Source 1review2000British Journal of Pharmacology
Toolkit/[3H]-XAC
[3H]-XAC
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The A1-selective antagonist [3H]-XAC, having high levels of non-specific binding (Ukena et al., 1986), does not permit satisfactory binding studies of A2A receptors.
Usefulness & Problems
Why this is useful
This is an antagonist radioligand discussed as one attempted tool for receptor binding studies. The review cites it mainly as an unsatisfactory option for A2A receptor characterization.; comparison point in radioligand selection for adenosine receptor binding studies
Source:
This is an antagonist radioligand discussed as one attempted tool for receptor binding studies. The review cites it mainly as an unsatisfactory option for A2A receptor characterization.
Source:
comparison point in radioligand selection for adenosine receptor binding studies
Problem solved
The abstract does not support a clear successful use case for A2A characterization.
Source:
The abstract does not support a clear successful use case for A2A characterization.
Problem links
The abstract does not support a clear successful use case for A2A characterization
LiteratureThe abstract does not support a clear successful use case for A2A characterization.
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The abstract does not support a clear successful use case for A2A characterization.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Techniques
Functional AssayTarget processes
No target processes tagged yet.
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
not suitable for satisfactory A2A receptor binding characterization according to the review
It does not provide satisfactory A2A receptor binding studies because of high non-specific binding.; high levels of non-specific binding; does not permit satisfactory binding studies of A2A receptors
Validation
Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication
Supporting Sources
Ranked Claims
Activation of platelet A2A receptors increases cyclic AMP accumulation and decreases platelet aggregation.
Adenotin is a low-affinity non-receptor binding protein that confounds membrane binding analyses of A2A receptors and precluded direct characterization in platelet membranes with earlier ligands.
A2A adenosine receptors are expressed in human peripheral blood cells including platelets, lymphocytes, and neutrophils and are linked to platelet antiaggregatory, neutrophil antiinflammatory, and immune-modulatory effects.
[3H]-CGS 21680 interacts with platelet A2A receptors but is unsatisfactory in human platelet membranes because it also labels low-affinity non-receptor sites; it becomes more adequate after purification that reduces adenotin interference.
[3H]-NECA is unsatisfactory for direct characterization of human platelet A2A receptors because much of its binding in platelet membranes is to non-receptor sites.
[3H]-XAC does not permit satisfactory A2A receptor binding studies because of high non-specific binding.
[3H]-SCH 58261 enabled satisfactory binding characterization of the A2A receptor subtype in human platelets and is presented as the first radioligand to do so.
Approval Evidence
1 source1 linked approval claimfirst-pass slug 3h-xac
The A1-selective antagonist [3H]-XAC, having high levels of non-specific binding (Ukena et al., 1986), does not permit satisfactory binding studies of A2A receptors.
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tool limitationsupports
[3H]-XAC does not permit satisfactory A2A receptor binding studies because of high non-specific binding.
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Comparisons
Source-stated alternatives
The review contrasts it with [3H]-CGS 21680 and [3H]-SCH 58261, with [3H]-SCH 58261 presented as the more successful A2A radioligand.
Source:
The review contrasts it with [3H]-CGS 21680 and [3H]-SCH 58261, with [3H]-SCH 58261 presented as the more successful A2A radioligand.
Source-backed strengths
The A1-selective antagonist [3H]-XAC, having high levels of non-specific binding (Ukena et al., 1986), does not permit satisfactory binding studies of A2A receptors.
Compared with [3H]-CGS 21680
The review contrasts it with [3H]-CGS 21680 and [3H]-SCH 58261, with [3H]-SCH 58261 presented as the more successful A2A radioligand.
Shared frame: source-stated alternative in extracted literature
Relative tradeoffs: high levels of non-specific binding; does not permit satisfactory binding studies of A2A receptors.
Source:
The review contrasts it with [3H]-CGS 21680 and [3H]-SCH 58261, with [3H]-SCH 58261 presented as the more successful A2A radioligand.
Compared with [3H]-SCH 58261
The review contrasts it with [3H]-CGS 21680 and [3H]-SCH 58261, with [3H]-SCH 58261 presented as the more successful A2A radioligand.
Shared frame: source-stated alternative in extracted literature
Relative tradeoffs: high levels of non-specific binding; does not permit satisfactory binding studies of A2A receptors.
Source:
The review contrasts it with [3H]-CGS 21680 and [3H]-SCH 58261, with [3H]-SCH 58261 presented as the more successful A2A radioligand.
Ranked Citations
- 1.