Some Secrets of Fluorescent Proteins: Distinct Bleaching in Various Mounting Fluids and Photoactivation of cyan fluorescent proteins at YFP-Excitation

Schmid, Johannes A.; Malkani, Naila

doi:10.1038/npre.2011.4517.2

Cited by 1 publication

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“…After 48 h cells, were fixed in 4% paraformaldehyde for 30 min and mounted on slides using a PBS/glycerol mixture 1:9 as mounting medium . Slides were sealed using colorless nail polish to avoid desiccation.…”

Section: Methodsmentioning

confidence: 99%

Cross-Receptor Interactions between Dopamine D_2L and Neurotensin NTS₁ Receptors Modulate Binding Affinities of Dopaminergics

Koschatzky

Tschammer

Gmeiner

2011

ACS Chem. Neurosci.

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T he ability to form spatial complexes allowing molecular interactions between receptor protomers facilitates cooperative effects and tissue specific control of neuronal activity. Thus, heterodimerization is discussed as an integral feature of G-protein coupled receptor (GPCR) mediated signal transduction. 1À3 Intramembrane receptorÀreceptor interactions of associated protomers may modify binding and activating properties of GPCR ligands. 4À7 Using F€ orster resonance energy transfer (FRET) technique, a recent study on the interactions between R 2A -adrenergic and μ-opioid receptors demonstrated a transinhibitory effect between the protomers. In detail, morphine binding to the μ-opioid receptor triggered the conformational changes in the norepinephrine-occupied R 2A -adrenergic receptor leading to the inhibition of its signaling. 8 Physical interactions between δ-and μ-opioid receptors were suggested to modulate μ-mediated tolerance and dependence 9 when the development of bivalent ligands was constituted as a useful approach to investigate changes in receptor properties as a consequence to dimerization. 10,11 Heterodimerization is also a highly relevant phenomenon for dopamine receptor mediated signaling. 12,13 Demonstrating the development of a new complex with enhanced functional activity through hetero-oligomerization, the physical interaction between the dopamine D 2L and the somatostatin SST5 receptor was investigated via radioligand binding studies, functional assays, and FRET microscopy. 14 The heterooligomerization of D 2L and SST5, known for their colocalization in the central nervous system (CNS), led to a synergistic effect on binding and signaling as molecular cross-talk and the correlation between activated receptor function and oligomerization was stressed.Dopaminergic systems have been also described to functionally interact with the neuromodulatory peptide neurotensin (NT, pE-L-Y-E-N-K-P-R-R-P-Y-I-L) 15 which is suggested to play a role in the pathophysiology of brain diseases including schizophrenia, Parkinson's disease. and Morbus Alzheimer. 16À18 Thus, neurotensin was shown to negatively alter binding affinity of the dopamine receptor agonist [ 3 H]N-n-propyl-nor-apomorphine in specific brain areas. 19À25 However, biomolecular interactions and a putative heteromer formation between dopamine receptors and neurotensin receptors have not been investigated yet.Employing fluorescence detected coimmunoprecipitation and radioligand binding experiments, we herein demonstrate that coexpression of dopamine D 2L receptor and the neurotensin receptor subtype NTS 1 in human embryonic kidney cells (HEK293 cells) leads to physical interaction at a molecular level. In this in vitro system, a trans-inhibitory effect on the agonist binding affinity of D 2 was observed in the presence of neurotensin. A biochemical fingerprint 26 of the D 2L -NTS 1 heteromer was explored by investigating the effect of both neurotensin and NTS 1 on the D 2 receptor binding properties of different ABSTRACT: Dopaminergic systems ...

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Section: Methodsmentioning

confidence: 99%

Cross-Receptor Interactions between Dopamine D_2L and Neurotensin NTS₁ Receptors Modulate Binding Affinities of Dopaminergics

Koschatzky

Tschammer

Gmeiner

2011

ACS Chem. Neurosci.

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Some Secrets of Fluorescent Proteins: Distinct Bleaching in Various Mounting Fluids and Photoactivation of cyan fluorescent proteins at YFP-Excitation

Cited by 1 publication

References 2 publications

Cross-Receptor Interactions between Dopamine D_2L and Neurotensin NTS₁ Receptors Modulate Binding Affinities of Dopaminergics

Cross-Receptor Interactions between Dopamine D_2L and Neurotensin NTS₁ Receptors Modulate Binding Affinities of Dopaminergics

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Some Secrets of Fluorescent Proteins: Distinct Bleaching in Various Mounting Fluids and Photoactivation of cyan fluorescent proteins at YFP-Excitation

Cited by 1 publication

References 2 publications

Cross-Receptor Interactions between Dopamine D2L and Neurotensin NTS1 Receptors Modulate Binding Affinities of Dopaminergics

Cross-Receptor Interactions between Dopamine D2L and Neurotensin NTS1 Receptors Modulate Binding Affinities of Dopaminergics

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Cross-Receptor Interactions between Dopamine D_2L and Neurotensin NTS₁ Receptors Modulate Binding Affinities of Dopaminergics

Cross-Receptor Interactions between Dopamine D_2L and Neurotensin NTS₁ Receptors Modulate Binding Affinities of Dopaminergics