Source 1review2000British Journal of Pharmacology
Toolkit/[3H]-SCH 58261
[3H]-SCH 58261
Also known as: tritium-labelled SCH 58261
Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.
Summary
The tritium-labelled form, [3H]-SCH 58261, has been found to label A2A receptors... On the basis of this pharmacological profile [3H]-SCH 58261 has been used to characterize A2A receptors in human platelet membranes... Thus, [3H]-SCH 58261 is the first radioligand that has allowed the binding characterization of the A2A receptor subtype in human platelets.
Usefulness & Problems
Why this is useful
This radioligand is used to label and characterize A2A adenosine receptors in binding assays. The review presents it as the first ligand that enabled satisfactory binding characterization of the A2A subtype in human platelets and also describes use in lymphocytes and neutrophils.; binding characterization of A2A receptors in human platelet membranes; binding characterization of A2A receptors in human lymphocytes; binding characterization of A2A receptors in human neutrophils; distinguishing A2A receptor binding from confounding non-receptor binding
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This radioligand is used to label and characterize A2A adenosine receptors in binding assays. The review presents it as the first ligand that enabled satisfactory binding characterization of the A2A subtype in human platelets and also describes use in lymphocytes and neutrophils.
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binding characterization of A2A receptors in human platelet membranes
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binding characterization of A2A receptors in human lymphocytes
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binding characterization of A2A receptors in human neutrophils
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distinguishing A2A receptor binding from confounding non-receptor binding
Problem solved
It addresses the prior lack of a selective A2A radioligand and helps avoid misleading non-receptor binding that complicated earlier membrane studies. The review specifically notes that it does not interact with adenotin.; lack of a selective A2A radioligand for direct receptor characterization; interference from adenotin-associated non-receptor binding seen with earlier ligands
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It addresses the prior lack of a selective A2A radioligand and helps avoid misleading non-receptor binding that complicated earlier membrane studies. The review specifically notes that it does not interact with adenotin.
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lack of a selective A2A radioligand for direct receptor characterization
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interference from adenotin-associated non-receptor binding seen with earlier ligands
Problem links
interference from adenotin-associated non-receptor binding seen with earlier ligands
LiteratureIt addresses the prior lack of a selective A2A radioligand and helps avoid misleading non-receptor binding that complicated earlier membrane studies. The review specifically notes that it does not interact with adenotin.
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It addresses the prior lack of a selective A2A radioligand and helps avoid misleading non-receptor binding that complicated earlier membrane studies. The review specifically notes that it does not interact with adenotin.
lack of a selective A2A radioligand for direct receptor characterization
LiteratureIt addresses the prior lack of a selective A2A radioligand and helps avoid misleading non-receptor binding that complicated earlier membrane studies. The review specifically notes that it does not interact with adenotin.
Source:
It addresses the prior lack of a selective A2A radioligand and helps avoid misleading non-receptor binding that complicated earlier membrane studies. The review specifically notes that it does not interact with adenotin.
Taxonomy & Function
Primary hierarchy
Technique Branch
Method: A concrete measurement method used to characterize an engineered system.
Techniques
Functional AssayTarget processes
recombinationInput: Chemical
Implementation Constraints
cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor
Use requires the tritiated ligand, receptor-containing membrane preparations, and radioligand binding assay infrastructure. The review also discusses comparison to functional readouts such as cyclic AMP accumulation and platelet aggregation inhibition.; requires tritium-labelled ligand and radioligand binding assay capability; requires membrane preparations from relevant cells or receptor-expressing systems
The review does not present it as resolving all downstream signaling ambiguities or all physiological questions about A2A function. It is mainly positioned as a receptor-characterization tool.; evidence here is limited to receptor characterization use rather than broader therapeutic utility; the review discusses it as a radioligand tool, not as a complete solution for all signaling questions
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 source3 linked approval claimsfirst-pass slug 3h-sch-58261
The tritium-labelled form, [3H]-SCH 58261, has been found to label A2A receptors... On the basis of this pharmacological profile [3H]-SCH 58261 has been used to characterize A2A receptors in human platelet membranes... Thus, [3H]-SCH 58261 is the first radioligand that has allowed the binding characterization of the A2A receptor subtype in human platelets.
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mechanistic summarysupports
Activation of platelet A2A receptors increases cyclic AMP accumulation and decreases platelet aggregation.
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review summarysupports
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.
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tool performancesupports
[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.
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Comparisons
Source-stated alternatives
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
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The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Source-backed strengths
reported to label one class of binding sites in human platelet membranes; high affinity binding in the nanomolar range is described; does not interact with the adenotin binding site; ligand affinity rankings correlate with functional studies according to the review
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reported to label one class of binding sites in human platelet membranes
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high affinity binding in the nanomolar range is described
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does not interact with the adenotin binding site
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ligand affinity rankings correlate with functional studies according to the review
Compared with [3H]-CGS 21680
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Shared frame: source-stated alternative in extracted literature
Strengths here: reported to label one class of binding sites in human platelet membranes; high affinity binding in the nanomolar range is described; does not interact with the adenotin binding site.
Relative tradeoffs: evidence here is limited to receptor characterization use rather than broader therapeutic utility; the review discusses it as a radioligand tool, not as a complete solution for all signaling questions.
Source:
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Compared with [3H]-NECA
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Shared frame: source-stated alternative in extracted literature
Strengths here: reported to label one class of binding sites in human platelet membranes; high affinity binding in the nanomolar range is described; does not interact with the adenotin binding site.
Relative tradeoffs: evidence here is limited to receptor characterization use rather than broader therapeutic utility; the review discusses it as a radioligand tool, not as a complete solution for all signaling questions.
Source:
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Compared with [3H]-XAC
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Shared frame: source-stated alternative in extracted literature
Strengths here: reported to label one class of binding sites in human platelet membranes; high affinity binding in the nanomolar range is described; does not interact with the adenotin binding site.
Relative tradeoffs: evidence here is limited to receptor characterization use rather than broader therapeutic utility; the review discusses it as a radioligand tool, not as a complete solution for all signaling questions.
Source:
The review contrasts it with [3H]-NECA, [3H]-CGS 21680, and [3H]-XAC. Those alternatives are described as less satisfactory in platelet membrane studies because of non-selective or non-specific binding issues.
Ranked Citations
- 1.