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Human GDNF Protein expressed in Escherichia coli (E. coli) - ABIN1686334
Pelletier, Lagacé, St-Amour, Arsenault, Cisbani, Chabrat, Fecteau, Lévesque, Cicchetti: The morphological and molecular changes of brain cells exposed to direct current electric field stimulation. in The international journal of neuropsychopharmacology / official scientific journal of the Collegium Internationale Neuropsychopharmacologicum (CINP) 2015
results contradict previous studies suggesting that mammalian GFRalpha1 (show GFRA1 Proteins) and GDNF cannot bind and activate non-mammalian RET (show RET Proteins) and vice versa
the dynamics of glial cell line-derived neurotrophic factor (gdnf) and nitric oxide synthases (nos) mRNA expression in various regions of zebrafish brain
GDNF family ligands including tyrosine kinase receptor (show KDR Proteins) RET (show RET Proteins) are investigated within the adult zebrafish brain.
GDNF is a major determinant of directed neuritic growth , and GDNF acts by promoting local neurite outgrowth.
These results demonstrated the expression of the GDNF receptorial complex in adult zebrafish cerebellum and suggest an autocrine mode of action of GDNF in Purkinje cells.
These results showed that the expression of GDNF is not probably restricted during development but it might be involved in the physiology of adult zebrafish retina.
The expression of glial cell line-derived neurotrophic factor (GDNF) was not restricted to developmental periods but it seems that this factor might be involved in adult zebrafish brain physiology, as observed in mammals.
Analysis of striatal brain samples confirms increased GDNF expression in lentiviral vector-GDNF treated aged animals that correlates with functional improvements and preserved dopaminergic markers, dependent upon GDNF levels.
These results suggest that chronic overexpression of GDNF in brain astrocytes exerts an opposing influence on nigrostriatal dopamine metabolism and neurotransmission.
GDNF promotes self-renewal by blocking differentiation and not by promoting proliferation.
Cross-platform single cell analysis of kidney development shows stromal cells express Gdnf.
Our study provides, for the first time, a global analysis of phosphorylation events in spermatogonial progenitor cells (SPCs) in response to GDNF, and we have identified activation of mTORC1 signaling through ERK kinase-mediated phosphorylation of multiple sites of raptor protein as an important pathway for SPC proliferation.
Data show that NEDL2 regulates GDNF/Ret/Akt pathway depends on its Nedd8 ligase activity rather than ubiquitin ligase activity.
Six2 (show SIX2 Proteins) mediates the protective effects of GDNF on damaged DA neurons by regulating Smurf1 (show SMURF1 Proteins) expression.
Ret (show RET Proteins) is essential to mediate GDNF's neuroprotective and neuroregenerative effect in a Parkinson disease mouse model.
identified IFNg (show IFNG Proteins), Neurturin (Nrtn (show NRTN Proteins)), and glial-derived neurotrophic factor (GDNF) as ligands with unexpected roles in promoting neurogenic differentiation (show NEUROD1 Proteins) of Neural Precursor Cells in vivo.
Using an organ culture system for prostate development and Ret mutant mice, we demonstrate that RET-mediated GDNF signaling in UGS increases proliferation of mesenchyme cells and suppresses androgen-induced proliferation and differentiation of prostate epithelial cells, inhibiting prostate development.
The GDNF-GFRalpha1 (show GFRA1 Proteins) complex is essential for proper hippocampal circuit development.
Spatial expression analysis by whole-mount in situ hybridization showed that the GDNF mRNA was predominantly detected in somites, pronephros, pharyngeal arches, epibranchial placodes, digestive tract and some of the lateral line structure.
the inverse relationship between GFRalpha1 (show GFRA1 Proteins) and C-Ret (show RET Proteins), as knocking down C-Ret (show RET Proteins) led to increases in GFRalpha1 (show GFRA1 Proteins) expression.
Our experiments presented a new mechanism adopted by GDNF supporting glioma development and indicated a possible therapeutic potential via the inhibition of proN-cadherin/FGFR1 (show FGFR1 Proteins) interaction.
This study showed that the GDNF levels in preterm newborns were higher in cord blood and lower in CSF (show CSF2 Proteins) as compared to term newborns.
We thus confirmed the role of GDNF as an adaptive survival factor, and its alteration appears to have a key role in nephrocalcinosis. We also discovered that, in GDNF-silenced cells, death occurs in a programmed but caspase (show CASP3 Proteins)-independent manner.
Results suggested that while alterations at 5:37812784 T > A and 5:37812782 T > A sites related with higher GDNF serum levels and less functionality, and alterations at rs62360370 G > A 3'UTR SNP of GDNF associated with higher severity and lower functionality. However, alterations at both rs2075680 C > A and rs79669773 T > C SNPs affect neither GDNF serum levels nor severity and functionality in bipolar disorder.
To our knowledge, this is the first study which correlates GDNF levels with metabolic parameters. Our results show no differences in GDNF serum level between schizophrenia, a first depressive episode, and healthy controls. GDNF serum level did not correlate with metabolic parameters except for total cholesterol in depression.
The results suggest an interaction between NGF (show NGFB Proteins), GDNF and MMP-9 (show MMP9 Proteins) during the transition to malignancy in prostate cancer (PC). Also this interaction may involve in regulating PC cell differentiation, tumor invasion, progression, and the agressiveness of PC.
Study also demonstrates that the interaction between GDNF and proN-cadherin activates specific intracellular signaling pathways; furthermore, GDNF promoted the secretion of matrix metalloproteinase-9 (MMP-9 (show MMP9 Proteins)), which degrades the ECM (show MMRN1 Proteins) via proN-cadherin.
Protective effect of GDNF-engineered amniotic fluid-derived stem cells on the renal ischaemia reperfusion injury in vitro.
GDNF has a role in lower than expected motor development, but while IL-1beta (show IL1B Proteins) and CXCL8/IL-8 (show IL8 Proteins) values were higher in the group with typical motor development among preterm neonates
This gene encodes a highly conserved neurotrophic factor. The recombinant form of this protein was shown to promote the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. Multiple transcript variants encoding different isoforms have been found for this gene. Mutations in this gene may be associated with Hirschsprung disease.
, Glial cell line derived neutrophic factor
, astrocyte-derived trophic factor
, glial cell line derived neurotrophic factor
, glial cell line-derived neurotrophic factor
, glial cell line-derived neurotrophic factor long form
, glial cell derived neurotrophic factor
, glial cell-line derived neurotrophic factor
, neurotrophic factor
, glial cell line-derived neurotrophic factor a
, glia-derived neurotrophic growth factor