Isolation and primary structure of β-endorphin and β-lipotropin from bovine pituitary glands

Li, Choh Hao; Tan, Liat; Chung, David

doi:10.1016/s0006-291x(77)80090-9

Cited by 53 publications

(10 citation statements)

References 16 publications

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“…Li et al (97,106) almost simultaneously confirmed our results for human betaendorphin and also isolated beta-endorphin from bovine pituitary tissue (107). Figure 3 gives a summary of the various endorphins isolated and completely characterized.…”

Section: Endorphins and Lipotropinssupporting

confidence: 80%

Chemistry and biosynthesis of pro-opiomelanocortin

Chrétien

Seidah

1981

Mol Cell Biochem

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Studies of lipotropins, melanotropins and endorphins on one hand, and of adrenocorticotropin on the other, has given rise to the concept of a multipotent precursor molecule recently renamed proopiomelanocortin. The preferential sites of cleavage of the precursor to produce its biologically active components are made of pairs of basic amino acid residues as described for the biosynthesis of beta-MSH and pro-insulin. Such structural feature is also found in other pro-hormone molecules. Pulse chase experiments and secretory studies carried out in both anterior and intermediate lobes of rat pituitary glands revealed the transformation of different forms of the precursor into different end-products, the anterior lobe producing preferentially ACTH and beta-LPH while the intermediate produces mainly the alpha-MSH and beta-endorphin. The multiple forms of precursors seem to differ in their carbohydrate content although at least two different gene products are still possible. The presence of similar peptides in the hypothalamus makes it highly probable that neuropeptides are biosynthesized with similar process. Thus the model of beta-LPH precursor, proposed as early as in 1967, is now applicable to the biosynthesis of all other neuropeptides. Major advances in this field are expected in the 1980s.

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Section: Endorphins and Lipotropinssupporting

confidence: 80%

Chemistry and biosynthesis of pro-opiomelanocortin

Chrétien

Seidah

1981

Mol Cell Biochem

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“…Since the discovery of the enkephalins (Hughes et al, 1975), the system of the endogenous opioid peptides has become more complicated by the characterization of many related opioid peptides. Each newly discovered peptide contains the amino acid sequence of either methionine-enkephalin (M-Enk) or leucine-enkephalin (L-Enk) (Li et al, 1977;Goldstein et al, 1979;Stern et al, 1979;Kangawa et al, 1981;Kilpatrick et al, 1981;Tachibana et al, 1982). Figure 1 shows the amino acid sequence of some of these peptides.…”

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confidence: 99%

Regional Distribution of Methionine‐Enkephalin‐Arg⁶‐Phe⁷ in the Rat Brain: Comparative Study with the Distribution of Other Opioid Peptides

Giraud¹,

Castanas

Patey

et al. 1983

Journal of Neurochemistry

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The distribution of the opioid peptide methionine-enkephalin-arginine6-phenylalanine7 (M-Enk-Arg6-Phe7) has been investigated in various structures of the rat brain by using a highly specific radioimmunoassay (RIA). Immunoreactive M-Enk-Arg6-Phe7 has been further characterized by high performance liquid chromatography. The levels of M-Enk-Arg6-Phe7 in various structures of the rat brain were compared with the levels of several other opioid peptides, including methionine-enkephalin (M-Enk), leucine-enkephalin (L-Enk), dynorphin 1-13, and alpha-neoendorphin, which were also measured by RIA. There was a close relationship between the distribution of M-Enk-Arg6-Phe7 immunoreactive material (ir), M-Enk ir, and L-Enk ir. The distribution of dynorphin 1-13 ir and alpha-neoendorphin ir appeared to be distinct from that of the enkephalin group. These results are in agreement with recent reports on the cloning and sequencing of the c-DNA coding for the prohormones, in which it has been hypothesized that M-Enk-Arg6-Phe7 and M-Enk are synthesized by the same precursor, called proenkephalin, and that dynorphin-related peptides and alpha-neoendorphin arise from a separate precursor, prodynorphin.

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“…1 and 2), share common NH2-terminal sequences with the COOH-terminal fragment of f3-lipotropin (,B-LPH) (3-7). The 31-amino acid COOH-terminal peptide of ,B-LPH, termed fl-endorphin (8), is an extremely potent opioid agonist (8-11). f3-Endorphin was isolated and purified from extracts of ovine and procine pituitary (3,4) as was a-endorphin [,B-LPH 61-76 (6)] and y-endorphin [fl-LPH 61-77 (7)]. Specific COOH-terminally directed antisera raised against synthetic fl-endorphin and a-endorphin have permitted selective radioimmunoassays for these peptides, which do not read enkephalin pentapeptides (12,13).…”

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confidence: 99%

“…This added myelinated fiber immunoreactivity was totally abolished by preincubation of this antiserum product with well-purified myelin basic protein (1 mg/ml; supplied by F. Westall and J. Salk). After preabsorption of this antiserum with f(-endorphin (1)(2)(3)(4)(5)(6)(7)(8)(9)(10) lOm), all reactivity (i.e., cell bodies, cell processes, and myelinated axons) was completely suppressed. When the antiserum product was absorbed only with myelin basic protein, the same immunoreactive cell bodies and processes could be detected as with RB 100-10/27.…”

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confidence: 99%

Neurons containing beta-endorphin in rat brain exist separately from those containing enkephalin: immunocytochemical studies.

Fe¹,

Battenberg²,

Rossier³

et al. 1978

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

510

139

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Well-characterized antisera to porcine #l-endorphin were used to localize immunoreactive sites in cryostat sections of formaldehyde-fixed rat brain by indirect immunohistochemistry. Specificity was established by absorption of immune sera with synthetic peptide fragments. Specific immunoreactivity was localized to neuronal perikarya in the basal tuberal hypothalamus, and to varicose nerve fibers which were distributed to midline nuclear areas throughout the diencephalon and anterior pons. These patterns of reactivity were unaffected by preabsorption of the immune sera with millimolar concentrations of f3-Endorphin was isolated and purified from extracts of ovine and procine pituitary (3, 4) as was a-endorphin [, (6)] and y-endorphin (7)]. Specific COOH-terminally directed antisera raised against synthetic fl-endorphin and a-endorphin have permitted selective radioimmunoassays for these peptides, which do not read enkephalin pentapeptides (12, 13). These immune antisera have already been used to reveal the immunocytochemical location of a-endorphin-and f3-endorphin-reactive cells in the rat intermediate lobe andBy radioimmunoassay, rat brain contains significant amounts of ,B-endorphin (15), and these levels are unchanged at 6-9 months after hypophysectomy (15). The regional distribution of f,-endorphin in rat brain shows no fixed relationship to radioimmunoassayable enkephalins (15), and many areas reported to be rich in enkephalin immunoreactivity (16)(17)(18)(19)(20)(21)(22) are devoid of detectable f3-endorphin. We now report that immunocytochemical localization studies reveal f3-endorphincontaining neuronal perikarya and fiber tracts throughout the diencephalon that can be clearly distinguished cytologically and immunologically from those cells and fibers observed by us and reported by others (16-23) to be enkephalin-containing neurons.The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact. 1591MATERIALS AND METHODS Antiserum Preparation and Characterization. As described in greater detail elsewhere (12, 13) antisera were raised in rabbits to synthetic f-endorphin that had been coupled to bovine serum albumin with bis-diazotized benzidine. The antisera used here for cellular localization of ,B-endorphin immunoreactivity were those used by us for the radioimmunoassay procedures already described (12,13,15). The majority of immunocytochemical results reported here were obtained with antiserum RB 100-10/27; this antiserum recognizes a segment of the COOH-terminal portion of p3-endorphin between asparagine-20 and histidine-27 (12). RB 100-10/27 does not recognize either enkephalin pentapeptide or a-or y-endorphin, but it shows parallel competition for binding of ovine f,-LPH and f3-endorphin. Similarly, this antiserum also shows parallel displacement for binding of ,B-endorphin with the purified 31,000 molecular weight precursor peptide...

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Isolation and primary structure of β-endorphin and β-lipotropin from bovine pituitary glands

Cited by 53 publications

References 16 publications

Chemistry and biosynthesis of pro-opiomelanocortin

Chemistry and biosynthesis of pro-opiomelanocortin

Regional Distribution of Methionine‐Enkephalin‐Arg⁶‐Phe⁷ in the Rat Brain: Comparative Study with the Distribution of Other Opioid Peptides

Neurons containing beta-endorphin in rat brain exist separately from those containing enkephalin: immunocytochemical studies.

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Isolation and primary structure of β-endorphin and β-lipotropin from bovine pituitary glands

Cited by 53 publications

References 16 publications

Chemistry and biosynthesis of pro-opiomelanocortin

Chemistry and biosynthesis of pro-opiomelanocortin

Regional Distribution of Methionine‐Enkephalin‐Arg6‐Phe7 in the Rat Brain: Comparative Study with the Distribution of Other Opioid Peptides

Neurons containing beta-endorphin in rat brain exist separately from those containing enkephalin: immunocytochemical studies.

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Regional Distribution of Methionine‐Enkephalin‐Arg⁶‐Phe⁷ in the Rat Brain: Comparative Study with the Distribution of Other Opioid Peptides