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anti mor1 mouse monoclonal antibody  (Santa Cruz Biotechnology)


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    Santa Cruz Biotechnology anti mor1 mouse monoclonal antibody
    Figure 4. Decreased expression of Oprm1 mRNA and protein with icKO. (A) Quantitative analysis of Oprm1 mRNA expression in the medial prefrontal cortex (mPFC), CA1-CA2 areas and dentate gyrus (DG) of the hippocampus, caudate putamen (CPu), nucleus accumbens (NAc), and the ventral tegmental area (VTA). Two-way ANOVA revealed a significant effect of genotype [F (1, 24) = 519.3, p < 0.001]. A Bonferroni post hoc test showed that Oprm1 icKO mice expressed significantly less Oprm1 mRNA in all brain regions of interest. n = 3 mice per group; 2 sections per mouse; 15 regions of interest (ROI) per data point. ROI was defined by a 15 µm circle over a field that contained at least one green-turquoise (Fast Green; labeling Aldh1 mRNA) punctum within an astrocyte, as seen in B. (B) Co-localization of Oprm1 mRNA expression (red dots) surrounding randomly selected Aldh1l1 mRNA expression loci (green-turquoise dots). The radius of the black circle (ROI) is 15 µm (707 µm2). Pixels for red (Fast Red) Oprm1 mRNA staining were counted within the ROI. (C,D) Representative images of sections counterstained with 50% Gill’s hematoxylin 1 to disclose tissue morphology, i.e., the cell nuclei (purple). The black circle denotes the ROI shown in B. (E,F) Quantitative analysis of Western blots revealed significantly decreased expression of astrocytic <t>MOR1</t> in Oprm1 icKO mice (Student’s t test; t = 23.22, p < 0.0001). n = 4 mice per group; Error bars indicate SEM. *** p < 0.001, **** p < 0.0001.
    Anti Mor1 Mouse Monoclonal Antibody, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mor1/MOR-1+Antibody/pm37408246-213-10-16
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    Images

    1) Product Images from "Loss of Astrocytic µ Opioid Receptors Exacerbates Aversion Associated with Morphine Withdrawal in Mice: Role of Mitochondrial Respiration."

    Article Title: Loss of Astrocytic µ Opioid Receptors Exacerbates Aversion Associated with Morphine Withdrawal in Mice: Role of Mitochondrial Respiration.

    Journal: Cells

    doi: 10.3390/cells12101412

    Figure 4. Decreased expression of Oprm1 mRNA and protein with icKO. (A) Quantitative analysis of Oprm1 mRNA expression in the medial prefrontal cortex (mPFC), CA1-CA2 areas and dentate gyrus (DG) of the hippocampus, caudate putamen (CPu), nucleus accumbens (NAc), and the ventral tegmental area (VTA). Two-way ANOVA revealed a significant effect of genotype [F (1, 24) = 519.3, p < 0.001]. A Bonferroni post hoc test showed that Oprm1 icKO mice expressed significantly less Oprm1 mRNA in all brain regions of interest. n = 3 mice per group; 2 sections per mouse; 15 regions of interest (ROI) per data point. ROI was defined by a 15 µm circle over a field that contained at least one green-turquoise (Fast Green; labeling Aldh1 mRNA) punctum within an astrocyte, as seen in B. (B) Co-localization of Oprm1 mRNA expression (red dots) surrounding randomly selected Aldh1l1 mRNA expression loci (green-turquoise dots). The radius of the black circle (ROI) is 15 µm (707 µm2). Pixels for red (Fast Red) Oprm1 mRNA staining were counted within the ROI. (C,D) Representative images of sections counterstained with 50% Gill’s hematoxylin 1 to disclose tissue morphology, i.e., the cell nuclei (purple). The black circle denotes the ROI shown in B. (E,F) Quantitative analysis of Western blots revealed significantly decreased expression of astrocytic MOR1 in Oprm1 icKO mice (Student’s t test; t = 23.22, p < 0.0001). n = 4 mice per group; Error bars indicate SEM. *** p < 0.001, **** p < 0.0001.
    Figure Legend Snippet: Figure 4. Decreased expression of Oprm1 mRNA and protein with icKO. (A) Quantitative analysis of Oprm1 mRNA expression in the medial prefrontal cortex (mPFC), CA1-CA2 areas and dentate gyrus (DG) of the hippocampus, caudate putamen (CPu), nucleus accumbens (NAc), and the ventral tegmental area (VTA). Two-way ANOVA revealed a significant effect of genotype [F (1, 24) = 519.3, p < 0.001]. A Bonferroni post hoc test showed that Oprm1 icKO mice expressed significantly less Oprm1 mRNA in all brain regions of interest. n = 3 mice per group; 2 sections per mouse; 15 regions of interest (ROI) per data point. ROI was defined by a 15 µm circle over a field that contained at least one green-turquoise (Fast Green; labeling Aldh1 mRNA) punctum within an astrocyte, as seen in B. (B) Co-localization of Oprm1 mRNA expression (red dots) surrounding randomly selected Aldh1l1 mRNA expression loci (green-turquoise dots). The radius of the black circle (ROI) is 15 µm (707 µm2). Pixels for red (Fast Red) Oprm1 mRNA staining were counted within the ROI. (C,D) Representative images of sections counterstained with 50% Gill’s hematoxylin 1 to disclose tissue morphology, i.e., the cell nuclei (purple). The black circle denotes the ROI shown in B. (E,F) Quantitative analysis of Western blots revealed significantly decreased expression of astrocytic MOR1 in Oprm1 icKO mice (Student’s t test; t = 23.22, p < 0.0001). n = 4 mice per group; Error bars indicate SEM. *** p < 0.001, **** p < 0.0001.

    Techniques Used: Expressing, Labeling, Staining, Western Blot

    Related Articles

    Staining:

    Article Title: Two-photon imaging in mice shows striosomes and matrix have overlapping but differential reinforcement-related responses
    Article Snippet: .. For staining, sections were first rinsed 3 × 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Polyclonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4°C, the sections were rinsed in PBS-Tx (3 × 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey anti-chicken, Invitrogen, 1:300) and Alexa Fluor 647 (donkey anti-goat, Invitrogen, 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 × 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Article Title: Two-Photon Imaging of Striatum Demonstrates Distinct Functions for Striosomes and Matrix in Reinforcement Learning
    Article Snippet: .. For staining, sections were first rinsed 3 x 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Polyclonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4oC, the sections were rinsed in PBS-Tx (3 x 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey anti-chicken (Invitrogen), 1:300) and Alexa Fluor 647 (Alexa Fluor 647, donkey anti-goat (Invitrogen), 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 x 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Article Title: Two-photon imaging in mice shows striosomes and matrix have overlapping but differential reinforcement-related responses
    Article Snippet: .. For staining, sections were first rinsed 3 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Poly- clonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4 ̊C, the sections were rinsed in PBS-Tx (3 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey antichicken, Invitrogen, 1:300) and Alexa Fluor 647 (donkey anti-goat, Invitrogen, 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Incubation:

    Article Title: Two-photon imaging in mice shows striosomes and matrix have overlapping but differential reinforcement-related responses
    Article Snippet: .. For staining, sections were first rinsed 3 × 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Polyclonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4°C, the sections were rinsed in PBS-Tx (3 × 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey anti-chicken, Invitrogen, 1:300) and Alexa Fluor 647 (donkey anti-goat, Invitrogen, 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 × 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Article Title: Two-Photon Imaging of Striatum Demonstrates Distinct Functions for Striosomes and Matrix in Reinforcement Learning
    Article Snippet: .. For staining, sections were first rinsed 3 x 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Polyclonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4oC, the sections were rinsed in PBS-Tx (3 x 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey anti-chicken (Invitrogen), 1:300) and Alexa Fluor 647 (Alexa Fluor 647, donkey anti-goat (Invitrogen), 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 x 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Article Title: Two-photon imaging in mice shows striosomes and matrix have overlapping but differential reinforcement-related responses
    Article Snippet: .. For staining, sections were first rinsed 3 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Poly- clonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4 ̊C, the sections were rinsed in PBS-Tx (3 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey antichicken, Invitrogen, 1:300) and Alexa Fluor 647 (donkey anti-goat, Invitrogen, 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Blocking Assay:

    Article Title: Two-photon imaging in mice shows striosomes and matrix have overlapping but differential reinforcement-related responses
    Article Snippet: .. For staining, sections were first rinsed 3 × 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Polyclonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4°C, the sections were rinsed in PBS-Tx (3 × 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey anti-chicken, Invitrogen, 1:300) and Alexa Fluor 647 (donkey anti-goat, Invitrogen, 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 × 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Article Title: Two-Photon Imaging of Striatum Demonstrates Distinct Functions for Striosomes and Matrix in Reinforcement Learning
    Article Snippet: .. For staining, sections were first rinsed 3 x 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Polyclonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4oC, the sections were rinsed in PBS-Tx (3 x 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey anti-chicken (Invitrogen), 1:300) and Alexa Fluor 647 (Alexa Fluor 647, donkey anti-goat (Invitrogen), 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 x 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).

    Article Title: Two-photon imaging in mice shows striosomes and matrix have overlapping but differential reinforcement-related responses
    Article Snippet: .. For staining, sections were first rinsed 3 5 min in PBS-Tx (0.01 M PBS + 0.2% Triton X-100), then were incubated in blocking buffer (Perkin Elmer TSA Kit) for 20 min followed by incubation with primary antibodies for GFP (Polyclonal, chicken, Abcam ab13970, 1:2000) and MOR1 (Poly- clonal, goat, Santa Cruz sc-7488, 1:500). .. After two nights of incubation at 4 ̊C, the sections were rinsed in PBS-Tx (3 5 min), incubated in secondary antibodies Alexa Fluor 488 (donkey antichicken, Invitrogen, 1:300) and Alexa Fluor 647 (donkey anti-goat, Invitrogen, 1:300) for 2 hr at room temperature, rinsed in 0.1 M PB (3 5 min), mounted and covered with a coverslip with ProLong Gold mounting medium with DAPI (Thermo Fisher Scientific).



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    Molecular and phenotypic analyses of the MOR1-3xYPet constructs in the wild-type (Col-0) background and in the mor1-6 and mor1-23 mutant backgrounds. (A) Structure of the Arabidopsis MOR1 genomic sequence. Three MOR1 mutant alleles are shown: mor1-1 (C1626T), mor1-6 (G7127A), and mor1-23 (SALK_032056). Black boxes represent exons, horizontal lines represent introns, and white boxes represent 5’ and 3’ untranslated regions (UTRs). qPCR primers were designed to amplify a region spanning exons 3 and 4 (marked in blue). (B) The MOR1 protein contains five TOG domains and a conserved C-terminal R4 domain. Mutant proteins include mor1-1 L174F , mor1-6 (splice mutation before amino acid 869), and mor1- 23 (T-DNA insertion). The linker between TOG1 and TOG2 was used as the antigen for creating the MOR1 antibody . Two C-terminal fusion proteins were generated: MOR1-3xYPet (three copies of YPet attached to MOR1), and mor1-1-YPet (one copy of YPet attached to mor1-1 L174F ). (C) RT-PCR analysis of mor1-23 and mor1-6 mutant backgrounds. For mor1-23 , primers failed to amplify through the 3xYPet sequence or the mor1-23 T-DNA insertion. For mor1-6 , blue arrows indicate wild-type cDNA amplicons when introns are correctly spliced, and magenta arrows indicate amplicons longer than wild-type cDNA but shorter than genomic DNA due to a retained intron. Forward and reverse primer binding sites are indicated below each gel. Exon- intron structures are confirmed by sequencing and marked with arrows corresponding to the amplicons. The premature stop codon within the intron is marked red. (D) RT-qPCR and digital PCR (dPCR) analysis of MOR1 transcript levels when MOR1-3xYPet was expressed in Col-0, mor1-23 , and mor1-6 backgrounds. Primers bind exons 3 and 4 as shown in (A) . Bars and error bars represent mean values of 3 technical replicates ± SE. (E) Western blot analysis of MOR1 proteins in seedling protein extracts. The affinity-purified MOR1 polyclonal antibody labelled 218 kDa bands (endogenous MOR1 protein), 300 kDa bands (MOR1-3xYPet), and bands with lower molecular weights (approx. 125 and 160 kDa). (F) Representative images showing root tip morphologies of 7-day old seedlings including wild- type Col-0, homozygous mor1-23 , heterozygous mor1-6 , and MOR1-3xYPet expressed in Col-0, mor1-23 , and mor1-6 backgrounds. Scale bar represents 0.5 mm. Sample sizes: 14-16 seedlings. (G) Mean root length (in cm) of genotypes shown in F . Bars and error bars represent mean ± SD. Kruskal-Wallis p = 3.69E-9. Letters represent statistical differences between genotypes revealed by Dunn’s test. (H) Confocal micrographs of MOR1-3xYPet in wild-type, mor1-23 , and mor1-6 backgrounds, as seen in etiolated hypocotyl cells. MOR1-3xYPet is more tightly localized to microtubule tips in the mor1-23 and mor1-6 backgrounds while distributed along the microtubule lattice in the wild- type background. Scale bars represent 10 μm.

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: Molecular and phenotypic analyses of the MOR1-3xYPet constructs in the wild-type (Col-0) background and in the mor1-6 and mor1-23 mutant backgrounds. (A) Structure of the Arabidopsis MOR1 genomic sequence. Three MOR1 mutant alleles are shown: mor1-1 (C1626T), mor1-6 (G7127A), and mor1-23 (SALK_032056). Black boxes represent exons, horizontal lines represent introns, and white boxes represent 5’ and 3’ untranslated regions (UTRs). qPCR primers were designed to amplify a region spanning exons 3 and 4 (marked in blue). (B) The MOR1 protein contains five TOG domains and a conserved C-terminal R4 domain. Mutant proteins include mor1-1 L174F , mor1-6 (splice mutation before amino acid 869), and mor1- 23 (T-DNA insertion). The linker between TOG1 and TOG2 was used as the antigen for creating the MOR1 antibody . Two C-terminal fusion proteins were generated: MOR1-3xYPet (three copies of YPet attached to MOR1), and mor1-1-YPet (one copy of YPet attached to mor1-1 L174F ). (C) RT-PCR analysis of mor1-23 and mor1-6 mutant backgrounds. For mor1-23 , primers failed to amplify through the 3xYPet sequence or the mor1-23 T-DNA insertion. For mor1-6 , blue arrows indicate wild-type cDNA amplicons when introns are correctly spliced, and magenta arrows indicate amplicons longer than wild-type cDNA but shorter than genomic DNA due to a retained intron. Forward and reverse primer binding sites are indicated below each gel. Exon- intron structures are confirmed by sequencing and marked with arrows corresponding to the amplicons. The premature stop codon within the intron is marked red. (D) RT-qPCR and digital PCR (dPCR) analysis of MOR1 transcript levels when MOR1-3xYPet was expressed in Col-0, mor1-23 , and mor1-6 backgrounds. Primers bind exons 3 and 4 as shown in (A) . Bars and error bars represent mean values of 3 technical replicates ± SE. (E) Western blot analysis of MOR1 proteins in seedling protein extracts. The affinity-purified MOR1 polyclonal antibody labelled 218 kDa bands (endogenous MOR1 protein), 300 kDa bands (MOR1-3xYPet), and bands with lower molecular weights (approx. 125 and 160 kDa). (F) Representative images showing root tip morphologies of 7-day old seedlings including wild- type Col-0, homozygous mor1-23 , heterozygous mor1-6 , and MOR1-3xYPet expressed in Col-0, mor1-23 , and mor1-6 backgrounds. Scale bar represents 0.5 mm. Sample sizes: 14-16 seedlings. (G) Mean root length (in cm) of genotypes shown in F . Bars and error bars represent mean ± SD. Kruskal-Wallis p = 3.69E-9. Letters represent statistical differences between genotypes revealed by Dunn’s test. (H) Confocal micrographs of MOR1-3xYPet in wild-type, mor1-23 , and mor1-6 backgrounds, as seen in etiolated hypocotyl cells. MOR1-3xYPet is more tightly localized to microtubule tips in the mor1-23 and mor1-6 backgrounds while distributed along the microtubule lattice in the wild- type background. Scale bars represent 10 μm.

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: Construct, Mutagenesis, Sequencing, Generated, Reverse Transcription Polymerase Chain Reaction, Binding Assay, Quantitative RT-PCR, Digital PCR, Western Blot, Affinity Purification

    MOR1 binds strongly to microtubule plus ends during microtubule growth, catastrophe and rescue and weakly to the microtubule lattice. (A) A spinning-disc confocal image of MOR1-3xYPet (red) on the plus ends of microtubules (cyan). See Supplementary Movie S1. The dotted line marks one microtubule used for fluorescence intensity measurements in (B) . Scale bar represents 5 μm. (B) Fluorescence intensity plots of MOR1-3xYPet and mRFP-TUB6 line scans of microtubule plus ends. Bars and error bars represent average intensities from 12 line scans ± SD. (C) Time-lapse montage of spinning-disc confocal images showing MOR1-3xYPet’s (red) ability to track the plus ends of growing microtubules (cyan). The yellow circles indicate a microtubule plus end. The white dotted line indicates the selection used to generate the kymograph in (D) . Scale bar represents 10 μm. See Supplementary Movie S1. (D) Kymograph of line selection in (C) , collected over 105 s. Scale bar represents 3 μm. (E) Time-lapse montage of spinning-disc confocal images of MOR1-3xYPet (red) and mRFP- TUB6 (cyan). MOR1-3xYPet is indicated on microtubule plus end during growth (t = 0-10 s, yellow circle), catastrophe (t = 15-30 s, white circle), and rescue (t = 35-45 s, yellow circle). The dotted line indicates the selection used to create the kymograph in (F) . Scale bar represents 5 μm. See Supplementary Movie S2. (F) Kymographs of line selection seen in (E) , collected over 1 0 s. Scale bar represents 5 μm. (G) Time-lapse montage of spinning-disc confocal images of MOR1-3xYPet (red) and mRFP- TUB6 (cyan) showing the polymerizing plus end (yellow circle) and depolymerizing minus end (arrowhead) of a treadmilling microtubule. Scale bar represents 5 μm. See Supplementary Movie S3. (H) Time-lapse montage of spinning-disc confocal images of MOR1-3xYPet (red) during microtubule (cyan) crossover and severing. Crossover (t = 25-30 s) is followed by severing (t = 30 s, arrowhead). The newly generated plus end undergoes rapid shrinkage. MOR1-3xYPet is recruited within 5 s (t = 35s, white circle) and tracks the shrinking plus end (t = 35-45 s). MOR1- 3xYPet remains at the growing microtubule’s plus end (yellow circle) throughout. Scale bar represents 5 μm. See Supplementary Movie S4. In the schematic diagram, a growing microtubule (blue) with MOR1 (red circle) crosses over an obstacle microtubule (blue) (t 1 -t 2 ). Following crossover (arrowhead), MOR1 tracks the existing, growing plus end as well as the newly generated, shrinking plus end (t 3 -t 4 ). + and – indicate the plus and minus ends, respectively. (I, J) Confocal imaging of MOR1-3xYPet (red) and mRFP-TUB6 (cyan) in (I) live and (J) fixed etiolated hypocotyl cells ( mor1-23 background). In live cells, MOR1-3xYPet is plus-end localized. In chemically fixed cells, MOR1-3xYPet is no longer plus-end localized and instead becomes cytoplasmic. Scale bars represent 20 μm. (K, L) Confocal imaging of MOR1-3xYPet (red) and EB1b-mCherry (cyan) in (K) live and (L) fixed cells (wild-type background). In live cells, MOR1-3xYPet is localized along the microtubule lattice, and EB1b-mCherry is plus-end localized; in chemically fixed cells, MOR1-3xYPet no longer appears on microtubule plus ends but still labelled lattice, and EB1b-mCherry is not localized to microtubules and instead becomes cytoplasmic. Scale bars represent 20 μm. (M, N) MOR1 is detected in low abundance along the microtubule lattice by altering imaging settings on the TIRF microscope. Live-cell images are taken from the etiolated hypocotyls of MOR1-3xYPet/mor1-23 seedlings. (M) Comparison of images obtained with a 200 ms and 4000 ms exposure time. White brackets indicate the average distance that a single MOR1-3xYPet puncta will travel over a 4000 ms time period. Scale bars represent 5 μm. (N) Comparison of images obtained by increasing the laser intensity from 13% to 70% while maintaining the same exposure time. Scale bars represent 5 μm.

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: MOR1 binds strongly to microtubule plus ends during microtubule growth, catastrophe and rescue and weakly to the microtubule lattice. (A) A spinning-disc confocal image of MOR1-3xYPet (red) on the plus ends of microtubules (cyan). See Supplementary Movie S1. The dotted line marks one microtubule used for fluorescence intensity measurements in (B) . Scale bar represents 5 μm. (B) Fluorescence intensity plots of MOR1-3xYPet and mRFP-TUB6 line scans of microtubule plus ends. Bars and error bars represent average intensities from 12 line scans ± SD. (C) Time-lapse montage of spinning-disc confocal images showing MOR1-3xYPet’s (red) ability to track the plus ends of growing microtubules (cyan). The yellow circles indicate a microtubule plus end. The white dotted line indicates the selection used to generate the kymograph in (D) . Scale bar represents 10 μm. See Supplementary Movie S1. (D) Kymograph of line selection in (C) , collected over 105 s. Scale bar represents 3 μm. (E) Time-lapse montage of spinning-disc confocal images of MOR1-3xYPet (red) and mRFP- TUB6 (cyan). MOR1-3xYPet is indicated on microtubule plus end during growth (t = 0-10 s, yellow circle), catastrophe (t = 15-30 s, white circle), and rescue (t = 35-45 s, yellow circle). The dotted line indicates the selection used to create the kymograph in (F) . Scale bar represents 5 μm. See Supplementary Movie S2. (F) Kymographs of line selection seen in (E) , collected over 1 0 s. Scale bar represents 5 μm. (G) Time-lapse montage of spinning-disc confocal images of MOR1-3xYPet (red) and mRFP- TUB6 (cyan) showing the polymerizing plus end (yellow circle) and depolymerizing minus end (arrowhead) of a treadmilling microtubule. Scale bar represents 5 μm. See Supplementary Movie S3. (H) Time-lapse montage of spinning-disc confocal images of MOR1-3xYPet (red) during microtubule (cyan) crossover and severing. Crossover (t = 25-30 s) is followed by severing (t = 30 s, arrowhead). The newly generated plus end undergoes rapid shrinkage. MOR1-3xYPet is recruited within 5 s (t = 35s, white circle) and tracks the shrinking plus end (t = 35-45 s). MOR1- 3xYPet remains at the growing microtubule’s plus end (yellow circle) throughout. Scale bar represents 5 μm. See Supplementary Movie S4. In the schematic diagram, a growing microtubule (blue) with MOR1 (red circle) crosses over an obstacle microtubule (blue) (t 1 -t 2 ). Following crossover (arrowhead), MOR1 tracks the existing, growing plus end as well as the newly generated, shrinking plus end (t 3 -t 4 ). + and – indicate the plus and minus ends, respectively. (I, J) Confocal imaging of MOR1-3xYPet (red) and mRFP-TUB6 (cyan) in (I) live and (J) fixed etiolated hypocotyl cells ( mor1-23 background). In live cells, MOR1-3xYPet is plus-end localized. In chemically fixed cells, MOR1-3xYPet is no longer plus-end localized and instead becomes cytoplasmic. Scale bars represent 20 μm. (K, L) Confocal imaging of MOR1-3xYPet (red) and EB1b-mCherry (cyan) in (K) live and (L) fixed cells (wild-type background). In live cells, MOR1-3xYPet is localized along the microtubule lattice, and EB1b-mCherry is plus-end localized; in chemically fixed cells, MOR1-3xYPet no longer appears on microtubule plus ends but still labelled lattice, and EB1b-mCherry is not localized to microtubules and instead becomes cytoplasmic. Scale bars represent 20 μm. (M, N) MOR1 is detected in low abundance along the microtubule lattice by altering imaging settings on the TIRF microscope. Live-cell images are taken from the etiolated hypocotyls of MOR1-3xYPet/mor1-23 seedlings. (M) Comparison of images obtained with a 200 ms and 4000 ms exposure time. White brackets indicate the average distance that a single MOR1-3xYPet puncta will travel over a 4000 ms time period. Scale bars represent 5 μm. (N) Comparison of images obtained by increasing the laser intensity from 13% to 70% while maintaining the same exposure time. Scale bars represent 5 μm.

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: Fluorescence, Selection, Generated, Imaging, Microscopy, Comparison

    MOR1 localizes to microtubules in various cell types and throughout the cell cycle in Arabidopsis seedlings. (A-H) MOR1-3xYPet is expressed throughout Arabidopsis seedlings. Scale bars represent 20 μm. (A) Root tip cells. The image consists of two stitched images and a merged stack of z-slices taken every 0.5 μm. (B) Root elongation zone. Image is a merged stack of z-slices taken every 0.5 μm. (C) A cross-section of the root elongation zone showing trichoblasts (t), atrichoblasts (a), cortex (c), and endodermal (e) cells. (D) Elongating root hairs. The image is a cortical slice of the root hair. The image is a merged stack of z-slices taken every 0.2 μm. (E) Mature root hairs. The image is a cortical slice of the root hair. The image is a merged stack of z-slices taken every 0.2 μm. (F) Petiole epidermal cells. The image is a merged stack of z-slices taken every 0.5 μm. (G) Etiolated epidermal hypocotyl cells. The image is a merged stack of z-slices taken every 0.5 μm. (H) Pavement cells (PC) and guard cells (GC) of cotyledons. The image is a merged stack of z- slices taken every 0.5 μm. (I-L) MOR1 is associated with microtubules throughout the cell cycle. (I) During pre-prophase, MOR1-3xYPet localizes to microtubules at the preprophase band (PPB, arrows) and around the nuclear envelope as seen in medial sections of a lateral root cap cell. Scale bar represents 10 μm. (J) MOR1-3xYPet localizes to microtubules from pre-prophase to late anaphase in dividing root tip cells. Each image shows two cells at different stages of mitosis: the top cell progressed from pre-prophase (PP) to anaphase (An), while the bottom cell progressed from metaphase (M) to late anaphase (LAn). MOR1-3xYPet localizes to microtubules at the PPB (arrows) and around the nuclear envelope during pre-prophase, and re-localizes to spindle microtubules. Scale bar represents 10 μm. See Supplementary Movie S5. (K) During telophase, MOR1-3xYPet localizes to the phragmoplast at microtubule plus ends and in microtubule-free domains as seen in root tip cells. Images show two cells at early and late stages of telophase. The middle of the phragmoplast is the newly formed cell plate that excludes microtubules, indicated by a decrease in mRFP-TUB6 signal. The increase in MOR1-3xYPet fluorescence intensity at the middle of the phragmoplast suggests an accumulation of MOR1-3xYPet at microtubule plus ends. (L) Fluorescence intensity of line scans of phragmoplasts at early and late telophase shown in (K) .

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: MOR1 localizes to microtubules in various cell types and throughout the cell cycle in Arabidopsis seedlings. (A-H) MOR1-3xYPet is expressed throughout Arabidopsis seedlings. Scale bars represent 20 μm. (A) Root tip cells. The image consists of two stitched images and a merged stack of z-slices taken every 0.5 μm. (B) Root elongation zone. Image is a merged stack of z-slices taken every 0.5 μm. (C) A cross-section of the root elongation zone showing trichoblasts (t), atrichoblasts (a), cortex (c), and endodermal (e) cells. (D) Elongating root hairs. The image is a cortical slice of the root hair. The image is a merged stack of z-slices taken every 0.2 μm. (E) Mature root hairs. The image is a cortical slice of the root hair. The image is a merged stack of z-slices taken every 0.2 μm. (F) Petiole epidermal cells. The image is a merged stack of z-slices taken every 0.5 μm. (G) Etiolated epidermal hypocotyl cells. The image is a merged stack of z-slices taken every 0.5 μm. (H) Pavement cells (PC) and guard cells (GC) of cotyledons. The image is a merged stack of z- slices taken every 0.5 μm. (I-L) MOR1 is associated with microtubules throughout the cell cycle. (I) During pre-prophase, MOR1-3xYPet localizes to microtubules at the preprophase band (PPB, arrows) and around the nuclear envelope as seen in medial sections of a lateral root cap cell. Scale bar represents 10 μm. (J) MOR1-3xYPet localizes to microtubules from pre-prophase to late anaphase in dividing root tip cells. Each image shows two cells at different stages of mitosis: the top cell progressed from pre-prophase (PP) to anaphase (An), while the bottom cell progressed from metaphase (M) to late anaphase (LAn). MOR1-3xYPet localizes to microtubules at the PPB (arrows) and around the nuclear envelope during pre-prophase, and re-localizes to spindle microtubules. Scale bar represents 10 μm. See Supplementary Movie S5. (K) During telophase, MOR1-3xYPet localizes to the phragmoplast at microtubule plus ends and in microtubule-free domains as seen in root tip cells. Images show two cells at early and late stages of telophase. The middle of the phragmoplast is the newly formed cell plate that excludes microtubules, indicated by a decrease in mRFP-TUB6 signal. The increase in MOR1-3xYPet fluorescence intensity at the middle of the phragmoplast suggests an accumulation of MOR1-3xYPet at microtubule plus ends. (L) Fluorescence intensity of line scans of phragmoplasts at early and late telophase shown in (K) .

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: Fluorescence

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet:

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques:

    MOR1 displays a stronger association to the microtubule plus end than the lattice. Seedlings Fluorescence recovery after photobleaching (FRAP) experiments were used to measure MOR1 dynamics within a circular region of interest (ROI, yellow circle) in etiolated hypocotyl cells of the following seedlings: (A) MOR1-3xYPet expressed in the mor1-23 background, (B) MOR1-3xYPet expressed in the wild-type Col-0 background, and (C) GFP- CLASP expressed in the clasp-1 background as a control for lattice-bound proteins. Scale bars represent 5 µm. (D) After subtracting the background signal (F background ), the ratio of fluorescence intensity within the ROI (F ROI ) to another unbleached region in the same cell (F reference ) is used to calculate the mobile fraction (F m ) and the off-rate (k off ) of fluorescent-tagged proteins from microtubules.

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: MOR1 displays a stronger association to the microtubule plus end than the lattice. Seedlings Fluorescence recovery after photobleaching (FRAP) experiments were used to measure MOR1 dynamics within a circular region of interest (ROI, yellow circle) in etiolated hypocotyl cells of the following seedlings: (A) MOR1-3xYPet expressed in the mor1-23 background, (B) MOR1-3xYPet expressed in the wild-type Col-0 background, and (C) GFP- CLASP expressed in the clasp-1 background as a control for lattice-bound proteins. Scale bars represent 5 µm. (D) After subtracting the background signal (F background ), the ratio of fluorescence intensity within the ROI (F ROI ) to another unbleached region in the same cell (F reference ) is used to calculate the mobile fraction (F m ) and the off-rate (k off ) of fluorescent-tagged proteins from microtubules.

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: Fluorescence, Control

    The mor1-1 L174F substitution reduces the rate of microtubule polymerization, alters TOG1 hydrogen bonding and flexibility, and reduces MOR1 turnover on the microtubule plus end. (A) Time projections of hypocotyl cells expressing MOR1-3xYPet and mor1-1-YPet at 21°C and 30 C, collected over 44 seconds. Scale bars represent 5 μm. (B) Boxplots showing MOR1-3xYPet and mor1-1-YPet velocities at 21°C and 30°C. Horizontal lines mark the median, boxes mark the range from the 25th to 75th percentile, and the whiskers show the highest and lowest data points within 1.5 times the interquartile range. Letters represent statistical differences between genotypes assessed by Kruskal-Wallis and Dunn’s test. n = 85 for MOR1-3xYPet 21°C, n = 113 for MOR1-3xYPet 30°C, n = 60 for mor1-1-YPet 21°C, n = 79 for mor1-1-YPet 30°C. (C) Structure of MOR1 TOG1 with six HEAT repeats coloured cyan or grey. The red colour marks the position of the L174 residue. (D) The mor1-1 L174F (in red) substitution alters hydrogen bonds within the alpha helix backbone in the fifth HEAT repeat of TOG1. Hydrogen bond lengths (in angstrom Å) are average values from five AlphaFold models. A nearby aromatic residue F178 is also shown. (E) An AlphaFold model of MOR1 TOG1 interacting with the Arabidopsis α/β-tubulin dimer TUA4 and TUB4. HEAT repeats 1-6 are coloured cyan or grey. (F) The mor1-1 L174F substitution (in red) alters the number of hydrogen bonds between MOR1 TOG1 and each tubulin monomer, calculated with a 0.4 Å tolerance. (G) Root mean square fluctuation (RMSF, in angstrom Å) of the TOG1 domain of MOR1 and mor1-1, modelled at 21°C and 30°C. Horizontal dashed lines represent mean RMSF values across residues 1-227. (H) FRAP data of MOR1-3xYPet and mor1-1-YPet at 21°C and 30°C.

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: The mor1-1 L174F substitution reduces the rate of microtubule polymerization, alters TOG1 hydrogen bonding and flexibility, and reduces MOR1 turnover on the microtubule plus end. (A) Time projections of hypocotyl cells expressing MOR1-3xYPet and mor1-1-YPet at 21°C and 30 C, collected over 44 seconds. Scale bars represent 5 μm. (B) Boxplots showing MOR1-3xYPet and mor1-1-YPet velocities at 21°C and 30°C. Horizontal lines mark the median, boxes mark the range from the 25th to 75th percentile, and the whiskers show the highest and lowest data points within 1.5 times the interquartile range. Letters represent statistical differences between genotypes assessed by Kruskal-Wallis and Dunn’s test. n = 85 for MOR1-3xYPet 21°C, n = 113 for MOR1-3xYPet 30°C, n = 60 for mor1-1-YPet 21°C, n = 79 for mor1-1-YPet 30°C. (C) Structure of MOR1 TOG1 with six HEAT repeats coloured cyan or grey. The red colour marks the position of the L174 residue. (D) The mor1-1 L174F (in red) substitution alters hydrogen bonds within the alpha helix backbone in the fifth HEAT repeat of TOG1. Hydrogen bond lengths (in angstrom Å) are average values from five AlphaFold models. A nearby aromatic residue F178 is also shown. (E) An AlphaFold model of MOR1 TOG1 interacting with the Arabidopsis α/β-tubulin dimer TUA4 and TUB4. HEAT repeats 1-6 are coloured cyan or grey. (F) The mor1-1 L174F substitution (in red) alters the number of hydrogen bonds between MOR1 TOG1 and each tubulin monomer, calculated with a 0.4 Å tolerance. (G) Root mean square fluctuation (RMSF, in angstrom Å) of the TOG1 domain of MOR1 and mor1-1, modelled at 21°C and 30°C. Horizontal dashed lines represent mean RMSF values across residues 1-227. (H) FRAP data of MOR1-3xYPet and mor1-1-YPet at 21°C and 30°C.

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: Expressing, Residue

    MOR1 turnover at the plus end is tightly coupled to MOR1 velocity and microtubule growth. (A) CRISPR/Cas9 generated a single base pair insertion (in red) in exon 6 of the Arabidopsis CLASP gene, resulting in a frameshift and a premature stop codon (*). (B-G) Microtubule growth is correlated with MOR1 turnover under various experimental conditions. Time projection over 20 seconds taken in etiolated hypocotyl cells expressing: (B) MOR1-3xYPet measured at 21°C as the control, (C) MOR1-3xYPet under taxol treatment, and (D) MOR1-3xYPet in the CRISPR clasp background. Scale bars represent 5 µm. All seedlings were also in the mor1-23 mutant background. (E) FRAP data of MOR1-3xYPet from control and taxol-treated cells. (F) FRAP data of MOR1-3xYPet from control and CRISPR clasp cells. (G) MOR1 mobile fraction is positively correlated with MOR1 velocity. Pearson R 2 = 0.79, p = 0.018.

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: MOR1 turnover at the plus end is tightly coupled to MOR1 velocity and microtubule growth. (A) CRISPR/Cas9 generated a single base pair insertion (in red) in exon 6 of the Arabidopsis CLASP gene, resulting in a frameshift and a premature stop codon (*). (B-G) Microtubule growth is correlated with MOR1 turnover under various experimental conditions. Time projection over 20 seconds taken in etiolated hypocotyl cells expressing: (B) MOR1-3xYPet measured at 21°C as the control, (C) MOR1-3xYPet under taxol treatment, and (D) MOR1-3xYPet in the CRISPR clasp background. Scale bars represent 5 µm. All seedlings were also in the mor1-23 mutant background. (E) FRAP data of MOR1-3xYPet from control and taxol-treated cells. (F) FRAP data of MOR1-3xYPet from control and CRISPR clasp cells. (G) MOR1 mobile fraction is positively correlated with MOR1 velocity. Pearson R 2 = 0.79, p = 0.018.

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: CRISPR, Generated, Expressing, Control, Mutagenesis

    A sidewinder model of MOR1’s polymerase activity and finite processivity at the microtubule plus end. (A) MOR1 C-terminus binds the microtubule lattice. TOG domains recruit free tubulin dimers. (B) TOG domains add free tubulin dimers to the plus end and detach from the dimers. This process alters MOR1’s conformation such that MOR1 positions itself in the next protofilament. MOR1 continues to incorporate free tubulin into the next protofilament. If MOR1 fails to incorporate tubulin dimers (such as the case for lattice-bound MOR1), MOR1 will dissociate. If MOR1 has impaired polymerase function (such as the case for mor1-1), it will take longer to add dimers and move more slowly from one protofilament to the next. (C) MOR1 moves across all 13 protofilaments and encounters a microtubule seam where α/β-tubulin units do not line up perfectly. (D) MOR1 may cross the seam to continue polymerization or dissociate from the microtubule.

    Journal: bioRxiv

    Article Title: Microtubule plus-end dynamics are tightly coupled to the turnover of the MOR1 polymerase

    doi: 10.1101/2024.10.30.621176

    Figure Lengend Snippet: A sidewinder model of MOR1’s polymerase activity and finite processivity at the microtubule plus end. (A) MOR1 C-terminus binds the microtubule lattice. TOG domains recruit free tubulin dimers. (B) TOG domains add free tubulin dimers to the plus end and detach from the dimers. This process alters MOR1’s conformation such that MOR1 positions itself in the next protofilament. MOR1 continues to incorporate free tubulin into the next protofilament. If MOR1 fails to incorporate tubulin dimers (such as the case for lattice-bound MOR1), MOR1 will dissociate. If MOR1 has impaired polymerase function (such as the case for mor1-1), it will take longer to add dimers and move more slowly from one protofilament to the next. (C) MOR1 moves across all 13 protofilaments and encounters a microtubule seam where α/β-tubulin units do not line up perfectly. (D) MOR1 may cross the seam to continue polymerization or dissociate from the microtubule.

    Article Snippet: 2 mg synthetic MOR1 antigen peptide (Cys-βAla- TRKIRSEQDKEPEAE, Kinexus) was dissolved in 1 mL Coupling Buffer (50 mM Tris- HCl, 5 mM Na 2 EDTA, pH 8.5).

    Techniques: Activity Assay

    Figure 4. Decreased expression of Oprm1 mRNA and protein with icKO. (A) Quantitative analysis of Oprm1 mRNA expression in the medial prefrontal cortex (mPFC), CA1-CA2 areas and dentate gyrus (DG) of the hippocampus, caudate putamen (CPu), nucleus accumbens (NAc), and the ventral tegmental area (VTA). Two-way ANOVA revealed a significant effect of genotype [F (1, 24) = 519.3, p < 0.001]. A Bonferroni post hoc test showed that Oprm1 icKO mice expressed significantly less Oprm1 mRNA in all brain regions of interest. n = 3 mice per group; 2 sections per mouse; 15 regions of interest (ROI) per data point. ROI was defined by a 15 µm circle over a field that contained at least one green-turquoise (Fast Green; labeling Aldh1 mRNA) punctum within an astrocyte, as seen in B. (B) Co-localization of Oprm1 mRNA expression (red dots) surrounding randomly selected Aldh1l1 mRNA expression loci (green-turquoise dots). The radius of the black circle (ROI) is 15 µm (707 µm2). Pixels for red (Fast Red) Oprm1 mRNA staining were counted within the ROI. (C,D) Representative images of sections counterstained with 50% Gill’s hematoxylin 1 to disclose tissue morphology, i.e., the cell nuclei (purple). The black circle denotes the ROI shown in B. (E,F) Quantitative analysis of Western blots revealed significantly decreased expression of astrocytic MOR1 in Oprm1 icKO mice (Student’s t test; t = 23.22, p < 0.0001). n = 4 mice per group; Error bars indicate SEM. *** p < 0.001, **** p < 0.0001.

    Journal: Cells

    Article Title: Loss of Astrocytic µ Opioid Receptors Exacerbates Aversion Associated with Morphine Withdrawal in Mice: Role of Mitochondrial Respiration.

    doi: 10.3390/cells12101412

    Figure Lengend Snippet: Figure 4. Decreased expression of Oprm1 mRNA and protein with icKO. (A) Quantitative analysis of Oprm1 mRNA expression in the medial prefrontal cortex (mPFC), CA1-CA2 areas and dentate gyrus (DG) of the hippocampus, caudate putamen (CPu), nucleus accumbens (NAc), and the ventral tegmental area (VTA). Two-way ANOVA revealed a significant effect of genotype [F (1, 24) = 519.3, p < 0.001]. A Bonferroni post hoc test showed that Oprm1 icKO mice expressed significantly less Oprm1 mRNA in all brain regions of interest. n = 3 mice per group; 2 sections per mouse; 15 regions of interest (ROI) per data point. ROI was defined by a 15 µm circle over a field that contained at least one green-turquoise (Fast Green; labeling Aldh1 mRNA) punctum within an astrocyte, as seen in B. (B) Co-localization of Oprm1 mRNA expression (red dots) surrounding randomly selected Aldh1l1 mRNA expression loci (green-turquoise dots). The radius of the black circle (ROI) is 15 µm (707 µm2). Pixels for red (Fast Red) Oprm1 mRNA staining were counted within the ROI. (C,D) Representative images of sections counterstained with 50% Gill’s hematoxylin 1 to disclose tissue morphology, i.e., the cell nuclei (purple). The black circle denotes the ROI shown in B. (E,F) Quantitative analysis of Western blots revealed significantly decreased expression of astrocytic MOR1 in Oprm1 icKO mice (Student’s t test; t = 23.22, p < 0.0001). n = 4 mice per group; Error bars indicate SEM. *** p < 0.001, **** p < 0.0001.

    Article Snippet: The nitrocellulose membrane was incubated overnight at 4 ◦C with anti-MOR1 mouse monoclonal antibody (1:500, sc-515933, Santa Cruz Biotechnology, Dallas, TX, USA) and then with horseradish peroxidase-conjugated anti-mouse secondary antibody (1:1000, NA931, Cytiva, Marlborough, MA, USA).

    Techniques: Expressing, Labeling, Staining, Western Blot

    a (Left) Bright-field image of a horizontal section through the brain of a rat, illustrating two examples of Py-CFs maintained in the brain, overlaid with a reverse-contrast fluorescent image of the section just above that was stained for markers (color key in figure) of cell nuclei (DAPI), blood brain permeability marker (IgG), and striosomes (MOR1). The Py-CFs were unable to remain in the thinner 25 μm slices typically used for immunohistochemical staining, and therefore sections were made thicker (100 μm) in some sections (sectioning schedule shown in a, right). Enhanced IgG staining is apparent just around the Py-CFs, confirming that the devices were not displaced during brain cutting. Blood vessels were perforated at the surface of the brain during insertion of the CFET array in order to provide staining along the CFET insertion track and to validate that the location of the Py-CFs remained fixed in the tissue section. b Fluorescence image of a MOR1-immunostained 100 μm thick section with embedded Py-CFs (black lines).

    Journal: bioRxiv

    Article Title: Scalable, flexible carbon fiber electrode thread arrays for three-dimensional spatial profiling of neurochemical activity in deep brain structures of rodents

    doi: 10.1101/2023.04.15.537033

    Figure Lengend Snippet: a (Left) Bright-field image of a horizontal section through the brain of a rat, illustrating two examples of Py-CFs maintained in the brain, overlaid with a reverse-contrast fluorescent image of the section just above that was stained for markers (color key in figure) of cell nuclei (DAPI), blood brain permeability marker (IgG), and striosomes (MOR1). The Py-CFs were unable to remain in the thinner 25 μm slices typically used for immunohistochemical staining, and therefore sections were made thicker (100 μm) in some sections (sectioning schedule shown in a, right). Enhanced IgG staining is apparent just around the Py-CFs, confirming that the devices were not displaced during brain cutting. Blood vessels were perforated at the surface of the brain during insertion of the CFET array in order to provide staining along the CFET insertion track and to validate that the location of the Py-CFs remained fixed in the tissue section. b Fluorescence image of a MOR1-immunostained 100 μm thick section with embedded Py-CFs (black lines).

    Article Snippet: After removing the excess liquid from slides, rabbit anti-MOR1 (Abcam Ab134054, 1:500) antibody diluted in TSA block was applied on the slides and slides were left for one night at 4°C in a humidity-controlled chamber.

    Techniques: Staining, Permeability, Marker, Immunohistochemical staining, Fluorescence

    Panel A : Control (non-transfected)(C), stable vector control (VC) and MOR1 overexpressing (O/E) H358 cell lines were generated, cell lysates obtained and immunoblotted with EMT markers anti-vimentin (a), anti-Snail (b), anti-Slug (c), anti-claudin-1 (d), anti-ZO-1 (e), anti-MOR (f) and anti-actin (g) antibodies. An increase in vimentin, Snail and Slug expression and a decrease in claudin-1 and ZO-1 expression suggest an epithelial mesenchymal transition. Panel B : Graphical quantitation of immunoreactivity of experiments performed described in Panel A with n = 3 independent experiments per condition. An asterisk (*) indicates a statistically significant difference (p<0.05) from control with error bars = standard deviation. Panel C : H358 human NSCLC cells were either untreated, treated with 100 ng/ml epidermal growth factor (EGF), 100 nM DAMGO, morphine or fentanyl or 100 ng/ml insulin growth factor (IGF) for 96 hours, cell lysates obtained and immunoblotted with EMT markers anti-vimentin (a), anti-Snail (b), anti-Slug (c), anti-claudin-1 (d), anti-ZO-1 (e), anti-MOR (f) and anti-actin (g) antibodies. A decrease in vimentin, Snail and Slug expression and an increase in claudin-1 and ZO-1 expression suggest inhibition of epithelial mesenchymal transition. Panel D : Control shRNA or MOR shRNA H358 cell lines were generated, cell lysates obtained and immunoblotted with EMT markers anti-vimentin (a), anti-Snail (b), anti-Slug (c), anti-claudin-1 (d), anti-ZO-1 (e), anti-MOR (f) and anti-actin (g) antibodies. An increase in vimentin, Snail and Slug expression and a decrease in claudin-1 and ZO-1 expression suggest an epithelial mesenchymal transition.

    Journal: PLoS ONE

    Article Title: The Mu Opioid Receptor Promotes Opioid and Growth Factor-Induced Proliferation, Migration and Epithelial Mesenchymal Transition (EMT) in Human Lung Cancer

    doi: 10.1371/journal.pone.0091577

    Figure Lengend Snippet: Panel A : Control (non-transfected)(C), stable vector control (VC) and MOR1 overexpressing (O/E) H358 cell lines were generated, cell lysates obtained and immunoblotted with EMT markers anti-vimentin (a), anti-Snail (b), anti-Slug (c), anti-claudin-1 (d), anti-ZO-1 (e), anti-MOR (f) and anti-actin (g) antibodies. An increase in vimentin, Snail and Slug expression and a decrease in claudin-1 and ZO-1 expression suggest an epithelial mesenchymal transition. Panel B : Graphical quantitation of immunoreactivity of experiments performed described in Panel A with n = 3 independent experiments per condition. An asterisk (*) indicates a statistically significant difference (p<0.05) from control with error bars = standard deviation. Panel C : H358 human NSCLC cells were either untreated, treated with 100 ng/ml epidermal growth factor (EGF), 100 nM DAMGO, morphine or fentanyl or 100 ng/ml insulin growth factor (IGF) for 96 hours, cell lysates obtained and immunoblotted with EMT markers anti-vimentin (a), anti-Snail (b), anti-Slug (c), anti-claudin-1 (d), anti-ZO-1 (e), anti-MOR (f) and anti-actin (g) antibodies. A decrease in vimentin, Snail and Slug expression and an increase in claudin-1 and ZO-1 expression suggest inhibition of epithelial mesenchymal transition. Panel D : Control shRNA or MOR shRNA H358 cell lines were generated, cell lysates obtained and immunoblotted with EMT markers anti-vimentin (a), anti-Snail (b), anti-Slug (c), anti-claudin-1 (d), anti-ZO-1 (e), anti-MOR (f) and anti-actin (g) antibodies. An increase in vimentin, Snail and Slug expression and a decrease in claudin-1 and ZO-1 expression suggest an epithelial mesenchymal transition.

    Article Snippet: The MOR1-Myc fusion product was then transferred to pcDNA3.2/v5 DEST vector (Invitrogen, CA) by LR reaction.

    Techniques: Transfection, Plasmid Preparation, Generated, Expressing, Quantitation Assay, Standard Deviation, Inhibition, shRNA