – c'' Immunolocalization of FLNc and tyrosylated tubulin (Tyr-tub) in C2C12 myotubes treated with basic EPS ( c – c'' ) and twitch EPS ( c''' – c''''' ). Arrowheads indicate sarcomeric lesions, strongly positive for FLNc, which are flanked by tyrosylated microtubules. d Representative western blots showing the expression level of tyrosylated tubulin (Tyr-tub) and EB3 in mechanoadapted C2C12 myotubes that were twitch EPS treated for the indicated time periods. GAPDH was used as loading and normalization control. e – e' Quantification of the data shown in ( d ) expressed as mean ± S.E.M. n = 3. Significance was assessed using One-way ANOVA and Tukey’s post hoc test or Kruskal–Wallis test and the post hoc Dunn’s multiple comparisons test. No significant differences were found. f – f''''' Immunolocalization of FLNc and acetylated tubulin in C2C12 upon mechanoadaptation ( f – f'' ) or twitch EPS ( f''' – f''''' ). Acetylated tubulin is not particularly arranged in close proximity to lesions ( f''' – f''''' , arrowheads). Bars: 10 μm

Article Snippet: EB3 , EB3 , rabbit pAb , 1:2,000 , Proteintech.

Techniques: Staining, Western Blot, Expressing, Control

Journal: Cell and Tissue Research

Article Title: Filamin-A-interacting protein 1 (FILIP1) is a dual compartment protein linking myofibrils and microtubules during myogenic differentiation and upon mechanical stress

doi: 10.1007/s00441-023-03776-4

Figure Lengend Snippet: FILIP1 mainly colocalizes with FLNc but not with EB3 after EPS-treatment. Immunolocalization of FLNc ( a ), FILIP1 ( b ) and EB3 ( c ) in EPS-treated myotubes reveals the presence of both, FLNc and FILIP1 in the remaining Z-discs (arrowheads) and in lesions (asterisks), while FILIP1 does not colocalize with EB3 (arrows). The merged picture is shown in panel d . Bar: 10 μm

Article Snippet: EB3 , EB3 , rabbit pAb , 1:2,000 , Proteintech.

Techniques:

Journal: bioRxiv

Article Title: Structural and Functional Versatility of the Amyloidogenic Antimicrobial Peptide Citropin 1.3

doi: 10.1101/2025.01.31.635854

Figure Lengend Snippet: A) Time dependent (0, 10, 17 and 20 min) experiments of the interaction between GUVs with a net negative charge (phospholipids panel, colored in magenta in the merged panel) and FITC-labelled citropin 1.3 (citropin panels, colored in green in the merged panel). The addition of the citropin 1.3 induced GUV fusion and the formation of condensates compose of the phospholipids and the peptide (indicated with white triangle). Scale bars, 10 μm. B) FRAP experiment targeting a single droplet (lightning symbol) displaying intensity recovery after bleaching, thereby supporting LLPS. Scale bar, 10 μm.

Article Snippet: Citropin 1.3 from Litoria citropa (Southern bell frog) (Uniprot ID P81846; sequence GLFDIIKKVASVIGGL) and citropin 1.3 labeled with FITC at the N-terminal end were purchased from GL Biochem Ltd. (Shanghai) as lyophilized peptides, at >98% purity.

Techniques:

Journal: bioRxiv

Article Title: Structural and Functional Versatility of the Amyloidogenic Antimicrobial Peptide Citropin 1.3

doi: 10.1101/2025.01.31.635854

Figure Lengend Snippet: Fluorescence live cell microscopy visualizing interactions between 21 μM citropin 1.3 and lung epithelial cells (A-549), tracked using four different fluorophores: citropin 1.3 (1% FITC-labelled and 99% unlabeled), wheat germ agglutinin (WGA), propidium iodide (PI) and Hoechst 33342 with colors reported in legend. A) Cell death induced by citropin 1.3 after 10 minutes of its injection as indicated by positive propidium iodide fluorescence. The colocalization of citropin 1.3 and PI-bound cellular components (i.e., containing nucleic acids) is indicated by white at the FITC and PI channels. B) A frame captured 240 minutes after the addition of citropin 1.3, showing the formation of peptide-rich droplets. C) Positive control showing cell death induced by Triton X. D) Negative control of cells without the addition of citropin 1.3. Scale bar: 10 μm.

Article Snippet: Citropin 1.3 from Litoria citropa (Southern bell frog) (Uniprot ID P81846; sequence GLFDIIKKVASVIGGL) and citropin 1.3 labeled with FITC at the N-terminal end were purchased from GL Biochem Ltd. (Shanghai) as lyophilized peptides, at >98% purity.

Techniques: Fluorescence, Microscopy, Injection, Positive Control, Negative Control

Journal: Cell reports

Article Title: Tau Pathology Drives Dementia Risk-Associated Gene Networks toward Chronic Inflammatory States and Immunosuppression

doi: 10.1016/j.celrep.2020.108398

Figure Lengend Snippet: KEY RESOURCES TABLE

Article Snippet: QuantSeq 3′ End Labeling Kit , Lexogen , Cat# 015.96.

Techniques: Control, Recombinant, Derivative Assay, Protease Inhibitor, End Labeling, Enzyme-linked Immunosorbent Assay, Microarray, Knock-Out, In Vivo, In Vitro, Isolation, Infection, Sequencing, Software, Binding Assay