Alterations in BDNF (brain derived neurotrophic factor) and GDNF (glial cell line-derived neurotrophic factor) serum levels in bipolar disorder: The role of lithium

2014 ◽  
Vol 166 ◽  
pp. 193-200 ◽  
Author(s):  
Zeliha Tunca ◽  
Aysegul Ozerdem ◽  
Deniz Ceylan ◽  
Yaprak Yalçın ◽  
Güneş Can ◽  
...  
2011 ◽  
Vol 25 (11) ◽  
pp. 1480-1484 ◽  
Author(s):  
Annemarie Heberlein ◽  
Kenneth M Dürsteler-MacFarland ◽  
Bernd Lenz ◽  
Helge Frieling ◽  
Michael Grösch ◽  
...  

Preclinical study results suggest that brain-derived neurotrophic factor (BDNF) and glial cell line-derived neurotrophic factor (GDNF) are involved in the modulation of addictive behaviour. We investigated alterations in serum levels of BDNF and GDNF in opiate-dependent patients (28 males) who received diacetylmorphine treatment within a structured opiate maintenance programme. BDNF ( T = 2.735, p = 0.009) serum levels were significantly increased in the opiate-dependent patients as compared with healthy controls (21 males), whereas GDNF serum levels ( T = 1.425, p = 0.162) did not differ significantly from GDNF serum levels of the healthy controls. BDNF serum levels were significantly associated with craving for heroin (measured by the Heroin Craving Questionnaire ( r = 0.420, p = 0.029) and by the General Craving Scale ( r = 0.457, p = 0.016), whereas GDNF serum levels were not associated with psychometric dimensions of heroin craving. In conclusion, our results show a positive association between BDNF serum levels and opiate craving in opiate-dependent patients.


2020 ◽  
Vol 12 (1) ◽  
pp. 25
Author(s):  
N.A. Shchelchkova ◽  
A.A. Kokaya ◽  
V.F. Bezhenar’ ◽  
O.V. Rozhdestvenskaya ◽  
M.A. Mamedova ◽  
...  

2020 ◽  
Vol 35 (4) ◽  
pp. 565-576 ◽  
Author(s):  
Daniel Enterría‐Morales ◽  
Ivette López‐López ◽  
José López‐Barneo ◽  
Xavier d'Anglemont de Tassigny

2007 ◽  
Vol 404 (1) ◽  
pp. 131-140 ◽  
Author(s):  
Ivan Alfano ◽  
Parvez Vora ◽  
Rosemary S. Mummery ◽  
Barbara Mulloy ◽  
Christopher C. Rider

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.


Neuroscience ◽  
2003 ◽  
Vol 122 (1) ◽  
pp. 229-235 ◽  
Author(s):  
C Harada ◽  
T Harada ◽  
H.-M.A Quah ◽  
F Maekawa ◽  
K Yoshida ◽  
...  

2004 ◽  
Vol 78 (2) ◽  
pp. 250-258 ◽  
Author(s):  
Atsumi Nitta ◽  
Hirofumi Nishioka ◽  
Hidefumi Fukumitsu ◽  
Yoshiko Furukawa ◽  
Haruo Sugiura ◽  
...  

2009 ◽  
Vol 170 (2-3) ◽  
pp. 273-275 ◽  
Author(s):  
Xiaobin Zhang ◽  
Zhijun Zhang ◽  
Weiwei Sha ◽  
Chunming Xie ◽  
Guangjun Xi ◽  
...  

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