Isolation of Melanocyte-Stimulating Hormone From Hog Pituitary Gland

Lee, Teh H.; Lerner, Aaron B.

doi:10.1016/s0021-9258(18)65208-1

Cited by 106 publications

(5 citation statements)

References 20 publications

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“…For the NMR spectra of the entire Chemset 1, see the Supporting Information. 1 (d) Mtt Cleavage Protocol. 19 4-Methyltrityl group was removed by dipping lanterns for 2 min (several times) in a TFA/DCM (1/99 v/v) solution (18 equiv of TFA).…”

Section: Methodsmentioning

confidence: 99%

“…Supporting Information Available. 1 H-NMR spectra of Chemset 1 (PDF). This information is available free of charge via the Internet at http: //pubs.acs.org.…”

Section: Biological Evaluationmentioning

confidence: 99%

“…R-Melanocyte-stimulating Hormone (R-MSH) is a tridecapeptide (Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH 2 ) synthesized in pituitary 1 and skin. 2 This hormone binds to four melanocortin receptor subtypes.…”

Section: Introductionmentioning

confidence: 99%

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Parallel Synthesis of a Lipopeptide Library by Hydrazone-Based Chemical Ligation

et al. 2007

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alpha-Melanocyte-stimulating hormone (alpha-MSH) is an endogeneous linear tridecapeptide with potential application for the modulation of skin tanning. To evaluate the interest of introducing a lipid moiety onto this peptide, we developed an efficient chemoselective parallel method to prepare a large series of analogues of alpha-melanocortin with high purity, varying the nature or the relative position of the lipid moiety. Two sets of building blocks containing lipidic alpha-oxo-aldehydes or alpha-hydrazinoacetyl peptides were combined to obtain a 102-membered library of amphiphilic alpha-MSH analogues. This library was pharmacologically tested at 1 x 10(-7) M for the ability to induce AMPc production in M4Be melanoma cell line after stimulation of the human melanocortin MC1 receptor. Among theses lipopeptides, 84 compounds exhibited an AMPc induction higher than Melitane, a patented alpha-MSH agonist. These results provide strong evidence of the interest of introduction of a lipid tail for the pharmacomodulation of bioactive peptides.

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Section: Methodsmentioning

confidence: 99%

“…Supporting Information Available. 1 H-NMR spectra of Chemset 1 (PDF). This information is available free of charge via the Internet at http: //pubs.acs.org.…”

Section: Biological Evaluationmentioning

confidence: 99%

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Parallel Synthesis of a Lipopeptide Library by Hydrazone-Based Chemical Ligation

et al. 2007

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“…α-MSH (first termed simply MSH before the discovery of β- and γ-MSH) is a POMC-derived peptide, first found in the pituitaries and considered a pituitary hormone [[18]]. However, it was later found that α-MSH can be produced by many extra pituitary cells including monocytes, astrocytes, gastrointestinal cells, and keratinocytes [[19]] and was also found in many other sites within the CNS, such as the hypothalamus, thalamus, midbrain [[20]], brainstem [[4]], pineal gland, forebrain, diencephalon [[21]], and the limbic system [[22]], additionally abundant in the ARC and NTS [[21]].…”

Section: Production Release and Expression Of α-Mshmentioning

confidence: 99%

Alpha-Melanocyte-Stimulating Hormone-Mediated Appetite Regulation in the Central Nervous System

Wu¹,

Jing-mei²,

Hua³

et al. 2023

Neuroendocrinology

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Understanding the complex action mechanism of appetite regulation peptides can significantly impact therapeutic options in the treatment of obesity and other metabolic diseases. Hypothalamic α-melanocyte-stimulating hormone (α-MSH) is an anorexigenic peptide, closely related to the occurrence of obesity, playing a central role in food intake and energy expenditure. In the central nervous system (CNS), α-MSH is cleaved from proopiomelanocortin (POMC) and then released into different hypothalamic regions to act on melanocortin 3/4 receptor (MC3/4R)-expressing neurons, lowering food intake and raising energy expenditure via appetite suppression and sympathetic nervous system. Furthermore, it can increase the transmission of some anorexigenic hormones (e.g., dopamine) and interact with other orexigenic factors (e.g., agouti-related protein, neuropeptide Y) to influence food reward rather than merely feeding behavior. Therefore, α-MSH is a critical node of the hypothalamus in transmitting appetite suppression signals and is a key component of the central appetite-regulating circuits. Herein, we describe the role of α-MSH in appetite suppression in terms of specific receptors, effector neurons, sites of action, and the interaction with other appetite-relative peptides, respectively. We focus on the role of α-MSH in obesity. The status of research on α-MSH-related drugs is also discussed. With the intention of illuminating a new approach for targeting α-MSH in the hypothalamus as a strategy to manage obesity, we hope to further understand the direct or indirect mechanisms by which α-MSH exerts its appetite-regulating effects.

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“…Two of them are identified as -melanotropin and deacetylated -melanotropin. There are also two /3-melanotropins whose structures are identical with the bovine hor-Two melanocyte-stimulating hormones have been identified in extracts from the posterior-intermediate lobes of pituitary glands (Lee and Lerner, 1956), and are known as -MSH1 and /3-MSH. -MSH was first isolated by Lerner and Lee (1955) from the porcine pituitary and its primary structure subsequently determined by Harris and Lerner (1957; Harris, 1959a).…”

mentioning

confidence: 99%

Isolation, characterization, and amino acid sequence of melanotropins from camel pituitary glands

Li¹,

Danho²,

Chung³

et al. 1975

Biochemistry

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The isolation of two beta-melanotropins and two alpha-melanotropins from camel pituitary glands has been described, and their amino acid sequences have been determined. Two of them are identified as alpha-melanotropin and deacetylated alpha-melanotropin. There are also two beta-melanotropins whose structures are identical with the bovine hormone except that one has glycine in position 2 and the other glycine in position 2 as well as glutamine in position 8. The melanocyte-stimulating and lipolytic activities of these four camel melanotropins have been investigated by in vitro assay procedures.

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Isolation of Melanocyte-Stimulating Hormone From Hog Pituitary Gland

Cited by 106 publications

References 20 publications

Parallel Synthesis of a Lipopeptide Library by Hydrazone-Based Chemical Ligation

Parallel Synthesis of a Lipopeptide Library by Hydrazone-Based Chemical Ligation

Alpha-Melanocyte-Stimulating Hormone-Mediated Appetite Regulation in the Central Nervous System

Isolation, characterization, and amino acid sequence of melanotropins from camel pituitary glands

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