I. Melanin concentrating hormone exhibits both MSH and MCH activities on individual melanophores

Ana Maria Ana; Mac E. Hadley; Brian C. Wilkes; Christian Zechel; Victor J. Hruby

doi:10.1016/0024-3205(87)90041-5

I. Melanin concentrating hormone exhibits both MSH and MCH activities on individual melanophores

Ana Maria Ana, Mac E. Hadley, Brian C. Wilkes, Christian Zechel, Victor J. Hruby

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

Abstract

AspThrMetArgCysMetValGlyArgValTyrArgProCysTrpGluVal (melanin concentrating hormone, MCH) and several fragment analogs (MCH_1-14, MCH_5-17, MCH_5-14) were synthesized and their biological activities determined in a very sensitive fish skin bioassay. The potency ranking and minimum effective doses of the peptides were determined to be: MCH_1-17 (10^-12M) >< MCH_5-17 (10^-12M) > MCH_1-14 (10^-11M) > MCH_5-14 (2 × 10^-10M). The melanosome aggregating activity of MCH could be completely reversed by a 100-fold higher concentration of ≺-MSH. MCH was self-antagonized in a dose-related manner by higher concentrations of the peptide as was the activity of the MCH_1-14 fragment analog. The MCH activities of the MCH_5-17 and MCH_5-14 analogs were not compromised by even the highest concentrations of the peptides employed. The MSH-like activity of MCH appears to relate to the N-terminus of the peptide whereas MCH activity is more a function of the C-terminus of the hormone. Self- antagonism of MCH at high concentrations appears to relate to the N-terminal tetrapeptide, which is responsible for the intrinsic MSH-like activity of the hormone.

Original language	English (US)
Pages (from-to)	1845-1851
Number of pages	7
Journal	Life Sciences
Volume	40
Issue number	19
DOIs	https://doi.org/10.1016/0024-3205(87)90041-5
State	Published - May 11 1987

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
Pharmacology, Toxicology and Pharmaceutics(all)

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10.1016/0024-3205(87)90041-5

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@article{886e45f52fe447c899837e77c1a39863,

title = "I. Melanin concentrating hormone exhibits both MSH and MCH activities on individual melanophores",

abstract = "AspThrMetArgCysMetValGlyArgValTyrArgProCysTrpGluVal (melanin concentrating hormone, MCH) and several fragment analogs (MCH1-14, MCH5-17, MCH5-14) were synthesized and their biological activities determined in a very sensitive fish skin bioassay. The potency ranking and minimum effective doses of the peptides were determined to be: MCH1-17 (10-12M) >< MCH5-17 (10-12M) > MCH1-14 (10-11M) > MCH5-14 (2 × 10-10M). The melanosome aggregating activity of MCH could be completely reversed by a 100-fold higher concentration of ≺-MSH. MCH was self-antagonized in a dose-related manner by higher concentrations of the peptide as was the activity of the MCH1-14 fragment analog. The MCH activities of the MCH5-17 and MCH5-14 analogs were not compromised by even the highest concentrations of the peptides employed. The MSH-like activity of MCH appears to relate to the N-terminus of the peptide whereas MCH activity is more a function of the C-terminus of the hormone. Self- antagonism of MCH at high concentrations appears to relate to the N-terminal tetrapeptide, which is responsible for the intrinsic MSH-like activity of the hormone.",

author = "Ana, {Ana Maria} and Hadley, {Mac E.} and Wilkes, {Brian C.} and Christian Zechel and Hruby, {Victor J.}",

note = "Funding Information: These investigations were supported by Public Health Service grant AM-17420, by National Science Foundation Grant PCM - 810078 (USA) and by Fundac~o de Amparo a Pesquisa do Estado de S~o Paulo, grants 84/1967 and 85/0718-7 ~rasil).",

year = "1987",

month = may,

day = "11",

doi = "10.1016/0024-3205(87)90041-5",

language = "English (US)",

volume = "40",

pages = "1845--1851",

journal = "Life Sciences",

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T1 - I. Melanin concentrating hormone exhibits both MSH and MCH activities on individual melanophores

AU - Ana, Ana Maria

AU - Hadley, Mac E.

AU - Wilkes, Brian C.

AU - Zechel, Christian

AU - Hruby, Victor J.

N1 - Funding Information: These investigations were supported by Public Health Service grant AM-17420, by National Science Foundation Grant PCM - 810078 (USA) and by Fundac~o de Amparo a Pesquisa do Estado de S~o Paulo, grants 84/1967 and 85/0718-7 ~rasil).

PY - 1987/5/11

Y1 - 1987/5/11

N2 - AspThrMetArgCysMetValGlyArgValTyrArgProCysTrpGluVal (melanin concentrating hormone, MCH) and several fragment analogs (MCH1-14, MCH5-17, MCH5-14) were synthesized and their biological activities determined in a very sensitive fish skin bioassay. The potency ranking and minimum effective doses of the peptides were determined to be: MCH1-17 (10-12M) >< MCH5-17 (10-12M) > MCH1-14 (10-11M) > MCH5-14 (2 × 10-10M). The melanosome aggregating activity of MCH could be completely reversed by a 100-fold higher concentration of ≺-MSH. MCH was self-antagonized in a dose-related manner by higher concentrations of the peptide as was the activity of the MCH1-14 fragment analog. The MCH activities of the MCH5-17 and MCH5-14 analogs were not compromised by even the highest concentrations of the peptides employed. The MSH-like activity of MCH appears to relate to the N-terminus of the peptide whereas MCH activity is more a function of the C-terminus of the hormone. Self- antagonism of MCH at high concentrations appears to relate to the N-terminal tetrapeptide, which is responsible for the intrinsic MSH-like activity of the hormone.

AB - AspThrMetArgCysMetValGlyArgValTyrArgProCysTrpGluVal (melanin concentrating hormone, MCH) and several fragment analogs (MCH1-14, MCH5-17, MCH5-14) were synthesized and their biological activities determined in a very sensitive fish skin bioassay. The potency ranking and minimum effective doses of the peptides were determined to be: MCH1-17 (10-12M) >< MCH5-17 (10-12M) > MCH1-14 (10-11M) > MCH5-14 (2 × 10-10M). The melanosome aggregating activity of MCH could be completely reversed by a 100-fold higher concentration of ≺-MSH. MCH was self-antagonized in a dose-related manner by higher concentrations of the peptide as was the activity of the MCH1-14 fragment analog. The MCH activities of the MCH5-17 and MCH5-14 analogs were not compromised by even the highest concentrations of the peptides employed. The MSH-like activity of MCH appears to relate to the N-terminus of the peptide whereas MCH activity is more a function of the C-terminus of the hormone. Self- antagonism of MCH at high concentrations appears to relate to the N-terminal tetrapeptide, which is responsible for the intrinsic MSH-like activity of the hormone.

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JO - Life Sciences

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ER -

I. Melanin concentrating hormone exhibits both MSH and MCH activities on individual melanophores

Abstract

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