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)

We surveyed retinas of Raja erinacea, Mustelus canis, and Squalus acanthias for neurotransmitter substances by using antisera directed against the substances themselves or against their synthesizing enzymes. Both the peroxidase-antiperoxidase (PAP) and indirect fluorescent techniques were employed to visualize the primary antisera. In all three species positive results were obtained with antisera directed against tyrosine hydroxylase (TOH), glutamic acid decarboxylase (GAD), serotonin (5-HT), and leucine enkephalin (Lenk). Antisera directed against glucagon, neurotensin, beta-endorphin, vasoactive intestinal peptide, or bombesin failed to show any specific staining. Immunoreactivity was located in amacrine, interplexiform, and horizontal cells as well as in axons of the optic fiber layer. The four antisera labelled different amacrine cell classes, distinguished on the bases of perikaryal morphology and the distribution of cell processes in the inner plexiform layer (IPL). Amacrine cells that labelled with the same marker were seen to have different morphologies in the species studied. Thus, TOH-like immunoreactivity was distributed in layers 1, 3, and 5 of the IPL in Mustelus but only in layers 1 and 3 in Raja retina. GAD-like immunoreactivity was found diffusely over all layers of the IPL in Raja, but in Mustelus it was confined primarily to layers 1, 3, and 5 of the IPL. Lenk- and 5-HT-like immunoreactivities showed similar species variations. Two neurochemical classes of interplexiform cell were identified in this study. In Mustelus GAD-like and Lenk-like immunoreactive interplexiform cells were seen whereas in Raja only GAD-positive interplexiform cells were detected. In squalus no unequivocal demonstration of any interplexiform cell was made with these antisera. The GAD antiserum also labelled a subset of the horizontal cells in the dorsal retina of Raja. TOH and 5-HT-antisera labelled axons in the optic fiber layer of all three species but reactive ganglion cell perikarya were not identified.
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PMID:Retinal neurochemistry of three elasmobranch species: an immunohistochemical approach. 286 65

Recent studies suggest that neurons containing adrenocorticotropin and catecholamines are localized to similar areas of the brain. In this immunocytochemical study, the distributions of neurons and terminals containing adrenocorticotropin and tyrosine hydroxylase, the first enzyme in the catecholamine biosynthetic pathway, were compared using the peroxidase-antiperoxidase technique. Neurons containing adrenocorticotropin and tyrosine hydroxylase formed overlapping hyperbolic lamina in the mediobasal hypothalamus. Although adrenocorticotropin and tyrosine hydroxylase containing neurons often formed small clusters, no double labeled cells were observed. Overlap also occurred between adrenocorticotropin and tyrosine hydroxylase terminal fields in several diencephalic nuclei including the periventricular hypothalamic gray and paraventricular thalamus. In contrast, other regions displayed striking compartmentalization of terminal fields; for example, in both the paraventricular hypothalamus and central nucleus of the amygdala, adrenocorticotropin was located in ventral and tyrosine hydroxylase in more dorsal aspects of the nuclei. Adjacent sections also showed a close correspondence between adrenocorticotropin terminals and tyrosine hydroxylase cell bodies in paraventricular, periventricular, dorsomedial and ventral hypothalamic nuclei. These data provide anatomical substrates for potential functional interactions between catecholamine and adrenocorticotropin systems in forebrain.
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PMID:Anatomical evidence for interactions between catecholamine- and adrenocorticotropin-containing neurons. 287 20

The distribution of arginine-vasopressin (AVP)-, oxytocin-, beta-endorphin (beta-EP)- and dynorphin-immunoreactive cells was examined by peroxidase-antiperoxidase (PAP) immunocytochemistry in the ovaries of Brattleboro and Long-Evans (LE) rats. The ovarian distribution of the peptide-immunoreactivity is indistinguishable between the two strains. AVP- and beta-EP-immunoreactivity is co-localized in the majority of luteal cells, and in some cells scattered in the interstitial tissue. Of the AVP/beta-EP-positive cells, 1-2% also contained immunoreactive (ir)-dynorphin. Some cells in the interstitium contained only ir-AVP (approximately 50%) or only ir-dynorphin (approximately 5%); in the corpora lutea, however, no luteal cells appeared to contain only one peptide. AVP-immunoreactivity is also present in theca cells surrounding secondary and large, antral follicles; ir-oxytocin was not observed in any ovarian cell type in the rat. These data suggest that most luteal, and some interstitial, cells in the ovary have the capacity to produce and store up to three different neuropeptides.
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PMID:Co-expression of vasopressin with beta-endorphin and dynorphin in individual cells from the ovaries of Brattleboro and Long-Evans rats: immunocytochemical studies. 287 49

Beta-endorphin (beta-EP) immunostainable cells were demonstrated in human ovarian tissue using a non-cross-reacting anti-beta-EP serum and the avidin-biotin-peroxidase detection technique. In ovaries from ovulating and premenopausal women, beta-EP immunoreactivity was localized in the luteinized cells of theca interna of maturing follicles with almost negligible staining in granulosa cells; cells of primary follicles did not stain. In corpora lutea, luteinized cells in both theca interna and granulosa, layers were equally positive. In postmenopausal ovaries, staining was detectable only in scattered luteinized stromal cells. This is the first report on the presence of immunoreactive beta-EP in human ovaries, in which beta-EP seems to be produced by the same sex cord cells engaged in active steroidogenesis and may be under gonadotropin central regulation. The significance of this finding is discussed.
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PMID:Immunoreactive beta-endorphin in human ovaries. 293 58

Ovaries from pregnant and postpartum Sprague-Dawley rats were examined for content of immunoreactive beta-endorphin by radioimmunoassay, and for its localization by the peroxidase-antiperoxidase technique. In addition, the molecular forms of beta-endorphin immunoreactivity were separated by gel chromatography and reverse-phase high performance liquid chromatography (RP-HPLC). Ovaries from rats early in pregnancy showed intense granular cytoplasmic staining of luteal cells, with an even distribution of granular material throughout the cytoplasm. By middle to late pregnancy the staining pattern was changed, with immunoreactive material showing a less granular and unevenly distributed staining pattern and with some areas of the cytoplasm totally devoid of immunoreactive material. The concentrations of immunoreactive beta-endorphin measured during pregnancy were significantly lower than levels in mature non-pregnant rat ovary. The ovarian concentration of immunoreactive beta-endorphin fell progressively during pregnancy and early lactation, returning to normal cyclic rat levels at 20 days post partum. The ovarian concentration of beta-endorphin-like material was lowest at 6 days post partum (0.53 +/- 0.08 ng/g wet weight; mean +/- S.E.M.), representing approximately 10% of the concentration found in pooled ovaries from randomly cyclic adult rats. Gel chromatography revealed only a single peak of immunoreactive beta-endorphin, co-eluting with 3.5 kD molecular weight ovine beta-endorphin (1-31). This contrasts with gel profiles of adult cyclic rat ovary, where large molecular weight species pro-opiomelanocortin (31 kD) and beta-lipotrophin (11.5 kD) are also present. On RP-HPLC the predominant species of low molecular weight immunoreactive material co-eluted with beta-endorphin(1-31).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Pregnancy-associated changes in ovarian immunoreactive beta-endorphin in rats. 293 66

The avidin-biotin-peroxidase technique is proposed for the immunological localization of beta-endorphin in the rat spinal cord. A rabbit specific antibody anti-human beta-endorphin was first obtained and then identified by immunoblotting and incubated with a quick-frozen section of young rat spinal cord. The use of a specific antibody with the immunoperoxidase reaction gave a morphological visualization of the beta-endorphin in the histological sections of the rat spinal cord.
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PMID:Localization of beta-endorphins in the rat spinal cord using avidin-biotin technology. 295 Aug 50

Chromogranin was demonstrated by immunohistochemistry in the cytoplasm of human beta-thyrotropin, human beta-follicle-stimulating hormone-, human beta-luteinizing hormone-, and human alpha-subunit-containing cells of the non tumorous human adenohypophyses. Some surgically removed human beta-thyrotropin-, human beta-follicle-stimulating hormone-, human beta-luteinzing hormone-, and human alpha-subunit-producing pituitary adenomas, as well as some null cell-adenomas, exhibited chromogranin immunoreactivity, whereas adenomas storing human growth hormone, human prolactin, or corticotropin were negative. Chromogranin immunopositivity was variable in extent and intensity; not every glycoprotein-producing cell could be immunostained in the nontumorous adenohypophysis and the majority of chromogranin-containing adenomas showed only focal positivity. No explanation can be offered for this variability. The demonstration of chromogranin by the avidin-biotin-peroxidase technique may be helpful in the immunohistochemical characterization of some glycoprotein hormone-producing pituitary adenomas, as well as null-cell adenomas of the human pituitary.
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PMID:Immunohistochemical localization of chromogranin in human hypophyses and pituitary adenomas. 298 72

Using an immunofluorescence microscopic staining technique, adrenocorticotropin (ACTH)-stained myenteric plexus perikarya and nerve fibers as well as ACTH-immunoreactive submucous plexus nerve processes were revealed in the rat duodenum. However, ACTH-immunostained cells were also seen in Bunner's glands. In immunoelectron microscopic experiments could be demonstrated that the ACTH-immunoreactivity was contained within presumptive endocytotic vesicles of these cells. The ACTH-positive vesicles had a mean diameter of 270 nm. The ACTH-peroxidase anti-peroxidase (PAP) complex (mean diameter 50 nm) was located on the inner surface of the vesicle. At light microscopic level, ACTH-immunofluorescent nerve fibers were in close association with these ACTH-stained Brunner's gland cells. These findings might indicate that ACTH influences both the quality and quantity of the mucous produced by Brunner's gland cells.
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PMID:Adrenocorticotropin immunoreactivity is contained within presumptive endocytotic vesicles of rat Brunner's gland cells. 298 1

Electron-immunocytochemical staining with lectin (concanavalin A: Con A) binding sites analysis was applied to study secretory granules of human pituitary adenomas and surrounding normal pituitary tissue using post-embedded serial ultrathin sections. Twelve cases of human pituitary adenoma and three specimens of normal pituitary tissue surrounding adenomas were studied: the cases were operated on between 1982 and 1984. The tumors consisted of four prolactin (PRL)-, six growth hormone (GH)-, and two adrenocorticotropic hormone (ACTH)-producing adenomas. In parallel with the detection of Con A binding sites of secretory granules, their secreting hormones were characterized electron-microscopically with the immunocytochemical horseradish peroxidase (HRP) labeling using the avidin-biotin technique. The two cases of ACTH-producing adenomas showed either weak or negative reactions with Con A on secretory granules, while normal ACTH-producing pituitary cells showed strong reactions with Con A on every secretory granule observed. Large secretory granules of PRL- or GH-producing cells showed negative reactions with Con A both in the pituitary adenoma and normal pituitary, while some small granulated or sparsely granulated adenoma cells also showed strong reactions with Con A. The complexity of human pituitary adenomas is illustrated as well as the difference in biochemical structure of normal pituitary cells and pituitary adenoma cells secreting the same specific hormone.
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PMID:Difference of lectin binding sites of secretory granules between normal pituitary and adenoma cells. 299 Jan 44

The identification of immunoreactive beta-endorphin, beta-lipotropin and ACTH from extracts of human placentas by radioimmunoassay suggests a probable synthesis of these peptides in the placenta. In this study we investigated the presence of beta-endorphin and ACTH in placenta, amniotic membranes and umbilical cord using a peroxidase-antiperoxidase staining technique. Tissues were obtained immediately after delivery, fixed in formalin and embedded in paraffin. As control tissues autopsy specimens of pituitary glands from adults and newborns were used. All sections of pituitary glands showed a positive reaction; negative results were observed in sections of placentas, umbilical cords and amniotic membranes. We conclude that no intracellular storage of beta-endorphin and ACTH takes place in the examined tissues.
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PMID:Investigation of beta-endorphin and adrenocorticotropic hormone in placenta, amniotic membrane and umbilical cord using an immunoperoxidase technique. 299 Oct 90


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