bdnf  (Alomone Labs)


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    Structured Review

    Alomone Labs bdnf
    Cuprizone-lesioned mice exhibit an increase in <t>BDNF</t> and myelin protein levels 6 h after a single stereotaxic injection of ACPD. a , Western blots demonstrate BDNF, MBP, and MAG protein levels in the corpus callosum of wild-type mice subjected to a 4 week cuprizone lesion and injected with ACPD or 0.9% saline vehicle. GAPDH is shown as a loading control. b , Graphs represent a densitometric analysis of Western blots normalized to GAPDH and are presented as percentage saline-injected control. Levels of mature BDNF are indicated in this analysis. c , Immunohistochemical analysis of MBP, MAG and <t>PLP</t> reactivity in the corpus callosum reveals strong staining intensity in the intact corpus callosum that is decreased following exposure to cuprizone. This MBP, MAG, and PLP deficit is reversed in cuprizone-lesioned animals 6 h after the administration of ACPD. Western blot data analyzed by ANOVA; ***significantly different from saline-injected control at p
    Bdnf, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 95/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 95 stars, based on 31 article reviews
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    Images

    1) Product Images from "Astrocyte-Derived BDNF Supports Myelin Protein Synthesis after Cuprizone-Induced Demyelination"

    Article Title: Astrocyte-Derived BDNF Supports Myelin Protein Synthesis after Cuprizone-Induced Demyelination

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.4267-13.2014

    Cuprizone-lesioned mice exhibit an increase in BDNF and myelin protein levels 6 h after a single stereotaxic injection of ACPD. a , Western blots demonstrate BDNF, MBP, and MAG protein levels in the corpus callosum of wild-type mice subjected to a 4 week cuprizone lesion and injected with ACPD or 0.9% saline vehicle. GAPDH is shown as a loading control. b , Graphs represent a densitometric analysis of Western blots normalized to GAPDH and are presented as percentage saline-injected control. Levels of mature BDNF are indicated in this analysis. c , Immunohistochemical analysis of MBP, MAG and PLP reactivity in the corpus callosum reveals strong staining intensity in the intact corpus callosum that is decreased following exposure to cuprizone. This MBP, MAG, and PLP deficit is reversed in cuprizone-lesioned animals 6 h after the administration of ACPD. Western blot data analyzed by ANOVA; ***significantly different from saline-injected control at p
    Figure Legend Snippet: Cuprizone-lesioned mice exhibit an increase in BDNF and myelin protein levels 6 h after a single stereotaxic injection of ACPD. a , Western blots demonstrate BDNF, MBP, and MAG protein levels in the corpus callosum of wild-type mice subjected to a 4 week cuprizone lesion and injected with ACPD or 0.9% saline vehicle. GAPDH is shown as a loading control. b , Graphs represent a densitometric analysis of Western blots normalized to GAPDH and are presented as percentage saline-injected control. Levels of mature BDNF are indicated in this analysis. c , Immunohistochemical analysis of MBP, MAG and PLP reactivity in the corpus callosum reveals strong staining intensity in the intact corpus callosum that is decreased following exposure to cuprizone. This MBP, MAG, and PLP deficit is reversed in cuprizone-lesioned animals 6 h after the administration of ACPD. Western blot data analyzed by ANOVA; ***significantly different from saline-injected control at p

    Techniques Used: Mouse Assay, Injection, Western Blot, Immunohistochemistry, Plasmid Purification, Staining

    The ACPD effect on myelin protein expression is blocked when astrocyte-derived BDNF is reduced. Cre recombinase + GFAPcreERT2-floxBDNF-ROSA26 mice and Cre recombinase − floxBDNF-ROSA26 controls were injected with tamoxifen and fed cuprizone-laden food for 4 weeks before they received a single stereotaxic injection of either ACPD or saline vehicle. a , Western blots demonstrate MBP and MAG protein in the corpus callosum of these mice. GAPDH is shown as a loading control. b , Graph represents a densitometric analysis of Western blots normalized to GAPDH and are presented as percentage cre- saline-injected control. Western blot data analyzed by ANOVA; *significantly different from saline-injected, cre- controls at p
    Figure Legend Snippet: The ACPD effect on myelin protein expression is blocked when astrocyte-derived BDNF is reduced. Cre recombinase + GFAPcreERT2-floxBDNF-ROSA26 mice and Cre recombinase − floxBDNF-ROSA26 controls were injected with tamoxifen and fed cuprizone-laden food for 4 weeks before they received a single stereotaxic injection of either ACPD or saline vehicle. a , Western blots demonstrate MBP and MAG protein in the corpus callosum of these mice. GAPDH is shown as a loading control. b , Graph represents a densitometric analysis of Western blots normalized to GAPDH and are presented as percentage cre- saline-injected control. Western blot data analyzed by ANOVA; *significantly different from saline-injected, cre- controls at p

    Techniques Used: Expressing, Derivative Assay, Mouse Assay, Injection, Western Blot

    2) Product Images from "Heat-Stress Preconditioning Attenuates Behavioral Responses to Psychological Stress: The Role of HSP-70 in Modulating Stress Responses"

    Article Title: Heat-Stress Preconditioning Attenuates Behavioral Responses to Psychological Stress: The Role of HSP-70 in Modulating Stress Responses

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms23084129

    Cellular markers under basal thermoneutral naive and after heat stress. Immunoreactive-cell numbers and representative immunohistochemical images of HSP-70, GR, AVP, BDNF, NPY, COX-2 and Iba-1 positive cells within the CA1, CA3 and the DG of the hippocampus and the hypothalamic PVN ( a – e ). Results displayed as mean ± S.E.M.
    Figure Legend Snippet: Cellular markers under basal thermoneutral naive and after heat stress. Immunoreactive-cell numbers and representative immunohistochemical images of HSP-70, GR, AVP, BDNF, NPY, COX-2 and Iba-1 positive cells within the CA1, CA3 and the DG of the hippocampus and the hypothalamic PVN ( a – e ). Results displayed as mean ± S.E.M.

    Techniques Used: Immunohistochemistry

    3) Product Images from "Brain-derived neurotrophic factor increases expression of MnSOD in human circulating angiogenic cells"

    Article Title: Brain-derived neurotrophic factor increases expression of MnSOD in human circulating angiogenic cells

    Journal: Microvascular Research

    doi: 10.1016/j.mvr.2012.01.001

    BDNF increased MnSOD expression in EPCs. A and B: Human EPCs were treated with BDNF (50 or 100 ng/ml) in EBM2 for 24 h. Protein samples were subjected to Western blotting. Blots are representative of 3 independent experiments. B: Optical density analysis of MnSOD protein levels; n=3, *P
    Figure Legend Snippet: BDNF increased MnSOD expression in EPCs. A and B: Human EPCs were treated with BDNF (50 or 100 ng/ml) in EBM2 for 24 h. Protein samples were subjected to Western blotting. Blots are representative of 3 independent experiments. B: Optical density analysis of MnSOD protein levels; n=3, *P

    Techniques Used: Expressing, Western Blot

    Phenotyping of EPCs. Mononuclear cells were cultured on fibronectin-coated plates in EGM2 for 4 days. A: Phase contrast image of day 4 EPCs (× 20 magnification). B–E: FACS analysis of cell surface markers on EPCs. Shown are representative data from at least 3 independent experiments for each marker. The open black-lined histograms represent tested antibodies, and filled histograms represent the control IgG. F: Human EPCs expressed receptors that bind to BDNF, TrkB and p75 NTR . Positive controls (Post) for p75NTR and TrkB are SK-N-MC cell lysate and mouse brain, respectively. G: mRNA expressions of TrkB and p75 NTR in day 4 EPCs and circulating mononuclear cells (MNC).
    Figure Legend Snippet: Phenotyping of EPCs. Mononuclear cells were cultured on fibronectin-coated plates in EGM2 for 4 days. A: Phase contrast image of day 4 EPCs (× 20 magnification). B–E: FACS analysis of cell surface markers on EPCs. Shown are representative data from at least 3 independent experiments for each marker. The open black-lined histograms represent tested antibodies, and filled histograms represent the control IgG. F: Human EPCs expressed receptors that bind to BDNF, TrkB and p75 NTR . Positive controls (Post) for p75NTR and TrkB are SK-N-MC cell lysate and mouse brain, respectively. G: mRNA expressions of TrkB and p75 NTR in day 4 EPCs and circulating mononuclear cells (MNC).

    Techniques Used: Cell Culture, FACS, Marker

    BDNF induced phosphorylation of IKKα/β, and JNK. A–C: EPCs were cultured in EBM-2 for 20 h, then were treated with BDNF for indicated periods. All blots are representative of at least 3 independent experiments. A: n=6–9, P
    Figure Legend Snippet: BDNF induced phosphorylation of IKKα/β, and JNK. A–C: EPCs were cultured in EBM-2 for 20 h, then were treated with BDNF for indicated periods. All blots are representative of at least 3 independent experiments. A: n=6–9, P

    Techniques Used: Cell Culture

    BDNF protected EPCs from oxidative stress. A and B: EPCs were incubated with indicated treatments, then were subjected to TUNEL assay (A, n=5–8, *P
    Figure Legend Snippet: BDNF protected EPCs from oxidative stress. A and B: EPCs were incubated with indicated treatments, then were subjected to TUNEL assay (A, n=5–8, *P

    Techniques Used: Incubation, TUNEL Assay

    4) Product Images from "Positive Feedback Regulation between ?-Aminobutyric Acid Type A (GABAA) Receptor Signaling and Brain-derived Neurotrophic Factor (BDNF) Release in Developing Neurons *"

    Article Title: Positive Feedback Regulation between ?-Aminobutyric Acid Type A (GABAA) Receptor Signaling and Brain-derived Neurotrophic Factor (BDNF) Release in Developing Neurons *

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.201582

    GABA A R activation induces BDNF/TrkB-dependent phosphorylation of CREB. A , immunofluorescence of CREB ( left panels ; red ) and pCREB ( middle panels ; green ) in cortical neurons in control conditions ( Ctrl ) or treated with muscimol alone (50 μ m ; Musc
    Figure Legend Snippet: GABA A R activation induces BDNF/TrkB-dependent phosphorylation of CREB. A , immunofluorescence of CREB ( left panels ; red ) and pCREB ( middle panels ; green ) in cortical neurons in control conditions ( Ctrl ) or treated with muscimol alone (50 μ m ; Musc

    Techniques Used: Activation Assay, Immunofluorescence

    GABA A R-dependent release of endogenous BDNF mediates increase in cell surface expression. A , cultured cerebrocortical neurons (6 DIV) in control conditions ( Ctrl ) or treated with muscimol in the absence ( Musc ) or presence of TrkB-IgG ( Musc + TrkB-IgG
    Figure Legend Snippet: GABA A R-dependent release of endogenous BDNF mediates increase in cell surface expression. A , cultured cerebrocortical neurons (6 DIV) in control conditions ( Ctrl ) or treated with muscimol in the absence ( Musc ) or presence of TrkB-IgG ( Musc + TrkB-IgG

    Techniques Used: Expressing, Cell Culture

    5) Product Images from "Effects of Exercise Training during Advanced Maternal Age on the Cognitive Function of Offspring"

    Article Title: Effects of Exercise Training during Advanced Maternal Age on the Cognitive Function of Offspring

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms23105517

    Effects of exercise on BDNF and PSD95 in the hippocampus of the offspring from mothers with advanced maternal age (AMA). CON: offspring from the control group; CON + EX: offspring from the control and exercised group; AMA: offspring from the advanced maternal age group; AMA + EX: offspring from the advanced maternal age and exercised group. Data are expressed as means ± standard error of the mean (SEM). * p
    Figure Legend Snippet: Effects of exercise on BDNF and PSD95 in the hippocampus of the offspring from mothers with advanced maternal age (AMA). CON: offspring from the control group; CON + EX: offspring from the control and exercised group; AMA: offspring from the advanced maternal age group; AMA + EX: offspring from the advanced maternal age and exercised group. Data are expressed as means ± standard error of the mean (SEM). * p

    Techniques Used:

    6) Product Images from "Astrocytes from cortex and striatum show differential responses to mitochondrial toxin and BDNF: implications for protection of striatal neurons expressing mutant huntingtin"

    Article Title: Astrocytes from cortex and striatum show differential responses to mitochondrial toxin and BDNF: implications for protection of striatal neurons expressing mutant huntingtin

    Journal: Journal of Neuroinflammation

    doi: 10.1186/s12974-020-01965-4

    BDNF modifies astrocyte cytokine release. Cortical and striatal astrocytes were treated for 24 h with 3NP 15 mM with or without BDNF 50 ng/ml ( a ) or with LPS 1 μg/ml with or without BDNF 50 ng/ml ( b ). TNF-α release into the culture supernatant was assessed by ELISA and normalized to viability values obtained with the MTT assay for each experimental group. Data are the mean ± SEM of n = 3 independent experiments. Differences between two groups were analyzed by Student’s t test. ^ p
    Figure Legend Snippet: BDNF modifies astrocyte cytokine release. Cortical and striatal astrocytes were treated for 24 h with 3NP 15 mM with or without BDNF 50 ng/ml ( a ) or with LPS 1 μg/ml with or without BDNF 50 ng/ml ( b ). TNF-α release into the culture supernatant was assessed by ELISA and normalized to viability values obtained with the MTT assay for each experimental group. Data are the mean ± SEM of n = 3 independent experiments. Differences between two groups were analyzed by Student’s t test. ^ p

    Techniques Used: Enzyme-linked Immunosorbent Assay, MTT Assay

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    alomone labs bdnf quantification plasma bdnf
    NTSR2 phosphorylation in B-CLL and recruitment of G i α proteins. ( a ) Representative western blot analysis of Src phosphorylation in MEC-1 cells overexpressing NTSR2 (pCMV6-NTSR2) in the presence or absence of <t>BDNF</t> (100 ng/ml), pertussis toxin (PTX, 200 ng/ml) or K252a (100 nM) for 24 h. ( b ) Ratio of phosphorylated Src vs pan-Src protein, normalized against actin. Values are means±s.e.m. of three independent experiments in a.u. ( c , d ). After immunoprecipitation (IP) of NTSR2 from MEC-1 cells overexpressing NTSR2 (pCMV6-NTSR2) or not (EV), or from B-CLL cells in the presence or absence of BDNF (100 ng/ml) or <t>NTS</t> (40 μ M /ml), the immunocomplexes were immunoblotted (IB) with anti-G i α1/2 antibodies. ( e , f ) After immunoprecipitation (IP) of anti-pan-phosphoprotein was performed on MEC-1 cells overexpressing NTSR2 and B-CLL cells in the presence or absence of BDNF (100 ng/ml) or SR142948A (67 μ M ), the phosphorylation of NTSR2 was detected by immunoblotting (IB) with anti-NTSR2 antibodies. ( g ) Apoptotic ratio, assessed by cell death ELISA, in B-CLL in the presence or absence of SR142948A (67 μ M ) for 24 h. Values are mean ratios of apoptotic cells (±s.e.m.) of three independent experiments from different patients ( n =3). Significant P -values are indicated in the graphs * P
    Bdnf Quantification Plasma Bdnf, supplied by alomone labs, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Alomone Labs bdnf prodomain
    <t>BDNF</t> <t>prodomain</t> in low concentration (1 nM) pre-synaptically increases ACh quantal size and simultaneously induces oppositely directed presynaptic effects affecting the evoked ACh release at newly formed NMJs of reinnervated mouse m. EDL. (A) Representative recordings of MEPPs (left above) and mean MEPP amplitude and cumulative probability plots (right above), frequency and time-course parameters (left to right below) in control ( n = 20) and upon application of BDNF prodomain ( n = 22). (B) Mean MEPP amplitude in control ( n = 16) and during inhibition of vesicular ACh transporter by vesamicol (1 μM, n = 17) (left) and mean MEPP amplitude and cumulative probability plots in control ( n = 15) and upon application of BDNF prodomain in the presence of vesamicol ( n = 16). (C) Changes in the EPP amplitude (left) and their quantal content (right) in control ( n = 31) and in the presence of BDNF prodomain ( n = 41). Inset shows MEPP amplitudes.
    Bdnf Prodomain, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Alomone Labs pro bdnf
    <t>α-BDNF,</t> α-Myc, and α–pro-BDNF antibodies all generate similar staining patterns. (A) A schematic representation of the BDNF precursor pro-BDNF and the two cleavage products pro-peptide and BDNF. (B) Low-power view of a WT hippocampal section stained with anti-BDNF antibodies. Note the intense staining in the hilus of the DG and in SL of CA3, each of which contains the axon terminals of mossy fibers. (C and D) Higher magnification view of the DG (C) and CA3 region (D) of the cbdnf ko hippocampus stained with anti-BDNF. Note the absence of immunoreactive signals in all cellular and neuropil layers. GCL, granule cell layer; H, hilus; IML, inner molecular layer; PCL, pyramidal cell layer. (E) Bdnf-Myc hippocampi stained with Myc antibodies show a similar staining pattern to that produced by BDNF antibodies. (F and G) Note the absence of staining in the corresponding DG (F) and CA3 regions (G) of WT sections treated with Myc antibodies. (H) <t>Polyclonal</t> pro-BDNF antibodies yield a similar pattern to that of anti-BDNF. (I and J) The same antibodies do not produce an immunoreactive signal in hippocampal sections from cbdnf ko animals. (B, E, and H) Arrows denote the end bulb of the mossy fiber projection, which delineates CA3 and CA1. Note the relative lack of staining in CA1 in WT and Bdnf-Myc sections. Bars: (B, E, and H) 500 µm; (C, F, and I) 100 µm; (D, G, and J) 50 µm.
    Pro Bdnf, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    NTSR2 phosphorylation in B-CLL and recruitment of G i α proteins. ( a ) Representative western blot analysis of Src phosphorylation in MEC-1 cells overexpressing NTSR2 (pCMV6-NTSR2) in the presence or absence of BDNF (100 ng/ml), pertussis toxin (PTX, 200 ng/ml) or K252a (100 nM) for 24 h. ( b ) Ratio of phosphorylated Src vs pan-Src protein, normalized against actin. Values are means±s.e.m. of three independent experiments in a.u. ( c , d ). After immunoprecipitation (IP) of NTSR2 from MEC-1 cells overexpressing NTSR2 (pCMV6-NTSR2) or not (EV), or from B-CLL cells in the presence or absence of BDNF (100 ng/ml) or NTS (40 μ M /ml), the immunocomplexes were immunoblotted (IB) with anti-G i α1/2 antibodies. ( e , f ) After immunoprecipitation (IP) of anti-pan-phosphoprotein was performed on MEC-1 cells overexpressing NTSR2 and B-CLL cells in the presence or absence of BDNF (100 ng/ml) or SR142948A (67 μ M ), the phosphorylation of NTSR2 was detected by immunoblotting (IB) with anti-NTSR2 antibodies. ( g ) Apoptotic ratio, assessed by cell death ELISA, in B-CLL in the presence or absence of SR142948A (67 μ M ) for 24 h. Values are mean ratios of apoptotic cells (±s.e.m.) of three independent experiments from different patients ( n =3). Significant P -values are indicated in the graphs * P

    Journal: Oncogene

    Article Title: Neurotensin receptor type 2 protects B-cell chronic lymphocytic leukemia cells from apoptosis

    doi: 10.1038/onc.2017.365

    Figure Lengend Snippet: NTSR2 phosphorylation in B-CLL and recruitment of G i α proteins. ( a ) Representative western blot analysis of Src phosphorylation in MEC-1 cells overexpressing NTSR2 (pCMV6-NTSR2) in the presence or absence of BDNF (100 ng/ml), pertussis toxin (PTX, 200 ng/ml) or K252a (100 nM) for 24 h. ( b ) Ratio of phosphorylated Src vs pan-Src protein, normalized against actin. Values are means±s.e.m. of three independent experiments in a.u. ( c , d ). After immunoprecipitation (IP) of NTSR2 from MEC-1 cells overexpressing NTSR2 (pCMV6-NTSR2) or not (EV), or from B-CLL cells in the presence or absence of BDNF (100 ng/ml) or NTS (40 μ M /ml), the immunocomplexes were immunoblotted (IB) with anti-G i α1/2 antibodies. ( e , f ) After immunoprecipitation (IP) of anti-pan-phosphoprotein was performed on MEC-1 cells overexpressing NTSR2 and B-CLL cells in the presence or absence of BDNF (100 ng/ml) or SR142948A (67 μ M ), the phosphorylation of NTSR2 was detected by immunoblotting (IB) with anti-NTSR2 antibodies. ( g ) Apoptotic ratio, assessed by cell death ELISA, in B-CLL in the presence or absence of SR142948A (67 μ M ) for 24 h. Values are mean ratios of apoptotic cells (±s.e.m.) of three independent experiments from different patients ( n =3). Significant P -values are indicated in the graphs * P

    Article Snippet: Plasma NTS and BDNF quantification Plasma BDNF and NTS levels were measured using commercial ELISA kits: BDNF Emax ELISA ImmunoAssay System (Promega, WI, USA) and Human Neurotensin, NT ELISA Kit (CUSABIO Life Science, College Park, MD, USA).

    Techniques: Western Blot, Immunoprecipitation, Enzyme-linked Immunosorbent Assay

    BDNF prodomain in low concentration (1 nM) pre-synaptically increases ACh quantal size and simultaneously induces oppositely directed presynaptic effects affecting the evoked ACh release at newly formed NMJs of reinnervated mouse m. EDL. (A) Representative recordings of MEPPs (left above) and mean MEPP amplitude and cumulative probability plots (right above), frequency and time-course parameters (left to right below) in control ( n = 20) and upon application of BDNF prodomain ( n = 22). (B) Mean MEPP amplitude in control ( n = 16) and during inhibition of vesicular ACh transporter by vesamicol (1 μM, n = 17) (left) and mean MEPP amplitude and cumulative probability plots in control ( n = 15) and upon application of BDNF prodomain in the presence of vesamicol ( n = 16). (C) Changes in the EPP amplitude (left) and their quantal content (right) in control ( n = 31) and in the presence of BDNF prodomain ( n = 41). Inset shows MEPP amplitudes.

    Journal: Frontiers in Cellular Neuroscience

    Article Title: ProBDNF and Brain-Derived Neurotrophic Factor Prodomain Differently Modulate Acetylcholine Release in Regenerating and Mature Mouse Motor Synapses

    doi: 10.3389/fncel.2022.866802

    Figure Lengend Snippet: BDNF prodomain in low concentration (1 nM) pre-synaptically increases ACh quantal size and simultaneously induces oppositely directed presynaptic effects affecting the evoked ACh release at newly formed NMJs of reinnervated mouse m. EDL. (A) Representative recordings of MEPPs (left above) and mean MEPP amplitude and cumulative probability plots (right above), frequency and time-course parameters (left to right below) in control ( n = 20) and upon application of BDNF prodomain ( n = 22). (B) Mean MEPP amplitude in control ( n = 16) and during inhibition of vesicular ACh transporter by vesamicol (1 μM, n = 17) (left) and mean MEPP amplitude and cumulative probability plots in control ( n = 15) and upon application of BDNF prodomain in the presence of vesamicol ( n = 16). (C) Changes in the EPP amplitude (left) and their quantal content (right) in control ( n = 31) and in the presence of BDNF prodomain ( n = 41). Inset shows MEPP amplitudes.

    Article Snippet: Next, it was necessary to reveal which targets and signaling pathways mediate the negative effect of the BDNF prodomain on synaptic transmission in mature NMJs.

    Techniques: Concentration Assay, Inhibition

    BK channels do not but GIRK channels mediate BDNF prodomain-induced inhibition of evoked ACh release at mature NMJs. (A) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 15) and upon BDNF prodomain (1 nM) in the presence of BK-blocker iberiotoxin (ITx, 100 nM) with L-type Ca 2+ -channel blocker nitrendipine (Nitr., 1 μM) ( n = 21). (B) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 15) and in the presence of GIRK blocker tertiapin-Q (100 nM, n = 17). (C) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 16) and upon BDNF prodomain (1 nM) in the presence of tertiapin-Q ( n = 19). Insets show MEPP amplitudes.

    Journal: Frontiers in Cellular Neuroscience

    Article Title: ProBDNF and Brain-Derived Neurotrophic Factor Prodomain Differently Modulate Acetylcholine Release in Regenerating and Mature Mouse Motor Synapses

    doi: 10.3389/fncel.2022.866802

    Figure Lengend Snippet: BK channels do not but GIRK channels mediate BDNF prodomain-induced inhibition of evoked ACh release at mature NMJs. (A) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 15) and upon BDNF prodomain (1 nM) in the presence of BK-blocker iberiotoxin (ITx, 100 nM) with L-type Ca 2+ -channel blocker nitrendipine (Nitr., 1 μM) ( n = 21). (B) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 15) and in the presence of GIRK blocker tertiapin-Q (100 nM, n = 17). (C) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 16) and upon BDNF prodomain (1 nM) in the presence of tertiapin-Q ( n = 19). Insets show MEPP amplitudes.

    Article Snippet: Next, it was necessary to reveal which targets and signaling pathways mediate the negative effect of the BDNF prodomain on synaptic transmission in mature NMJs.

    Techniques: Inhibition

    BDNF prodomain (1 nM) but not proBDNF (1 nM), induces strong inhibition of spontaneous end evoked ACh release at mature NMJs. (A) Mean MEPP amplitude, cumulative probability plots, frequency, and time-course parameters (left to right) in control ( n = 19) and upon application of proBDNF ( n = 26). (B) Representative recordings of MEPPs (top left) and mean MEPP amplitude, cumulative probability plots, frequency, (top right) and their time-course parameters (bottom) in control ( n = 23) and upon application of BDNF prodomain ( n = 33). (C) Representative recordings of EPPs during a short (1 s) high-frequency (50 Hz) train in control (above) and upon application of BDNF prodomain (below). (D) Changes in the EPP amplitude (above) and in the quantal content of EPPs (below) in control ( n = 22) and in the presence of proBDNF ( n = 21). Inset shows MEPP amplitudes.

    Journal: Frontiers in Cellular Neuroscience

    Article Title: ProBDNF and Brain-Derived Neurotrophic Factor Prodomain Differently Modulate Acetylcholine Release in Regenerating and Mature Mouse Motor Synapses

    doi: 10.3389/fncel.2022.866802

    Figure Lengend Snippet: BDNF prodomain (1 nM) but not proBDNF (1 nM), induces strong inhibition of spontaneous end evoked ACh release at mature NMJs. (A) Mean MEPP amplitude, cumulative probability plots, frequency, and time-course parameters (left to right) in control ( n = 19) and upon application of proBDNF ( n = 26). (B) Representative recordings of MEPPs (top left) and mean MEPP amplitude, cumulative probability plots, frequency, (top right) and their time-course parameters (bottom) in control ( n = 23) and upon application of BDNF prodomain ( n = 33). (C) Representative recordings of EPPs during a short (1 s) high-frequency (50 Hz) train in control (above) and upon application of BDNF prodomain (below). (D) Changes in the EPP amplitude (above) and in the quantal content of EPPs (below) in control ( n = 22) and in the presence of proBDNF ( n = 21). Inset shows MEPP amplitudes.

    Article Snippet: Next, it was necessary to reveal which targets and signaling pathways mediate the negative effect of the BDNF prodomain on synaptic transmission in mature NMJs.

    Techniques: Inhibition

    p75 receptors and Rho-signaling pathway underlie BDNF prodomain-triggered inhibition of evoked ACh release at mature NMJs. Moreover, the inhibitory effect of the BDNF prodomain (1 nM) on the evoked neuromuscular transmission depends on the endogenous activity of synaptic purinoreceptors at mature NMJs. (A) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 20) and upon BDNF prodomain (1 nM) in the presence of Rho-GDI-associated p75 signaling inhibitor TAT-Pep5 (1 μM, n = 21). (B) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 17) and in the presence of ROCK inhibitor Y-27632 (3 μM, n = 21). (C) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 15) and upon BDNF prodomain (1 nM) in the presence of Y-27632 ( n = 21). (D) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right), registered from NMJs of Panx1 –/– mice in control ( n = 24) and in the presence of BDNF prodomain ( n = 22). Insets show MEPP amplitudes.

    Journal: Frontiers in Cellular Neuroscience

    Article Title: ProBDNF and Brain-Derived Neurotrophic Factor Prodomain Differently Modulate Acetylcholine Release in Regenerating and Mature Mouse Motor Synapses

    doi: 10.3389/fncel.2022.866802

    Figure Lengend Snippet: p75 receptors and Rho-signaling pathway underlie BDNF prodomain-triggered inhibition of evoked ACh release at mature NMJs. Moreover, the inhibitory effect of the BDNF prodomain (1 nM) on the evoked neuromuscular transmission depends on the endogenous activity of synaptic purinoreceptors at mature NMJs. (A) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 20) and upon BDNF prodomain (1 nM) in the presence of Rho-GDI-associated p75 signaling inhibitor TAT-Pep5 (1 μM, n = 21). (B) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 17) and in the presence of ROCK inhibitor Y-27632 (3 μM, n = 21). (C) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right) in control ( n = 15) and upon BDNF prodomain (1 nM) in the presence of Y-27632 ( n = 21). (D) Changes in the EPP amplitude (left) and in the quantal content of EPPs (right), registered from NMJs of Panx1 –/– mice in control ( n = 24) and in the presence of BDNF prodomain ( n = 22). Insets show MEPP amplitudes.

    Article Snippet: Next, it was necessary to reveal which targets and signaling pathways mediate the negative effect of the BDNF prodomain on synaptic transmission in mature NMJs.

    Techniques: Inhibition, Transmission Assay, Activity Assay, Mouse Assay

    α-BDNF, α-Myc, and α–pro-BDNF antibodies all generate similar staining patterns. (A) A schematic representation of the BDNF precursor pro-BDNF and the two cleavage products pro-peptide and BDNF. (B) Low-power view of a WT hippocampal section stained with anti-BDNF antibodies. Note the intense staining in the hilus of the DG and in SL of CA3, each of which contains the axon terminals of mossy fibers. (C and D) Higher magnification view of the DG (C) and CA3 region (D) of the cbdnf ko hippocampus stained with anti-BDNF. Note the absence of immunoreactive signals in all cellular and neuropil layers. GCL, granule cell layer; H, hilus; IML, inner molecular layer; PCL, pyramidal cell layer. (E) Bdnf-Myc hippocampi stained with Myc antibodies show a similar staining pattern to that produced by BDNF antibodies. (F and G) Note the absence of staining in the corresponding DG (F) and CA3 regions (G) of WT sections treated with Myc antibodies. (H) Polyclonal pro-BDNF antibodies yield a similar pattern to that of anti-BDNF. (I and J) The same antibodies do not produce an immunoreactive signal in hippocampal sections from cbdnf ko animals. (B, E, and H) Arrows denote the end bulb of the mossy fiber projection, which delineates CA3 and CA1. Note the relative lack of staining in CA1 in WT and Bdnf-Myc sections. Bars: (B, E, and H) 500 µm; (C, F, and I) 100 µm; (D, G, and J) 50 µm.

    Journal: The Journal of Cell Biology

    Article Title: BDNF and its pro-peptide are stored in presynaptic dense core vesicles in brain neurons

    doi: 10.1083/jcb.201201038

    Figure Lengend Snippet: α-BDNF, α-Myc, and α–pro-BDNF antibodies all generate similar staining patterns. (A) A schematic representation of the BDNF precursor pro-BDNF and the two cleavage products pro-peptide and BDNF. (B) Low-power view of a WT hippocampal section stained with anti-BDNF antibodies. Note the intense staining in the hilus of the DG and in SL of CA3, each of which contains the axon terminals of mossy fibers. (C and D) Higher magnification view of the DG (C) and CA3 region (D) of the cbdnf ko hippocampus stained with anti-BDNF. Note the absence of immunoreactive signals in all cellular and neuropil layers. GCL, granule cell layer; H, hilus; IML, inner molecular layer; PCL, pyramidal cell layer. (E) Bdnf-Myc hippocampi stained with Myc antibodies show a similar staining pattern to that produced by BDNF antibodies. (F and G) Note the absence of staining in the corresponding DG (F) and CA3 regions (G) of WT sections treated with Myc antibodies. (H) Polyclonal pro-BDNF antibodies yield a similar pattern to that of anti-BDNF. (I and J) The same antibodies do not produce an immunoreactive signal in hippocampal sections from cbdnf ko animals. (B, E, and H) Arrows denote the end bulb of the mossy fiber projection, which delineates CA3 and CA1. Note the relative lack of staining in CA1 in WT and Bdnf-Myc sections. Bars: (B, E, and H) 500 µm; (C, F, and I) 100 µm; (D, G, and J) 50 µm.

    Article Snippet: Pro-BDNF was detected with a rabbit polyclonal antibody (anti–pro-BDNF; #ANT-006, batch AN-03; Alomone Labs) raised against the prodomain of BDNF protein (see ).

    Techniques: Staining, Produced