Differential structural requirements for the MSH and MCH activities of melanin concentrating hormone

Mac E. Hadley; Christian Zechel; Brain C. Wilkes; Ana M. Ana; Maria A. Visconti; Manuel Pozo-Alonso; Victor J. Hruby

doi:10.1016/0024-3205(87)90231-1

Differential structural requirements for the MSH and MCH activities of melanin concentrating hormone

Mac E. Hadley, Christian Zechel, Brain C. Wilkes, Ana M. Ana, Maria A. Visconti, Manuel Pozo-Alonso, Victor J. Hruby

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

22 Scopus citations

Abstract

{A figure is presented} melanin concentrating hormone (MCH), exhibits both melanin granule concentrating and dispersing (MSH-like) activities. Fragment analogues of MCH were synthesized as described herein and the melanotropic activities of the peptides were determined. In the frog (Rana pipiens) and lizard (Anolis carolinensis) skin bioassays, the 5-17 and 5-14 fragments of MCH were inactive (at concentrations of 10^-5M or less), whereas the 1-14 sequence exhibited minimal (about 10%) MSH-like activity compared to MCH, which, as reported previously, was about 600 times less active than α-MSH. In the teleost (fish) skin bioassay, the MCH_5-17 analogue was equipotent to MCH, whereas the 1-14 analogue was 10-30 times and the cyclic N- and C- terminal truncated analogue, MCH_5-14, was about 300 times less active than MCH. These results suggest that the N-terminal sequence is particularly critical to MSH-like activity in the tetrapod species studied, whereas other structural regions of MCH, particularly in the C-terminal, are more related to MCH activity in teleosts.

Original language	English (US)
Pages (from-to)	1139-1145
Number of pages	7
Journal	Life Sciences
Volume	40
Issue number	12
DOIs	https://doi.org/10.1016/0024-3205(87)90231-1
State	Published - Mar 23 1987
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
General Pharmacology, Toxicology and Pharmaceutics

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10.1016/0024-3205(87)90231-1

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title = "Differential structural requirements for the MSH and MCH activities of melanin concentrating hormone",

abstract = "{A figure is presented} melanin concentrating hormone (MCH), exhibits both melanin granule concentrating and dispersing (MSH-like) activities. Fragment analogues of MCH were synthesized as described herein and the melanotropic activities of the peptides were determined. In the frog (Rana pipiens) and lizard (Anolis carolinensis) skin bioassays, the 5-17 and 5-14 fragments of MCH were inactive (at concentrations of 10-5M or less), whereas the 1-14 sequence exhibited minimal (about 10%) MSH-like activity compared to MCH, which, as reported previously, was about 600 times less active than α-MSH. In the teleost (fish) skin bioassay, the MCH5-17 analogue was equipotent to MCH, whereas the 1-14 analogue was 10-30 times and the cyclic N- and C- terminal truncated analogue, MCH5-14, was about 300 times less active than MCH. These results suggest that the N-terminal sequence is particularly critical to MSH-like activity in the tetrapod species studied, whereas other structural regions of MCH, particularly in the C-terminal, are more related to MCH activity in teleosts.",

author = "Hadley, {Mac E.} and Christian Zechel and Wilkes, {Brain C.} and Ana, {Ana M.} and Visconti, {Maria A.} and Manuel Pozo-Alonso and Hruby, {Victor J.}",

note = "Funding Information: Supported in part hy U.S. Public Health Service grant AM17420 and by National Science Foundation grants PCM-8112200 and PCM-8412084. M.A. Visconti is a Fellow of Fundaczo de Amparo A Pesquisa do Estado de Sgo Paulo, Brazil, Grant 84/1263-O.",

year = "1987",

month = mar,

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doi = "10.1016/0024-3205(87)90231-1",

language = "English (US)",

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pages = "1139--1145",

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T1 - Differential structural requirements for the MSH and MCH activities of melanin concentrating hormone

AU - Hadley, Mac E.

AU - Zechel, Christian

AU - Wilkes, Brain C.

AU - Ana, Ana M.

AU - Visconti, Maria A.

AU - Pozo-Alonso, Manuel

AU - Hruby, Victor J.

N1 - Funding Information: Supported in part hy U.S. Public Health Service grant AM17420 and by National Science Foundation grants PCM-8112200 and PCM-8412084. M.A. Visconti is a Fellow of Fundaczo de Amparo A Pesquisa do Estado de Sgo Paulo, Brazil, Grant 84/1263-O.

PY - 1987/3/23

Y1 - 1987/3/23

N2 - {A figure is presented} melanin concentrating hormone (MCH), exhibits both melanin granule concentrating and dispersing (MSH-like) activities. Fragment analogues of MCH were synthesized as described herein and the melanotropic activities of the peptides were determined. In the frog (Rana pipiens) and lizard (Anolis carolinensis) skin bioassays, the 5-17 and 5-14 fragments of MCH were inactive (at concentrations of 10-5M or less), whereas the 1-14 sequence exhibited minimal (about 10%) MSH-like activity compared to MCH, which, as reported previously, was about 600 times less active than α-MSH. In the teleost (fish) skin bioassay, the MCH5-17 analogue was equipotent to MCH, whereas the 1-14 analogue was 10-30 times and the cyclic N- and C- terminal truncated analogue, MCH5-14, was about 300 times less active than MCH. These results suggest that the N-terminal sequence is particularly critical to MSH-like activity in the tetrapod species studied, whereas other structural regions of MCH, particularly in the C-terminal, are more related to MCH activity in teleosts.

AB - {A figure is presented} melanin concentrating hormone (MCH), exhibits both melanin granule concentrating and dispersing (MSH-like) activities. Fragment analogues of MCH were synthesized as described herein and the melanotropic activities of the peptides were determined. In the frog (Rana pipiens) and lizard (Anolis carolinensis) skin bioassays, the 5-17 and 5-14 fragments of MCH were inactive (at concentrations of 10-5M or less), whereas the 1-14 sequence exhibited minimal (about 10%) MSH-like activity compared to MCH, which, as reported previously, was about 600 times less active than α-MSH. In the teleost (fish) skin bioassay, the MCH5-17 analogue was equipotent to MCH, whereas the 1-14 analogue was 10-30 times and the cyclic N- and C- terminal truncated analogue, MCH5-14, was about 300 times less active than MCH. These results suggest that the N-terminal sequence is particularly critical to MSH-like activity in the tetrapod species studied, whereas other structural regions of MCH, particularly in the C-terminal, are more related to MCH activity in teleosts.

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JO - Life Sciences

JF - Life Sciences

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Differential structural requirements for the MSH and MCH activities of melanin concentrating hormone

Abstract

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