• Corpus ID: 11426911

Melanoma-targeting properties of (99m)technetium-labeled cyclic alpha-melanocyte-stimulating hormone peptide analogues.

  title={Melanoma-targeting properties of (99m)technetium-labeled cyclic alpha-melanocyte-stimulating hormone peptide analogues.},
  author={J Chen and Z Cheng and Timothy Joseph Hoffman and Silvia S. Jurisson and Thomas P. Quinn},
  journal={Cancer research},
  volume={60 20},
Preliminary reports have demonstrated that (99m)technetium (Tc)-labeled cyclic [Cys(3,4,10), D-Phe7]alpha-MSH(3-13) (CCMSH) exhibits high tumor uptake and retention values in a murine melanoma mouse model. In this report, the tumor targeting mechanism of 99mTc-CCMSH was studied and compared with four other radiolabeled alpha-melanocyte stimulating hormone (alpha-MSH) peptide analogues: 125I-(Tyr2)-[Nle4, D-Phe7]alpha-MSH [125I-(Tyr2)-NDP]; 99mTc-CGCG-NDP; 99mTc-Gly11-CCMSH; and 99mTc-Nle11… 
Design and evaluation of new Tc-99m-labeled lactam bridge-cyclized alpha-MSH peptides for melanoma imaging.
Overall, high melanoma uptake coupled with fast urinary clearance of (99m)Tc(EDDA)-HYNIC-GGNle-CycMSH(hex) highlighted its potential for metastatic melanoma detection in the future.
Glycosylated DOTA-alpha-melanocyte-stimulating hormone analogues for melanoma targeting: influence of the site of glycosylation on in vivo biodistribution.
Six glycosylated derivatives of NAPamide, an alpha-MSH octapeptide analogue with high tumor selectivity, are synthesized and evaluated in vitro for MC1R binding and bioactivity and, after labeling with (111)In, for in vitro cellular uptake and in vivo tissue distribution in mice carrying B16F1 melanoma tumors.
111In-labeled lactam bridge-cyclized alpha-melanocyte stimulating hormone peptide analogues for melanoma imaging.
The feasibility of using (111)In-labeled lactam bridge-cyclized alpha-MSH peptide analogues as a novel class of imaging probes for receptor- targeting and biodistribution properties of the radiolabeled conjugates is demonstrated.
PET of Malignant Melanoma Using 18F-Labeled Metallopeptides
Specific in vivo targeting of 18F-FB-RMSH-1 to malignant melanoma was successfully achieved in preclinical models with high MC1R expression and the radiofluorinated metallopeptide 18F/RMSh-1 is a promising molecular probe for PET ofMC1R-positive tumors.
Radiopharmacological characterization of 64Cu-labeled α-MSH analogs for potential use in imaging of malignant melanoma
Due to the prospective radiochemical and radiopharmacological properties of the linear α-MSH derivative [64Cu]Cu-2, this conjugate is a promising candidate for tracer development in human melanoma imaging.
99mTc- and 111In-labeled alpha-melanocyte-stimulating hormone peptides as imaging probes for primary and pulmonary metastatic melanoma detection.
  • Y. Miao, K. Benwell, T. Quinn
  • Biology, Chemistry
    Journal of nuclear medicine : official publication, Society of Nuclear Medicine
  • 2007
The favorable tumor imaging properties of (99m)Tc- and (111)In-labeled alpha-melanocyte-stimulating hormone (alpha-MSH) peptides highlighted their potential as novel probes for primary and metastatic melanoma detection.


In vivo evaluation of 99mTc/188Re-labeled linear alpha-melanocyte stimulating hormone analogs for specific melanoma targeting.
Fluorine-18-labeled [Nle4,D-Phe7]-alpha-MSH, an alpha-melanocyte stimulating hormone analogue.
The normal tissue clearance of [Nle4, D-Phe7, Lys11-(18F) PFB]-alpha-MSH in mice was quite rapid, with little evidence for defluorination.
Binding and internalization of the melanocyte stimulating hormone receptor ligand [Nle4, D-Phe7] alpha-MSH in B16 melanoma cells.
  • W. Wong, R. Minchin
  • Biology
    The international journal of biochemistry & cell biology
  • 1996
Receptor-mediated cytotoxicity of alpha-MSH fragments containing melphalan in a human melanoma cell line.
The data strongly suggest a receptor-mediated cytotoxicity mechanism occurring with alpha-MSH central fragments in human melanoma cells due to the presence of alpha- MSH-specific receptors.
Synthesis and characterization of rhenium-complexed alpha-melanotropin analogs.
A method of labeling peptides with rhenium using a natural amino acid chelating moiety could provide a general means of labeling bioactive peptide fragments that would simplify product purification and characterization.
Characterization of receptors for alpha-melanocyte-stimulating hormone on human melanoma cells.
Receptors for alpha-melanocyte-stimulating hormone (alpha-MSH) on human malignant melanoma cell lines were investigated with a specific binding assay and characterized with structural analogues of
Melanotropin receptors demonstrated in situ in human melanoma.
The use of an in situ binding technique to demonstrate specific MSH receptors in surgical specimens of human melanoma suggests that endogenous melanotropins may modulate the activities of human Melanocyte-stimulating hormones cells in vivo.
Specific receptors for alpha-melanocyte-stimulating hormone are widely distributed in tissues of rodents.
Results show that specific receptors foralpha MSH are widely distributed, suggesting that alpha MSH may affect the functions of a number of organs.
Homologous and Heterologous Regulation of α-Melanocyte-stimulating Hormone Receptors in Human and Mouse Melanoma Cell Lines
Taken together, MSH receptors on melanoma cells are both positively and negatively regulated, whereas cAMP-dependent protein kinase activation seems to be involved in down-regulation, the mechanism responsible for up-regulation remains to be elucidated.