Amino acid sequence of porcine β-lipotropic hormone

Gráf, László; Barát, Erzsébet; Cseh, G; Sajgó, M

doi:10.1016/0005-2795(71)90344-8

Cited by 68 publications

(9 citation statements)

References 8 publications

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“…p-~m d ?-LPM in diflerent species-We, like others, have isolated and characterized /3-EPH from porcine and human pituitaries (27)(28)(29)(30)(31)(32)(33)(34) and were able to establish that the homologous peptides occur in the two species. It has also been found in bovine pituitaries (35).…”

Section: Ianh~duetionmentioning

confidence: 93%

From β-lipotropin to β-endorphin and 'pro-opio-melanocortin'

Chrétien¹,

Benjannet²,

Gossard³

et al. 1979

Can. J. Biochem.

149

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Studies on the biosynthesis of beta-LPH on the one hand, and of ACTH on the other, have produced a new concept, that of a single precursor form which contains three active molecules. Thus, it is proper to name such a precursor 'pro-opio-melanocortin.' The concept that beta-LPH was a precursor molecule was first put forward in 1967 and was based on both structural forms and biological activities. The discovery that morphine-like substances are part of the C-terminal fragment of beta-LPH brought an additional important biological side product. That, together with the recent demonstration of ACTH as part of a still larger precursor, constitutes an exciting model for the study of peptide hormone biosynthesis. We have shown unambiguously that beta-endorphin is the result of a maturation process from the large precursor, while beta-LPH is an important and transient intermediary. Since it is also present in the brain, our recent results using pars intermedia cells can be applied to study the fabrication and degradation of these molecules in the brain. We expect to see it established that all other neuropeptides are also biosynthesized as larger precursor molecules whose structure at the site of cleavage could well be constituted of two basic amino acids like in the pro-opio-melanocortin.

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Section: Ianh~duetionmentioning

confidence: 93%

From β-lipotropin to β-endorphin and 'pro-opio-melanocortin'

Chrétien¹,

Benjannet²,

Gossard³

et al. 1979

Can. J. Biochem.

149

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“…Several lines of evidence suggest that side product peptides created at the maturation of precursor proteins have biological activities that are distinct from those of peptides presumed to be the main active components. For example, multiple bioactive peptides including adrenocorticotropin (ACTH),6 α‐melanocyte stimulating hormone (α‐MSH),7 β‐endorphin (β‐END),8 and β‐lipotropin (β‐LPH),8 which induce cortisol and androgen release, melanin production, opiate function, and lipolysis, respectively, are produced from a common precursor protein, preproopiomelanocortin by cleavages by prohormone convertases 1 and 2 (Figure 1B) 9–11. Similarly, substance P12 and neurokinin A,13 which are considered to be neurotransmitters of primary sensory neurons are both produced from β‐preprotachykinin A14, 15 and hypotensive neurotensin16 and contractile neuromedin N17 are both produced from the neurotensin/neuromedin N precursor 18.…”

Section: Possible Production Of Multiple Bioactive Peptides During Mamentioning

confidence: 99%

Cryptides: Functional cryptic peptides hidden in protein structures

et al. 2007

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Peptidergic hormones, neurotransmitters, and neuromodulators are extracellular signaling molecules that play central roles in physiological signal transmissions between various cells, tissues, and organs. These factors are primarily translated as inactive precursor proteins according to the genetic information. These precursor proteins are then cleaved by various proteases including signal peptidases and processing enzymes to produce matured bioactive factors. During these processes, various fragmented peptides are also produced from the same precursor proteins. Such fragmented peptides may have various unexpected biological activities that have not been identified yet because these peptides are considered to be produced and released along with mature factors at the same secretary pathways. Recently, we found that various fragmented peptides of mitochondrial proteins that are produced during the maturation processes, such as fragments of cytochrome c oxidase, activate neutrophils whose functions are distinct from their parent proteins. These findings suggest the existence of many different functional peptides whose functions have not been identified yet. These unidentified peptides may play a variety of roles in various regulatory mechanisms, and therefore, they are expected to provide novel regulatory and signaling mechanisms, "Peptide World".

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“…When the sequence is compared with known structures of other adenohypophyseal hormones (13), it is found that N-C has the same sequence of the COOH-terminal '31 aminoacid residues in the ovine fl-lipotropin molecule (2-4). It may be noted that the COOH-terminal sequences of porcine (14)(15)(16), bovine (17), and human ,B-lipotropin (18) are identical to that of the ovine hormone, except for Val-83 in porcine and Tyr-87 and Glu-91 in the human hormone.…”

Section: Figurementioning

confidence: 99%

Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.

Li¹,

Chung²

1976

Proc. Natl. Acad. Sci. U.S.A.

544

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The isolation of an untriakontapeptide from camel pituitary extracts has been described. Its structure has been determined and shown to be identical to the sequence of carboxyl-terminal 31 amino acids of ovine f-lipotropin.The peptide possesses very low lipotropic activity but significant opiate activity.During the course of isolation of melanotropins from camel pituitary glands (1), we obtained an untriakontapeptide that has an amino-acid sequence identical to the COOH-terminal 31 residues of ovine fl-lipotropin (2-4). This peptide was found to possess opiate activity. This article describes the isolation, amino-acid sequence, and biological activity of the untriakontapeptide. EXPERIMENTALThe starting material was component N, which was obtained by chromatography of fraction D on a carboxymethyl-cellulose column (1). Fraction D was prepared from acid acetone extracts of whole camel (Camelus dromedarius) pituitaries. Component N was purified further by gel filtration on Sephadex G-25 (fine), followed by electrophoresis on Whatman no. 3 MM paper in pyridine-HOAc buffer, pH 3.7 (pyridine-HOAc-H20, 4:40:1150 vol/vol) for 2 hr at 400 V.Trypsin was obtained from Calbiochem and subtilisin from Sigma. Digestions were performed with 1 mg of peptide and 0.02 mg of trypsin or 0.05 mg of subtilisin in 0.2 M NH4OAc, pH 8.0, at 370 for 8 hr for trypsin and 1 hr for subtilisin. The digests were mapped by paper chromatography (butanol-HOAc-H20, 4:1:5 vol/vol) and subsequent high voltage electrophoresis at pH 2.0 [HCOOH (88%)-HOAc-H20, 218:63:719 vol/vol] for 1.5 hr at 2000 V. Maps were sprayed with 1% ninhydrin in ethanol solution and allowed to develop in the dark for 20 hr; the spots were cut out and material was eluted with 0

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Amino acid sequence of porcine β-lipotropic hormone

Cited by 68 publications

References 8 publications

From β-lipotropin to β-endorphin and 'pro-opio-melanocortin'

From β-lipotropin to β-endorphin and 'pro-opio-melanocortin'

Cryptides: Functional cryptic peptides hidden in protein structures

Isolation and structure of an untriakontapeptide with opiate activity from camel pituitary glands.

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