BDNF - Second Best?
Alon Meir, Ph.D.
Brain Derived Neurotrophic Factor (BDNF) is the second best characterized neurotrophin
(following NGF) and acts as a key contributor to neuronal development as well as neuronal
plasticity. BDNF is a homo-dimer protein which is secreted to affect cells that express
the BDNF receptors- TrkB and p75NTR. Each receptor mediates a different signaling
cascade resulting in different physiological outputs. The vast research and knowledge
concerning BDNF, includes studies exploring neuronal populations and mechanisms
responsible for protein synthesis and secretion. In addition, a great effort has been made
in characterizing target neuronal populations and the mechanisms resulting from BDNF
binding. In this report we describe recent use of Alomone Labs' recombinant human
BDNF, Anti-BDNF antibody and signaling modulators and their contributions to the
growing understanding regarding the role played by BDNF in physiology and disease.
Introduction
The BDNF protein complex is a large intercellular
signaling molecule, which is synthesized,
and exocytosed from a defined population of
neurons in order to affect neighboring and remote
cells. The affected cells respond in a variety of
signaling cascades at the molecular level. The
complexity of the signaling system affected by
neurotrophins in general and BDNF in particular,
arises also from the notion that the precursor
protein (proBDNF) is also a signaling mediator.
In addition, the TrkB and p75NTR receptors might
be stimulated by more than one neurotrophin.
Cellular signaling, following BDNF binding, may
lead to many physiological outcomes at the
cellular and systemic levels. These include,
synapse formation and modulation of synaptic
elements during neuronal development, injury,
repair or plasticity associated with sleep control,
pain perception, learning and memory, as well
as with related diseases. BDNF binding may also
lead to the inhibition of neuronal apoptosis,
which might be involved in the control of neuronal
death and injury repair, strongly associated with
neurodegenerative diseases such as Alzheimer’s,
Parkinson’s and Huntington’s diseases (for review
see reference 31).
The BDNF effects on cell migration are involved in
embryonic development of the nervous system as
well as in malignant brain diseases.
Figure 1. Mutant Huntington’s (mhtt) Reduces the Number of Val-BDNF but not MetBDNF Vesicles.
A) BDNF-containing vesicles were counted as follows: each stack of images was thresholded, and Anti-BDNF antibody
(#ANT-010) staining was marked in red. B) All of the marked spots comprising 2–10 pixels were counted, showing
a reduction in Val-BDNF-containing vesicles in mhtt cells compared with wild type cells. C) Colocalization between
Val-BDNF or Met-BDNF and secretogranin II (SecII). D) Val-BDNF in mhtt cells showed a reduced colocalization with
secretogranin II compared with wild type cells.
Adapted from reference 9 with permission of The Society for Neuroscience.
Neural Pathways No.1 Spring 2010 www.alomone.com
11
Perhaps due to a combination of all or some of
the actions mentioned above, BDNF is, for some
cellular populations, an agent promoting neuronal
differentiation and survival both in vivo and in
culture.
BDNF Processing, Secretion and
Receptor Binding
the activation and type of glutamate receptor,
on lesion localization and on the developmental
stage21 (Figure 2).
that knockdown of BDNF in specific brain regions
brings on behaviors associated with depression
and reduced neurogenesis43 (Figure 3).
Depression could be associated with reduced
expression of BDNF in the hippocampus. In order
to validate the reduced expression of BDNF in
specific brain regions following shRNA, Anti-BDNF
was used in in vivo studies43. It was concluded
In in vivo cortical unilateral microinjections of
BDNF, EEG sleep-related parameters in rats are
affected, suggesting that BDNF may also have
a role in the homeostatic regulation of sleep12.
In addition, intrahippocampal delivery of BDNF
BDNF is expressed in neurons and its synthesis
and secretion are highly regulated (for review see,
reference 15).
In order to study the differential vesicular
targeting and time course of synaptic secretion
of mammalian BDNF in cultured hippocampal
neurons3, hBDNF (#B-250) was used to compare
its activity with that of expressed GFP-BDNF.
Heterologously expressed GFP-BDNF behaved
similarly to hBDNF-treated cells.
Figure 2. Effects of Intracerebral BDNF on Cortical Gray Matter, DNA Fragmentation
and Caspase 3 Activation Induced by Ibotenate Injection on P5.
In a study initiated to explore the involvement
of BDNF polymorphism in Huntington’s disease,
Anti-BDNF antibody (#ANT-010) was used to
investigate intracellular trafficking and release of
mutant BDNF9. In this study it was demonstrated
that the gene mutated in Huntington’s disease
(htt), differentially affects the trafficking and
release of two BDNF polymorphs, and as a
consequence, differentially affects cell survival,
depending on the BDNF polymorph9 (Figure 1).
As mentioned above, following its release to
the extracellular space, BDNF binds to TrkB
and to a lesser extent p75NTR on the cell surface
membrane6. It was demonstrated, using K252a
(#K-150) (a known kinase inhibitor, which also
inhibits TrkB), that BDNF exerts its effect by
directly activating TrkB17,19,36,2. Accordingly, in a
different study in hippocampal neurons, the role
of a truncated form of TrkB receptor, TrkB.T1, was
studied. It was demonstrated that the truncated
receptor is constitutively active and the induction
of filopodia, is independent of BDNF binding18.
Physiological Outcomes of
Cellular Activation by BDNF
Signaling
The physiological effects of elevated BDNF
levels are clearly demonstrated by in vivo
injections, followed by behavioral as well as other
functional examinations of the injected animals.
Such studies, suggest that BDNF plays a role
in processes ranging from neuroprotection to
memory storage.
It was demonstrated that BDNF has a protective
role in induced neonatal excitotoxicity, by
inhibiting apoptotic pathways, when injected in
vivo. This protective effect was dependent on
12
Analyses were performed on P6. Tunel-stained sections showing DNA fragmentation induced by ibotenate alone (A)
or hBDNF (#B-250) labeled with ibotenate (B). C) Quantitative analysis of Tunel-stained nuclei in the cortical gray
matter. Cleaved caspase 3 immunostained sections showing caspase 3 activation induced by ibotenate alone (D) or
ibotenate-BDNF (E). F) Quantitative analysis of cleaved caspase 3-immunolabeled cells in the cortical gray matter.
Adapted from reference 21 with permission of Oxford University Press.
Neural Pathways No.1 Spring 2010 www.alomone.com
reverses the deficit in memory persistence caused
by inhibition of hippocampal protein synthesis.
Thus, BDNF is necessary and sufficient to induce
a late post-acquisition phase in the hippocampus,
essential for persistence of long term memory
storage1 (Figure 4).
be blocked by K252a)8 leading to cell survival.
and promote survival23 by activating PDK1,
The activation of the cell survival pathway also
ERK1/2 and RSK1/227. In this experiment BDNF
leads to the inhibition of the pro-apoptotic kinase,
was used to stimulate neurons, while several
GSK3β.
parameters related to the downstream signaling
In a central nervous system trauma model, using
adult rat retinal ganglion cells, it was observed
cascades were measured. For instance, the
effect and time course of BDNF stimulation on
the phosphorylation state of RSK was measured
BDNF and Neuronal Survival
that in vivo injection of BDNF enhances neuronal
survival by activating the PI3K-PKB pathway,
by western blot detection of the phosphorylated
In general, the cell signaling pathways activated
by BDNF mostly include that of PI3K-PKB, and in
parallel, the activation ERK1/2 MAPK (which could
which suppresses apoptosis by inhibiting caspase
versus the non phosphorylated protein. BDNF was
328. In cortical neurons, as well as in hippocampal
found to increase the phosphorylation of RSK27
neurons, BDNF was shown to prevent apoptosis
(Figure 5).
Figure 3. Validation of LV-shBDNF Infection and BDNF Knockdown in vitro
Figure 4. BDNF is Necessary and Sufficient
and in vivo.
for Memory Persistence.
A
B
C
D
BDNF protein expression using Anti-BDNF antibody (#ANT-010) was measured in C6 rat glioma cell
line and in vivo in response to infection with lentiviral vector (LV) expressing either green fluorescent
protein (GFP) only (LV-GFP; infection control), scrambled shRNA (LV-shSCR; shRNA control) or shRNA
complementary to the coding exon of the rat BDNF gene (LV-shBDNF; active sequence). A) BDNF
levels measured in a C6 cell medium 48 h after infection. Data are presented as percentages of
BDNF secreted from non-infected control cells. B) BDNF levels in the dentate gyrus (DG) measured
by immunohistochemistry and epifluorescence microscopy. C) BDNF levels in the dDG measured
A) hBDNF (#B-250) rescues the impairment in memory persistence
by ELISA and normalized per total protein. D) Representative micrographs of hippocampal slices
caused by inhibition of protein synthesis. Anisomycin caused amnesia
including the dDG from rats injected with LV-shSCR (control) or LV-shBDNF (BDNF KD) (upper panels).
7 days after training when infused 12 h after learning (dark gray). This
The micrographs in the left represent the infection spread based on GFP expression (green) within the
effect was reversed by infusion of hBDNF (0.25 μg per side) 15 min
sections. BDNF protein expression was visualized by immunohistochemical staining (middle panels).
later (light gray). B) Intrahippocampal infusion of BDNF antisense
Note the significant reduction in BDNF expression induced by the LV-shBDNF microinjection. Cell
oligonucleotide (BDNF ASO) late after IA training blocks memory
nuclei were visualized using Hoechst staining (lower panels). The micrographs on the right show a
retention at 7, but not at 2 days after training. BDNF ASO, but not BDNF
higher magnification of an infected hippocampal region. The upper panels shows GFP expression as
missense oligonucleotide (BDNF MSO) infusion, 10 h after training
an infection marker, whereas the middle panels shows BDNF protein staining. The lower panels shows
hinders memory persistence at 7 days but leaves memory intact 2 days
superimposition of the upper and middle panels to highlight cells expressing both GFP and BDNF. The
after training. The dorsal hippocampus of the animals was infused with
arrows highlight that while the rat brain infected with LV-shSCR shows BDNF expression within infected
BDNF MSO (white bars) or BDNF ASO (gray bars) 10 h after training.
(GFP) cells, none of the infected cells in the LV-shBDNF rat brain show BDNF expression.
Adapted from reference 1 with permission of The National Academy of
Adapted from reference 43 with permission of Macmillan Publishers Ltd.
Sciences of the USA (copyright 2008).
Neural Pathways No.1 Spring 2010 www.alomone.com
13
BDNF promotes cell survival in chicken motor
neuron culture, via the activation of PKB
which is dependent on Ca2+, CaM, membrane
depolarization and Calmodulin Kinase IV11,24. In
rat and mouse spinal motor neurons, neuronal
death elicited in vitro by excitotoxic insult,
or the expression of mutant SOD1, or polyQexpanded androgen receptor was abrogated
by the expression of nuclear-targeted FOXO3a
transcription factor. The downstream effectors of
this pathway are not clear but, BDNF which caused
a reduction in FOXO3a phosphorylation did not
protect against mutant SOD toxicity38.
BDNF Effects on Gene Expression
BDNF was shown to affect gene expression either
by measuring transcription factor activity or by
directly measuring mRNA or protein levels. Such
alterations in gene expression may establish the
basis of neuronal survival, memory storage and
pain perception in response to BDNF. Presented is
a list of publications showing usage of hBDNF and
its downstream effects on gene expression.
In cultured neocortical neurons, BDNF-induced
CREB phosphorylation/activation which is
dependent on MSK1 (Mitogen- and StressActivated Protein Kinase) and mediated by
ERK1/2-activated kinase, was absent in cells
deficient for MSK141. In rat cerebral cortical
neurons, BDNF (and other neurotrophins) activate
PARP-1 to control gene expression45. In developing
cortical neurons, BDNF increases glucose
utilization and the expression of GLUT34, but does
not lead to GLUT8 surface expression in PC12
cells and hippocampal neurons47. In cultured
rat hippocampal neurons, BDNF activates NFAT
(Nuclear Factor of Activated T-Cells) dependent
transcription via TrkB which is inhibited upon
K252a treatment and triggers the rapid nuclear
translocation of NFATc417. In cultured DRG
neurons, axonal levels of the KV3.1a K+ channel
mRNA were decreased by NGF and BDNF, while
NT-3 increased its expression48. In another
experiment in DRG neurons, it was demonstrated
that BDNF affected the expression of DamageInduced Neuronal Endopeptidase (DINE/ECEL) in
DRG neurons26.
BDNF Effects on Morphological
Neuro- and Synapto-Genesis
One of the main activities attributed to BDNF as
a neurotrophic factor is neuritis and synapse
formation, during embryonic and postnatal
development as well as in adult plasticity, such
as memory storage. In order to demonstrate its
role in synapse formation, hBDNF was injected in
vivo in rat brain to initiate re-innervations in the
cerebellum. Following hBDNF injection, VGLUT2positive climbing fibers (a synaptic marker)
were found to contact somatic thorns during late
postnatal re-innervations of Purkinje cells30.In a
different study it was demonstrated that BDNF
promotes growth of filopodia in dendrites and
in parallel also destabilizes the spines, each of
these, mediated by a different signaling cascade.
These different pathways were assessed by
selectively blocking key components of the
pathway, after BDNF stimulation and examining
the effects using microscopy to visualize the
dendrites morphology as well as with western
blot to measure phosphorylation of key enzymes29
(Figure 6). In addition, it was demonstrated
that, signaling by BDNF regulates axon
morphogenesis and branching, through β-catenin
phosphorylation7. In nonpyramidal neocortical
interneurons, in developing organotypic cultures,
BDNF mediates depolarization-induced dendritic
growth and branching22. In chick DRG neurons,
it was demonstrated that the process of neurite
outgrowth is initiated by BDNF and is dependent
on signaling cations such as zinc40. As mentioned
above, BDNF affects many parameters of neuronal
growth, proper function and morphology.
However, it has no effect on myelination in mouse
brain cultures42.
BDNF Effects on Synaptic
Transmission
Figure 5. PDK1-Mediated Activation of RSK1/2 in BDNF-Stimulated Neurons.
Neurons were stimulated with 10 ng/ml hBDNF (#B-250) as indicated. A) BDNF increased PDK1mediated phosphorylation of RSK1/2. B) The BDNF-mediated increase of pSer221/227 required
activities of the ERK1/2 pathway and PDK1. Although in neurons treated with either the vehicle (Veh)
or the PI3K inhibitor LY294002 (LY), BDNF treatment elevated pSer221/227, the MKK1/2 inhibitor
U0126 or the PDK1 pathway inhibitor TPCK blocked that effect.
Adapted from reference 27 with permission of The Society for Neuroscience.
14
In addition to the observed morphological
changes, BDNF directly affects the activity of
certain synapses, leading to changes in brain
activity and behavior. In general, BDNF inhibits
inhibitory synapses and enhances excitatory
synapses, leading to increased overall activity. For
example, BDNF increases spontaneous network
activity in the superficial layers of the mouse
superior colliculus by suppressing GABAergic
inhibition by the acute downregulation of GABA
(A) Receptors, through PKC activation in the
postsynaptic cell via TrkB. These effects, were
induced by BDNF in Bdnf -/- mice19. BDNF-induced
changes in GABA (A) Receptor phosphorylation
may provide a dynamic mechanism for modulating
the efficacy of fast synaptic inhibition and
thereby, neuronal excitability in the brain. In
cultured cortical and hippocampal neurons, the
mechanisms underlying the BDNF dependent
modulation of GABAergic synaptic transmission
was studied in detail. Results show that BDNF
modulates both GABAergic synaptic currents and
GABA (A) Receptor -β3 subunit phosphorylation
by selectively targeting PKC, RACK-1, and protein
phosphatase 2A (PP2A) to these receptors25.
BDNF modulates both postsynaptic and
presynaptic NMDA Receptors to enhance
transmission in brain slices. Such effects are
Neural Pathways No.1 Spring 2010 www.alomone.com
different depending on the brain regions35. In
distal basal dendritic regions of neocortical
pyramidal neurons, pairing of NMDA spikes and
BDNF is necessary for LTP induction14.
In the rat superficial spinal dorsal horn
organotypic culture, BDNF differentially affects
inhibitory and excitatory synapses, contributing
to the overall excitability and central sensitization
related to pain sensation33 (Figure 7). Like in
the chronic constriction injury (CCI) model of
chronic pain, BDNF mimics the effect of activated
microglia in reducing inhibitory drive and
enhancing excitatory drive34.
BDNF Effects on Differentiation
and Proliferation
Probably due to a combination of many of the
factors mentioned above, BDNF is also considered
as a general agent that promotes, in certain
cellular populations, neuro-differentiation and
proliferation. Below, we list several recent papers
in which BDNF was used to maintain neuronal
cultures.
hBDNF is used to differentiate SH-SY5Y cells into
neuron like cells10 and does so by ultimately upregulating Bcl-2 which leads to the inhibition of
apoptosis46 (Figure 8). Hypoxia-inducible Factor-1
(HIF-1) is a transcriptional activator activated
under hypoxic conditions and involved in TRKB
gene transcription. Enhanced expression of
TrkB could represent a critical switch for the
dedifferentiation of neuroblastoma cells under
hypoxic conditions. Cell migration under hypoxia
and normal O2 levels was reduced significantly in
the absence of BDNF36.
cholinergic neurons, noradrenaline (NA) rescues
cells from degeneration caused by low-level
oxidative stress. Neither NGF nor BDNF alone,
was able to mimic the protective action of NA,
although when combined, both neurotrophins
seemed dependent on the presence of the
neurotransmitter to reinforce the expression of
the cholinergic phenotype44.
BDNF supports survival of cortical projection
neurons5, GABAergic cerebellar interneurons13 and
motor neuron cultures37, as well as postmortem
brain tissue maintained in culture medium39.
hBDNF could also be used to maintain sensory
neurons and promote explant geniculation16.
In hippocampal granule neurons, BDNF regulation
of proliferation and differentiation is mediated
by the SMAD pathway32. In cultured septal
Figure 6. BDNF Promotes Growth of Filopodia and Destabilizes Dendritic Spines, and Short-Term Inhibition of PI3K-Akt-mTOR and Promotes
Spine Development.
The micrographs depict close-up views of 15 days in vitro (DIV) dendritic protrusions from hippocampal neurons transfected with GFP on 6 DIV and treated with hBDNF (#B-250) alone or with
drugs for 24 h starting on 14 DIV. GFP control (A), hBDNF (20 ng/ml) (B), and coapplication of hBDNF with K252a (200 nM) (C), LY294002 (D; LY), wortmannin (E; Wort), U0126 (F; U0), LY294002
plus U0126 (G), and rapamycin (H; Rap). I) and J) show mean for spine and filopodia densities, respectively. K), L) Western blot analysis to ascertain the efficacy and specificity of treatment with
hBDNF and pharmacological inhibitors for the above morphological experiments. Sister coverslips were harvested and probed for pAkt, pMAPK, and pS6. A representative experiment is shown
(K). L) Quantifications of the western blots from three independent experiments.
Adapted from reference 29 with permission of The Society for Neuroscience.
Neural Pathways No.1 Spring 2010 www.alomone.com
15
Figure 7. Enhanced K+-Induced Ca2+ Rise in BDNF-Treated Organotypic Culture Slices.
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E
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Related Products
Compound
B
C
A) SH-SY5Y cells were differentiated by
sequential treatment with retinoic acid (RA)
and hBDNF (#B-250). The undifferentiated
SH-SY5Y (filled circle) and the differentiated
SH-SY5Y-N cells (empty circle) were treated
for 16 h with various doses of camptothecin
D
E
(B), etoposide (D), and cisplatin (E) or 30 ng/
ml camptothecin over a time course (C). Cell
viability was analyzed by the trypan blue
exclusion assay.
Adapted from reference 46 with permission
of Macmillan Publishers Ltd.
Cat. #
Neutrophins
hBDNF________________________________________
BDNF prodomain (WT-human)____________________
proBDNF (WT-mouse)_ __________________________
proBDNF (Mut-mouse)___________________________
proBDNF (WT-human)_ __________________________
proBDNF (Mut-human)__________________________
B-250
B-245
B-240
B-243
B-257
B-256
Neutrophic Factor Antibodies
Anti-BDNF_ ____________________________________ ANT-010
Anti-proBDNF_ _________________________________ ANT-006
Protein Kinase Inhibitors (non-specific)
K252a_________________________________________ K-150
16
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