Modulation of GABAA receptor binding in human brain by neuroactive steroids: Species and brain regional differences

Synapse ◽  
1995 ◽  
Vol 19 (2) ◽  
pp. 77-87 ◽  
Author(s):  
Quyen Nguyen ◽  
Douglas W. Sapp ◽  
Paul C. Van Ness ◽  
Richard W. Olsen
Keyword(s):  
Human Brain ◽  
Gabaa Receptor ◽  
Receptor Binding ◽  
Regional Differences ◽  
Neuroactive Steroids

Vergleich von Blutfluß und Benzodiazepin-Rezeptorverteilung bei fokaler Epilepsie: Vorläufige Ergebnisse einer SPECT-Studie

1989 ◽  
Vol 28 (05) ◽  
pp. 181-186
Author(s):  
A. Ludolph ◽  
O. Schober ◽  
G. Lottes ◽  
I. Böttger ◽  
H.-F. Beer ◽  
...  
Keyword(s):  
Human Brain ◽  
Receptor Binding ◽  
Brain Area ◽  
Brain Perfusion ◽  
Partial Epilepsy ◽  
Cerebral Lesion ◽  
Receptor Ligand ◽  
Receptor Mapping ◽  
Hmpao Spect ◽  
99Mtc Hmpao

99mTc-HMPAO-SPECT and SPECT with the 123I-labelled benzodiazepine (Bz) receptor ligand Ro 16-0154 were performed in 10 patients suffering from partial epilepsy, without cerebral lesion in MRT or CT. 2 h p.i. of Ro 16-0154 the distribution of activity correlated with the known distribution of Bz- receptors in the human brain. Perfusion and receptor-binding were found decreased in 7 patients of each study in the suspicious brain-area. 123l-labelled Ro 16-0154 is suitable for Bz-receptor mapping by SPECT. The decrease of Bz-receptor binding in epileptic foci, as described in PET-studies, was also detected by SPECT in 7 of 10 patients.

PW01-155 - Seasonal alterations of serotonin-1A receptor binding in the healthy human brain

2010 ◽  
Vol 25 ◽  
pp. 1571
Author(s):  
C. Spindelegger ◽  
P. Stein ◽  
W. Wadsak ◽  
M. Fink ◽  
M. Mitterhauser ◽  
...  
Keyword(s):  
Human Brain ◽  
Receptor Binding ◽  
Serotonin 1A Receptor ◽  
Healthy Human

Subchronic phencyclidine in rats: alterations in locomotor activity, maze performance, and GABAA receptor binding

2010 ◽  
Vol 21 (1) ◽  
pp. 1-10 ◽  
Author(s):  
Richard J. Beninger ◽  
Jonathan Beuk ◽  
Tomek J. Banasikowski ◽  
Michael van Adel ◽  
Gregory A. Boivin ◽  
...  
Keyword(s):  
Locomotor Activity ◽  
Gabaa Receptor ◽  
Receptor Binding ◽  
Maze Performance

Celecoxib does not induce convulsions nor does it affect GABAA receptor binding activity in the presence of new quinolones in mice

2005 ◽  
Vol 507 (1-3) ◽  
pp. 69-76 ◽  
Author(s):  
Taiji Yoshino ◽  
Masahiro Noguchi ◽  
Hiroko Okutsu ◽  
Aishi Kimoto ◽  
Masao Sasamata ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Binding Activity ◽  
Receptor Binding Activity ◽  
New Quinolones

Measurement of GABAA receptor binding in vivo with [11C]Flumazenil: A test–retest study in healthy subjects

NeuroImage ◽  
2008 ◽  
Vol 41 (2) ◽  
pp. 260-269 ◽  
Author(s):  
Elina Salmi ◽  
Sargo Aalto ◽  
Jussi Hirvonen ◽  
Jaakko W. Långsjö ◽  
Anu T. Maksimow ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Receptor Binding ◽  
Healthy Subjects

scholarly journals Ethanol-induced GABAA receptor alpha4 subunit plasticity involves phosphorylation and neuroactive steroids

2016 ◽  
Vol 72 ◽  
pp. 1-8 ◽  
Author(s):  
David F. Werner ◽  
Patrizia Porcu ◽  
Kevin N. Boyd ◽  
Todd K. O'Buckley ◽  
Jenna M. Carter ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Neuroactive Steroids

Neuroactive steroids inhibit spinal reflex potentiation by selectively enhancing specific spinal GABAA receptor subtypes

Pain ◽  
2009 ◽  
Vol 143 (1) ◽  
pp. 12-20 ◽  
Author(s):  
Hsien-Yu Peng ◽  
Gin-Den Chen ◽  
Shin-Da Lee ◽  
Cheng-Yuan Lai ◽  
Chun-Hsien Chiu ◽  
...  
Keyword(s):  
Gabaa Receptor ◽  
Neuroactive Steroids ◽  
Spinal Reflex ◽  
Receptor Subtypes ◽  
Gabaa Receptor Subtypes

scholarly journals Cortisol Stress Response and in Vivo PET Imaging of Human Brain Serotonin 1A Receptor Binding

2019 ◽  
Vol 22 (5) ◽  
pp. 329-338 ◽  
Author(s):  
Louisa J Steinberg ◽  
Harry Rubin-Falcone ◽  
Hanga C Galfalvy ◽  
Joshua Kaufman ◽  
Jeffrey M Miller ◽  
...  
Keyword(s):  
Stress Response ◽  
Human Brain ◽  
Receptor Binding ◽  
Pet Imaging ◽  
Brain Serotonin ◽  
Serotonin 1A Receptor

scholarly journals Single Domain Antibodies Targeting Receptor Binding Pockets of NadA Restrain Adhesion of Neisseria meningitidis to Human Brain Microvascular Endothelial Cells

2020 ◽  
Vol 7 ◽  
Author(s):  
Amod Kulkarni ◽  
Evelína Mochnáčová ◽  
Petra Majerova ◽  
Ján Čurlík ◽  
Katarína Bhide ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Phage Display ◽  
Human Brain ◽  
Receptor Binding ◽  
Phage Library ◽  
Microvascular Endothelial Cells ◽  
Brain Microvascular Endothelial Cells ◽  
Binding Pockets ◽  
Microvascular Endothelial

Neisseria adhesin A (NadA), one of the surface adhesins of Neisseria meningitides (NM), interacts with several cell types including human brain microvascular endothelial cells (hBMECs) and play important role in the pathogenesis. Receptor binding pockets of NadA are localized on the globular head domain (A33 to K69) and the first coiled-coil domain (L121 to K158). Here, the phage display was used to develop a variable heavy chain domain (VHH) that can block receptor binding sites of recombinant NadA (rec-NadA). A phage library displaying VHH was panned against synthetic peptides (NadA-gdA33−K69 or NadA-ccL121−K158), gene encoding VHH was amplified from bound phages and re-cloned in the expression vector, and the soluble VHHs containing disulfide bonds were overexpressed in the SHuffle E. coli. From the repertoire of 96 clones, two VHHs (VHHF3–binding NadA-gdA33−K69 and VHHG9–binding NadA-ccL121−K158) were finally selected as they abrogated the interaction between rec-NadA and the cell receptor. Preincubation of NM with VHHF3 and VHHG9 significantly reduced the adhesion of NM on hBMECs in situ and hindered the traversal of NM across the in-vitro BBB model. The work presents a phage display pipeline with a single-round of panning to select receptor blocking VHHs. It also demonstrates the production of soluble and functional VHHs, which blocked the interaction between NadA and its receptor, decreased adhesion of NM on hBMECs, and reduced translocation of NM across BBB in-vitro. The selected NadA blocking VHHs could be promising molecules for therapeutic translation.

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