Glial-cell-line-derived neurotrophic factor enhances biosynthesis of substance P in striatal neurons in vitro

1996 ◽  
Vol 286 (2) ◽  
pp. 249-255 ◽  
Author(s):  
C. Humpel ◽  
J. Marksteiner ◽  
A. Saria
Keyword(s):  
Substance P ◽  
Cell Line ◽  
Glial Cell ◽  
Neurotrophic Factor ◽  
Striatal Neurons

Glial cell line-derived neurotrophic factor supplementation promotes bovine in vitro oocyte maturation and early embryo development

2018 ◽  
Vol 113 ◽  
pp. 92-101 ◽  
Author(s):  
Dong-Hui Wang ◽  
Hong-Xia Zhou ◽  
Shu-Jun Liu ◽  
Cheng-Jie Zhou ◽  
Xiang-Wei Kong ◽  
...  
Keyword(s):  
Cell Line ◽  
Glial Cell ◽  
Embryo Development ◽  
Oocyte Maturation ◽  
Neurotrophic Factor ◽  
Early Embryo ◽  
Early Embryo Development ◽  
In Vitro Oocyte Maturation

scholarly journals The major determinant of the heparin binding of glial cell-line-derived neurotrophic factor is near the N-terminus and is dispensable for receptor binding

2007 ◽  
Vol 404 (1) ◽  
pp. 131-140 ◽  
Author(s):  
Ivan Alfano ◽  
Parvez Vora ◽  
Rosemary S. Mummery ◽  
Barbara Mulloy ◽  
Christopher C. Rider
Keyword(s):  
Cell Line ◽  
Glial Cell ◽  
Neurotrophic Factor ◽  
Transforming Growth Factor ◽  
Basic Amino Acid ◽  
Transforming Growth Factor Β ◽  
Heparin Binding ◽  
Binding Sequence

GDNF (glial cell-line-derived neurotrophic factor), and the closely related cytokines artemin and neurturin, bind strongly to heparin. Deletion of a basic amino-acid-rich sequence of 16 residues N-terminal to the first cysteine of the transforming growth factor β domain of GDNF results in a marked reduction in heparin binding, whereas removal of a neighbouring sequence, and replacement of pairs of other basic residues with alanine had no effect. The heparin-binding sequence is quite distinct from the binding site for the high affinity GDNF polypeptide receptor, GFRα1 (GDNF family receptor α1), and heparin-bound GDNF is able to bind GFRα1 simultaneously. The heparin-binding sequence of GDNF is dispensable both for GFRα1 binding, and for activity for in vitro neurite outgrowth assay. Surprisingly, the observed inhibition of GDNF bioactivity with the wild-type protein in this assay was still found with the deletion mutant lacking the heparin-binding sequence. Heparin neither inhibits nor potentiates GDNF–GFRα1 interaction, and the extracellular domain of GFRα1 does not bind to heparin itself, precluding heparin cross-bridging of cytokine and receptor polypeptides. The role of heparin and heparan sulfate in GDNF signalling remains unclear, but the present study indicates that it does not occur in the first step of the pathway, namely GDNF–GFRα1 engagement.

Glial cell line derived neurotrophic factor (GDNF) regulates VR1 and substance P in cultured sensory neurons

Neuroreport ◽  
1999 ◽  
Vol 10 (10) ◽  
pp. 2107-2111 ◽  
Author(s):  
Patrick Ogun-Muyiwa ◽  
Rachel Helliwell ◽  
Peter McIntyre ◽  
Janet Winter
Keyword(s):  
Substance P ◽  
Cell Line ◽  
Glial Cell ◽  
Sensory Neurons ◽  
Neurotrophic Factor

In vitro non-viral lipofectamine delivery of the gene for glial cell line-derived neurotrophic factor to human umbilical cord blood CD34+ cells

2010 ◽  
Vol 1325 ◽  
pp. 147-154 ◽  
Author(s):  
Guolong Yu ◽  
Cesar V. Borlongan ◽  
Yali Ou ◽  
Christine E. Stahl ◽  
SeongJin Yu ◽  
...  
Keyword(s):  
Cord Blood ◽  
Cell Line ◽  
Glial Cell ◽  
Umbilical Cord Blood ◽  
Neurotrophic Factor ◽  
Human Umbilical Cord Blood ◽  
Human Umbilical Cord ◽  
Cd34 Cells ◽  
Cord Blood Cd34

scholarly journals A Novel Activating Mutation in the RET Tyrosine Kinase Domain Mediates Neoplastic Transformation

2006 ◽  
Vol 20 (7) ◽  
pp. 1633-1643 ◽  
Author(s):  
Aaron Cranston ◽  
Cristiana Carniti ◽  
Sam Martin ◽  
Piera Mondellini ◽  
Yvette Hooks ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Cell Line ◽  
Glial Cell ◽  
Neurotrophic Factor ◽  
Functional Characterization ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Exogenous Substrate

Abstract We report the finding of a novel missense mutation at codon 833 in the tyrosine kinase of the RET proto-oncogene in a patient with a carcinoma of the thyroid. In vitro experiments demonstrate that the R833C mutation induces transformed foci only when present in the long 3′ splice isoform and, in keeping with a model in which the receptor has to dimerize to be completely activated, glial cell line-derived neurotrophic factor stimulation leads the RETR833C receptor to a higher level of activation. Tyrosine kinase assays show that the RETR833C long isoform has weak intrinsic kinase activity and phosphorylation of an exogenous substrate is not elevated even in the presence of glial cell line-derived neurotrophic factor. Furthermore, the R833C mutation is capable of sustaining the transformed phenotype in vivo but does not confer upon the transformed cells the ability to degrade the basement membrane in a manner analogous to metastasis. Our functional characterization of the R833C substitution suggests that, like the V804M and S891A mutations, this tyrosine kinase mutation confers a weak activating potential upon RET. This is the first report demonstrating that the introduction of an intracellular cysteine can activate RET. However, this does not occur via dimerization in a manner analogous to the extracellular cysteine mutants.

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