Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P01189 (beta-endorphin)
 21,003 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The pituitary glands of two urodelan species (Mertensiella caucasica, Triturus cristatus) and one one caecilian species (Chthonerpeton indistinctum) were examined with histological (Alcian blue, Brookes' trichrome stain), enzyme histochemical (acid phosphatase, alpha-naphthylacetate-esterase, acetylcholinesterase) and immunofluorescence techniques (anti-carp GTH, anti-ovine prolactin, anti-synthetic alpha-MSH). In the pituitary gland of Mertensiella and Triturus six chromophilic cell types could be distinguished. A strong fluorescence was observed in the MSH-, GTH- and TSH-cells. In the pituitary gland of Chthonerpeton only five chromophilic cell types could be distinguished: in the rostral part of the pituitary gland the B3-cell; in the basal region of the central area the B2-cell; dorsocaudally the B1-cell. The acidophilic cells were found in the central and caudal part of the pars distalis. The basophils of the pars intermedia could be observed in the dorsocaudal part of the pituitary gland surrounding the neurohypophysis. All acidophilic cells showed a strong immunofluorescence with anti-ovine prolactin (LTH).
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PMID:Histological, immuno- and enzyme-histochemical investigations on the adenohypophysis of the urodeles, Mertensiella caucasica and Triturus cristatus and the caecilian, Chthonerpeton indistinctum. 34 44

Immunocytochemistry on frozen sections revealed that in both the trout and the carp, parvocellular neurones located in the medial basal hypothalamus (medial nucleus lateralis tuberis) were immunostained by antisera against three molecules known to be derived from the proopiomelanocortin (POMC) molecule, viz: alpha-melanocyte-stimulating hormone (alpha MSH), ACTH, and salmonid NPP--the whole N-terminal sequence preceding ACTH in the POMC precursor. Axons from these neurones extended into various regions of the brain but did not appear to project into the pituitary gland. Antiserum against salmonid melanin-concentrating hormone (MCH) immunostained magnocellular neurones in the lateral basal hypothalamus (lateral nucleus lateralis tuberis). Axons from some of these neurones projected into the brain while other axons extended into the pituitary gland. In the carp, but not in the trout, some MCH neurones were also immunostained by antisera against alpha MSH but not by antisera against the other POMC molecules.
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PMID:Immunocytochemical demonstration of melanin-concentrating hormone and proopiomelanocortin-like products in the brain of the trout and carp. 266 29

The existence of melanocyte-stimulating hormone (MSH) in fish brains was investigated by a range of techniques: radioimmunoassay, HPLC, bioassay, and immunocytochemistry. Immunoreactive alpha MSH (ir alpha MSH) was detected by radioimmunoassay in all regions of carp and trout brains, with the highest concentration in the basal hypothalamus. In trout, ir alpha MSH cell bodies were located by immunocytochemistry only periventricularly, in the medial basal hypothalamus near the third ventricle, whereas in the carp ir alpha MSH staining was seen both in periventricular cells and also in some of the magnocellular neurones in the lateral hypothalamus. When white-adapted fish were transferred to a black tank for 6 days, the melanin-concentrating hormone (MCH) content of the basal hypothalamus of both carp and trout increased 2- and 4.6-fold, respectively, but the alpha MSH content did not change in either species. Analysis by HPLC of pituitary gland, hypothalamic, and optic tectal extracts revealed that the pituitary contains desacetyl, monoacetyl, and diacetyl alpha MSH, although the ratio of these forms differed in the two species. The hypothalamus and optic tectum, however, contained predominantly the desacetyl form of alpha MSH. Bioassays for MSH in the HPLC fractions revealed the existence of presumptive beta MSH in both the pituitary and hypothalamus. An argument is advanced that the periventricular ir alpha MSH neurones are homologous with the proopiomelanocortin cells of the arcuate nucleus in mammals, and that the immunocytochemical alpha MSH-like activity in the MCH neurones may not be authentic alpha MSH.
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PMID:Localisation and identification of melanocyte-stimulating hormones in the fish brain. 320 71

The primary structure of the precursor of urotensin I, a neuropeptide hormone from the caudal neurosecretory system of the carp Cyprinus carpio, has been determined by analyzing the nucleotide sequence of cloned DNA complementary to the mRNA encoding it. The precursor consists of 145 amino acid residues and the carboxyl terminus represents the 41-amino acid sequence of urotensin I, preceded by Lys-Arg and followed by Gly-Lys. Sequence homology as well as similar organization of the precursors of urotensin I and mammalian corticotropin-releasing factors suggest that they are evolutionarily related. RNA transfer blot analysis indicates that mRNA encoding the precursor of urotensin I is present only in the spinal cord and not in the brain, intestine, liver, or kidney of the carp.
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PMID:Cloning and sequence analysis of cDNA encoding urotensin I precursor. 348 50

Using immunocytochemical methods at the electron microscope level, immunoreactivity for both melanin-concentrating hormone (MCH) and alpha-melanocyte-stimulating hormone (alpha-MSH) has been demonstrated in the carp neurohypophysis. A double-labelling technique, using colloidal gold probes of different sizes showed that immunoreactivity to both molecules coexists within the same neurosecretory granules in some neurones, while in other neurones the granules exhibit only MCH-like immunoreactivity. These observations suggest that the two immunoreactivities are attributable to separate molecules; if they are derived from the same precursor molecule, then this must be cleaved differently in the two sets of neurones. The absence of adrenocorticotropic hormone (ACTH)-like immunostaining in any neurosecretory granule might suggest the alpha-MSH-like molecule is not derived from the conventional pro-opiomelanocortin precursor.
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PMID:Ultrastructural demonstration that melanin-concentrating hormone-like and alpha-melanocyte-stimulating hormone-like immunoreactive molecules coexist in the same neurosecretory granules. 368 83

Highly purified synthetic salmonid melanin concentrating hormone (MCH) and some analogs were investigated for their ability to concentrate the pigment in scale melanophores of the Chinese grass carp, Ctenopharyngodon idellus, to produce melanin dispersion in frog or lizard melanophores and to inhibit alpha-MSH in its action on mouse melanoma and rat adrenal glomerulosa cells in vitro. In the grass carp, MCH produced half-maximal pigment aggregation at 6 X 10(-11) M and its oxidized form at 7 X 10(-11) M. Replacement of the two methionines at position 3 and 6 with norvaline lowered the potency by a factor of 2.7 and with propargylglycine by a factor of about 7. Linear, Cys5,14-Acm-protected MCH was a full agonist of MCH but with a 345-fold lower potency. Iodinated MCH showed similar, low activity. In tetrapods, salmonid MCH and its analogs displayed only marginal pigment dispersion at concentrations greater than 10(-5) M. Alkali-treatment of MCH increased the pigment-dispersing potency by a factor of about 30 whereas the activity for pigment aggregation in the grass carp was destroyed. At high concentrations (10(-6), 10(-5) M) MCH also stimulated tyrosinase activity in B-16 mouse melanoma cells but did not modify the effects of alpha-MSH in this system. By contrast, when tested on rat adrenal glomerulosa cells, salmonid MCH had no effect alone but at a concentration of greater than 10(-10) M it slightly reduced corticosterone production by an alpha-MSH concentration of 10(-7) M. Aldosterone production was not affected and MCH did not influence the response to ACTH.
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PMID:Effect of melanin concentrating hormone on pigment and adrenal cells in vitro. 393 41

The effects of vasoactive intestinal peptide (VIP) and several other peptides have been examined on cyclic AMP accumulation in intact pieces and isolated horizontal cells of the teleost (carp) retina. VIP was the most effective peptide examined, inducing a dose-related response, and an approximately fivefold increase in cyclic AMP production when used at a concentration of 10 microM. Porcine histidine isoleucine-containing peptide and secretin, peptides structurally related to VIP, also stimulated cyclic AMP accumulation, but at concentrations of 10 microM induced responses which were only approximately 40% and 10%, respectively, of the response observed with 10 microM VIP. In contrast, several other peptides, including glucagon, neurotensin, somatostatin, luteinizing hormone-releasing hormone, alpha-melanocyte-stimulating hormone, cholecystokinin octapeptide26-33, gastrin-releasing peptide, thyrotropin-releasing hormone, and VIP10-28 were totally inactive. The response to 10 microM VIP was not antagonized by several dopamine antagonists, indicating the presence of a population of specific VIP receptors coupled to adenylate cyclase, distinct from the population of dopamine receptors coupled to adenylate cyclase also known to be present in this tissue. Finally, experiments involving the use of fractions of isolated horizontal cells indicate that these neurons possess a population of VIP receptors coupled to cyclic AMP production which would appear to share a common pool of adenylate cyclase with a population of similarly coupled dopamine receptors.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effects of vasoactive intestinal peptide and other peptides on cyclic AMP accumulation in intact pieces and isolated horizontal cells of the teleost retina. 619 61

Urotensin I (UI), a 41-residue mammalian hypotensive and fish or mammalian corticotropin-releasing peptide, isolated from 0.1 N HCI extracts of urophyses of the carp (Cyprinus carpio) was purified and the amino acid sequence was determined to be: H-Asn-Asp-Asp-Pro-Pro-Ile-Ser-Ile-Asp-Leu-Thr-Phe-His-Leu-Leu- Arg-Asn-Met-Ile-Glu-Met-Ala-Arg-Asn-Glu-Asn-Gln-Arg-Glu-Gln-Ala-Gly-Leu-Asn-Arg-Lys-Tyr-Leu-Asp-Glu-Val-NH2. When the extraction procedure included heating at 100 degrees C for 15 min, UI was cleaved at a highly acid labile Asp-Pro bond to give the fully active UI (4-41). Urotensin I shows close structural and biological homology with the recently isolated ovine hypothalamic corticotropin-releasing factor (CRF) and the frog skin peptide sauvagine and thus may be considered an evolutionary prototype of unique mammalian-hypotensive and vertebrate corticotropin-releasing factors.
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PMID:Isolation and amino acid sequence of urotensin I, a vasoactive and ACTH-releasing neuropeptide, from the carp (Cyprinus carpio) urophysis. 675 95

The potencies of the corticotropin-releasing hormone (CRH) agonistic peptides oCRH, h/rCRH, frog sauvagine, and carp urotensin I and of the antagonistic peptide alpha-helical CRH9-41 were compared in 3 different in vitro assays: (a) receptor binding to rat brain membranes; (b) release of ACTH/beta-endorphin from rat pituitary cells; and (c) relaxation of rat mesenteric small arteries. From their potency profiles, especially from the high potency of sauvagine relative to CRH in the relaxation assay, it is concluded that the receptors mediating the hypotensive action of systemic CRH in vascular smooth muscle are different from those in the pituitary and brain, and may be identical or very similar to the recently cloned new CRH receptor type 2.
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PMID:Corticotropin-releasing hormone (CRH) receptors in the mesenteric small arteries of rats resemble the (2)-subtype. 878 99

Adrenocorticotropic hormone (ACTH)-releasing activity of synthetic carp Urotensin I (UI) and its ten synthetic fragments were examined using cultured rat pituitary cells. Both UI(1-41) and rat CRF (rCRF) increased ACTH release in a similar fashion at a concentration range from 10 pM to 100 nM. The potency of UI(1-41) was about one seventh that of rCRF on a molar basis. Four of ten UI fragments, UI(1-36), UI(4-36), UI(6-36) and UI(1-19) showed relatively strong ACTH-releasing activity, whereas both UI(9-36) and UI(17-36) showed extremely weak ACTH-releasing activity. However, all these fragments showed the activity in a dose-dependent manner parallel with that of UI(1-41). The activity of UI(1-36) was weaker than UI(1-41), suggesting that the C-terminal 37-41 sequence is required to express the full ACTH-release activity, although each of four C-terminal fragments, UI(24-36), UI(24-41), UI(29-36) and UI(29-41), exhibited no activity. In summary, the 4-19 amino acid sequence of UI(is important to exhibit ACTH-releasing activity and the C-terminal 37-41 sequence will be necessary to express the full activity.
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PMID:Adrenocorticotropic hormone-releasing activity of urotensin I and its fragments in vitro. 930 81


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