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)

90 primary breast carcinomas and 18 metastases were immunostained for c-erbB-2 protein and neuron specific enolase. 30 tumours were c-erbB-2 negative and NSE positive, 23 tumours were NSE negative and c-erbB-2 positive. 1 tumour expressed focal immunoreactivity for both markers. 54 of the 108 tumours (50%) did not express either marker. Hormone immunoreactivity was present in single cells and in small groups of cells in 18 of the 31 NSE positive tumours. Bombesin, neurotensin and prealbumin were present in 4 cases each, followed by beta-endorphin and VIP in 3 cases each, leu-enkephalin in 2 cases and gastrin, serotonin, substance P, glucagon and somatostatin in 1 case each. None of 10 NSE negative breast carcinomas were comprised of cells expressing immunoreactivity for hormones. By immunoelectron microscopic examination the c-erbB-2 protein was shown to be present on the cell membrane, on smooth areas, microvilli and in coated pits. Immunoreactivity was also expressed in vesicles in cytoplasm and along rough endoplasmic reticulum. The study shows that c-erbB-2 protein expression and neuroendocrine activity are present in different tumour cell populations. This supports the hypothesis that the presence of c-erbB-2 protein, indicating an elevated cellular tyrosine kinase activity with stimulation of growth, intracellular Ca++, and phosphatidylinositol derivates, means that the same cell does not need regulation of the same factors by stimulation of peptide hormone receptors. Thus the production of autocrine and paracrine factors is switched off.
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PMID:C-erbB-2 protein and neuroendocrine expression in breast carcinomas. 167 29

A transurethral prostatic resection for prostatism in a 73 year old man showed a cluster of richly capillarised clear cells originally thought to be indicative of invasive carcinoma. Immunohistochemical studies were carried out on this tissue specimen and three similar cases using a variety of antibodies--Neuron specific enolase, PGP 9.5, chromogranin, synaptophysin, serotonin, somatostatin, substance P, calcitonin, calcitonin gene related peptide, met-enkephalin, VIP, neurofilament, CAM 5.2, S100 protein, prostatic specific antigen and prostatic acid phosphatase. The cellular foci were shown to be composed of paraganglionic cells. The cell clusters were well defined and predominantly comprised clear cells with scanty, fine eosinophilic cytoplasmic granules in three cases. The cell nuclei were round to oval, moderately pleomorphic, with evenly dispersed dense chromatin. It is concluded that the presence of minute foci of paraganglial cells in the bladder wall and prostate gland may be misinterpreted as malignant because of their close association with nerves and their relative rarity. Immunohistochemical staining with neuroendocrine markers should dispel any doubt about their identity.
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PMID:Paraganglial cells of urinary bladder and prostate: potential diagnostic problem. 169 Feb 21

Adenomas of the pars intermedia from 19 horses and normal pituitary glands from seven horses were evaluated histologically and immunocytochemically for adrenocorticotropic hormone (ACTH), alpha-melanocyte-stimulating hormone (alpha-MSH), beta-endorphin (beta-END), proopiomelanocortin (POMC), prolactin, neuron specific enolase, and glial fibrillary acidic protein (GFAP). The 26 horses ranged in age from 7 to 31 years. Histologically, all adenomas had a uniform pattern characterized by cords of large columnar cells forming palisades and pseudoacini separated by a delicate fibrovascular stroma. Immunostaining of adenomas derived from the pars intermedia was similar to that of non-neoplastic equine pars intermedia. An immunocytochemical evaluation revealed a diffuse, strong cytoplasmic reaction for POMC, a moderate to strong reaction for alpha-MSH and beta-END, a weak reaction for ACTH, and negative immunostaining for prolactin, GFAP, and neuron specific enolase in the adenomas. The unique clinicopathologic syndrome that develops in horses with pituitary adenomas appears to be the result of an over-production of POMC-derived peptides in addition to space-occupying effects resulting in dysfunction of the hypothalamus and neurohypophysis.
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PMID:Immunocytochemical demonstration of proopiomelanocortin-derived peptides in pituitary adenomas of the pars intermedia in horses. 217 80

Forty-two breast carcinomas were studied with different markers for detecting neuroendocrine differentiation. The Bodian and Grimelius silver stains were applied, as well as immunostaining for neurone specific enolase (NSE), chromogranin, prealbumin and a battery of hormones. All cases were studied by electron microscopy as well. The material included 29 infiltrating ductal carcinomas, 10 infiltrating lobular carcinomas and 3 tubular carcinomas. Immunostaining for hormones was obtained in 11 cases (gastrin and PP (4 cases each), leu-enkephalin (3 cases), substance P (2 cases), beta-endorphin (2 cases), ACTH (1 case) and bombesin (1 case). Three cases revealed immunostaining for more than one hormone. Sixteen cases were positively stained with rabbit anti-NSE (Dako Corporation) and included all the 11 cases with proven immunoreactivity for hormones. 20 cases were positively stained with sheep anti-NSE and only 8 of the 11 cases with immunoreactivity for hormones were included. Immunostaining for prealbumin was observed in only 1 case and chromogranin in only 5 cases. All cases were unstained with the Bodian stain, whereas 3 cases showed a positive argyrophilic reaction with the Grimelius technique. Ultrastructural studies revealed typical small membrane-bound electron dense granules in cytoplasm in 4 cases, all among the 11 cases with immunoreactivity for hormones. We conclude that immunostaining with rabbit anti-NSE is the best screening method for detecting breast carcinomas with neuroendocrine differentiation.
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PMID:A study of different markers for neuroendocrine differentiation in breast carcinomas. 243 99

S-100 protein in clonal GA-1 and C6 rat glioma cell lines was released in serum-free medium supplemented with adrenocorticotropic hormone (ACTH). The induction of S-100 protein release by ACTH was dose-dependent, showing a half-maximal release at about 5 microM, and the S-100 protein concentration in the medium increased sharply within 3 min, but slightly during further incubation. The S-100 protein release was apparently accompanied by a decrease in the membrane-bound form of S-100 protein in the cell. The S-100 protein release was induced not by the ACTH1-24 fragment, which exhibits the known effects of ACTH, but by the ACTH18-39 fragment, which is designated as corticotropin-like intermediate-lobe peptide (CLIP). These results indicate that the C-terminal half of ACTH is responsible for the S-100 protein release. The enhancement of S-100 protein release by ACTH was also observed in normal rat glioblasts. The release induced by ACTH was apparently specific to S-100 protein, because little release of the cytoplasmic enzymes, creatine kinase, and enolase was observed under the same conditions. High concentrations (5 mM) of dibutyryl cyclic AMP or dibutyryl cyclic GMP were also found to induce S-100 protein release; however, catecholamines (epinephrine, norepinephrine, isoproterenol, and dopamine), acetylcholine, and glutamic acid did not enhance the release.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:S-100 protein in clonal astroglioma cells is released by adrenocorticotropic hormone and corticotropin-like intermediate-lobe peptide. 282 56

Report is made of a mature retroperitoneal teratoma in a 32-year-old man. Investigation of the tumor revealed cells immunoreactive for ACTH, Met-enkephalin, beta-LPH, serotonin, FSH, BPP, S100, Neuron-specific-enolase. These cells were mainly present in the glandular epithelium, lining the cysts of the tumor. Ultrastructurally, neuro-secretory granules were demonstrated in the cytoplasm of the tumoral endocrine cells. At no time did the patient display endocrine symptoms.
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PMID:Immunocytochemical and ultrastructural findings in a mature retroperitoneal teratoma. 283 Jun 4

N alpha-Acetyltransferase, which catalyzes the transfer of an acetyl group from acetyl coenzyme A to the alpha-NH2 group of proteins and peptides, was isolated from Saccharomyces cerevisiae and demonstrated by protein sequence analysis to be NH2-terminally blocked. The enzyme was purified 4,600-fold to apparent homogeneity by successive purification steps using DEAE-Sepharose, hydroxylapatite, DE52 cellulose, and Affi-Gel blue. The Mr of the native enzyme was estimated to be 180,000 +/- 10,000 by gel filtration chromatography, and the Mr of each subunit was estimated to be 95,000 +/- 2,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme has a pH optimum near 9.0, and its pI is 4.3 as determined by chromatofocusing on Mono-P. The enzyme catalyzed the transfer of an acetyl group to various synthetic peptides, including human adrenocorticotropic hormone (ACTH) (1-24) and its [Phe2] analogue, yeast alcohol dehydrogenase I (1-24), yeast alcohol dehydrogenase II (1-24), and human superoxide dismutase (1-24). These peptides contain either Ser or Ala as NH2-terminal residues which together with Met are the most commonly acetylated NH2-terminal residues (Persson, B., Flinta, C., von Heijne, G., and Jornvall, H. (1985) Eur. J. Biochem. 152, 523-527). Yeast enolase, containing a free NH2-terminal Ala residue, is known not to be N alpha-acetylated in vivo (Chin, C. C. Q., Brewer, J. M., and Wold, F. (1981) J. Biol. Chem. 256, 1377-1384), and enolase (1-24), a synthetic peptide mimicking the protein's NH2 terminus, was not acetylated in vitro by yeast acetyltransferase. The enzyme did not catalyze the N alpha-acetylation of other synthetic peptides including ACTH(11-24), ACTH(7-38), ACTH(18-39), human beta-endorphin, yeast superoxide dismutase (1-24). Each of these peptides has an NH2-terminal residue which is rarely acetylated in proteins (Lys, Phe, Arg, Tyr, Val, respectively). Among a series of divalent cations, Cu2+ and Zn2+ were demonstrated to be the most potent inhibitors. The enzyme was inactivated by chemical modification with diethyl pyrocarbonate and N-bromosuccinimide.
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PMID:Purification and characterization of an N alpha-acetyltransferase from Saccharomyces cerevisiae. 284 92

Eighteen cases of Cushing's syndrome caused by ectopic production of peptide hormones were investigated by histological and immunocytochemical methods and the findings correlated with clinical and biochemical observations. Immunocytochemistry showed immunoreactive adrenocorticotrophic hormone (ACTH) or peptides derived from the ACTH precursor (pro-opiomelanocortin (POMC], or both, in a total of 10 cases: five of these also contained immunoreactive-alpha-melanocyte stimulating hormone, indicating more extensive translational processing of POMC than normally occurs in healthy corticotrophs of the anterior pituitary; in two further cases peptides capable of stimulating ACTH release from the anterior pituitary were present. In the remaining six cases immunocytochemistry failed to show the presence of ACTH, other POMC derived peptides, or peptides with ACTH releasing properties. These findings correlate well with the histological and clinical observations, in that the six tumours had been clinically overt, caused rapid death, and histologically seemed to be highly malignant. In contrast, the 12 other tumours were occult to radiological examination, patients had a much improved survival rate, and histologically the tumours seemed to be less aggressive. All but one of the tumours in this series showed a degree of neuroendocrine differentiation, indicated by the presence of neuron specific enolase. These results suggest that one feature of highly malignant tumours, which cause an ectopic endocrine syndrome, is a high secretion of peptide hormones, leaving amounts that are too small to be shown by immunocytochemistry.
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PMID:Immunocytochemical study of 18 tumours causing ectopic Cushing's syndrome. 302 95

Immunoreactivity for endocrine peptides (serotonin, gastrin, somatostatin, insulin, corticotropin, calcitonin, neurotensin, vasoactive intestinal peptide, and bombesin), cytoskeletal proteins (high and low molecular weight keratins), and tumor differentiation markers (chromogranin, neuron-specific enolase, carcinoembryonic antigen, S100 protein, and Grimelius stain) was sought on nine cervical and one vaginal poorly differentiated small-cell carcinoids. Dense-core secretory granules were ultrastructurally identified in all cases (seven of ten) in which tissue was available for electron microscopy. Immunoreactivity for endocrine secretory products was rarely noted, and only in a minority cell population (serotonin in two of ten). The majority of the tumors exhibited immunoreactivity for low molecular weight keratin (AE1/AE3 in eight of ten; CAM 5.2 in seven of nine), and three of ten tumors focally expressed high molecular weight keratin. Among the markers of neuroendocrine differentiation, neurospecific enolase was more frequently expressed (ten of ten) than chromogranin (five of ten) or argyrophilia (three of ten). Carcinoembryonic antigen was present in eight of ten tumors. S100 protein was absent in all cases. In summary, poorly differentiated small-cell carcinoids of the lower female genital tract, similarly to other small-cell endocrine tumors, occasionally exhibit focal glandular and squamoid differentiation, and only relatively infrequently or focally express immunohistochemically detectable endocrine secretory products, chromogranin, and argyrophilia.
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PMID:Endocrine and tumor differentiation markers in poorly differentiated small-cell carcinoids of the cervix and vagina. 302 70

The pathophysiology of Hirschsprung's disease has not been fully elucidated but is known to have a neurogenic basis. In recent years, new neural proteins and peptides have been discovered and our aim in this study was to use immunocytochemistry to investigate their involvement in the neuronal abnormalities associated with this condition. Large bowel samples from 9 children undergoing surgery for Hirschsprung's disease were compared with those taken from 8 children with other gastrointestinal diseases but no aganglionosis. Immunocytochemistry was carried out using antibodies to a wide range of neuron specific proteins and peptides. Examination of sections immunostained for the general neuronal markers, protein gene product 9.5, neuron specific enolase and neurofilament triplet proteins, allowed rapid identification of aganglionic segments. Nerves containing vasoactive intestinal polypeptide/peptide histidine methionine (VIP/PHM), galanin, substance P, somatostatin, met-enkephalin or calcitonin gene-related peptide (CGRP) showed a marked reduction in all layers of the aganglionic bowel. However, scattered VIP/PHM immunoreactive fibres were also found in the hypertrophied nerve bundles. In contrast with these reduced peptide-containing nerves, fibres displaying NPY immunoreactivity showed a marked increase in all aganglionic segments, particularly in the circular muscle where few are found normally. Our findings shed further light on the neurobiology of aganglionic bowel and suggest that immunostaining of neural proteins and the peptide NPY can aid rapid histopathological diagnosis of congenital aganglionosis.
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PMID:Increased neuropeptide Y-immunoreactive innervation of aganglionic bowel in Hirschsprung's disease. 311 47


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