In membranes from human breast carcinomas, unlabeled hexarelin displaced bound [(125)I]-Tyr-Ala-hexarelin.
In plain wordsIn lab tests on human breast tumour membranes, hexarelin competed for the same binding sites as a labelled hexarelin analogue.
- Peptide
- Hexarelin
- Outcome
- Not applicableDisplacement of radioligand binding
- Study
humann: not reported in source
Human breast carcinoma membranes- Outcome group
- Receptor activity and mechanism · Cancer
- Studied dose
- Dose not stated
Source sentences
[(125)I]-Tyr-Ala-hexarelin bound to tumor membranes was displaced by different unlabeled GHS such as hexarelin, Tyr-Ala-hexarelin, human ghrelin, and MK-0677 as well as by desoctanoyl-ghrelin and hexarelin derivative EP-80317, which are devoid of GH-releasing properties in vivo.
1 context sentence(design, population, supporting numbers)
The presence of specific GHS-Rs has now been investigated in nontumoral and neoplastic human breast tissue using a radioiodinated peptidyl GHS ([(125)I]-Tyr-Ala-hexarelin) as ligand.