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)

Immunoblot techniques and immunohistochemistry have been used to investigate epitopes shared by alpha-melanocyte-stimulating hormone (alpha-MSH) and the 150-kD neurofilament protein (NF150). Three anti-alpha-MSH antisera (namely 31H2T, 4394, and M5) from a total of 12 sera were found to react with NF150. The three crossreacting sera are different in their binding properties to peptide fragments related to alpha-MSH, suggesting that at least two distinct epitopes are shared by NF150 and alpha-MSH. The only known sequence common to NF150 and alpha-MSH, the N-terminal Ac-S-Y residues, appears to be essential for binding of sera 31H2T and 4394. However, the binding of antiserum M5 involves other, currently unknown, similarities between NF150 and alpha-MSH. This is shown by the binding of M5 to peptides such as ACTH(4-10), which do not contain the N-terminal Ac-S-Y sequence. Binding of M5 to tobacco mosaic virus coat protein (TMV-coat protein), which is homologous with alpha-MSH and NF150 in its Ac-S-Y residues, was negligible. The peptide structures that are recognized by M5 have previously been shown to exert neurotrophic activity. The data are discussed in the light of the hypothesis that similarity between NF150 and alpha-MSH, as illustrated by binding to M5, may be significant in the neurotrophic activity of MSH-related peptides.
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PMID:Characterization of epitopes shared by alpha-melanocyte-stimulating hormone (alpha-MSH) and the 150-kD neurofilament protein (NF150): relationship to neurotrophic sequences. 243 75

Peptides related to alpha-MSH (collectively termed melanocortins) stimulate nerve growth following injury and may play a physiological role in the repair process. Melanocortins are not normally present in mature peripheral nerves but MSH-like bioactivity has been observed in extracts of injured nerves. alpha-MSH could derive from reexpression of the POMC prohormone in injured nerves or from proteolysis of the intermediate-size neurofilament protein that bears antigenic similarities to melanocortins. Using a radioimmunoassay that will distinguish between alpha-MSH and neurofilament-derived fragments, we have shown that alpha-MSH is not present (detection limit 74 pg alpha-MSH/mg protein) in damaged rat sciatic nerves.
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PMID:Damaged rat peripheral nerves do not contain detectable amounts of alpha-MSH. 283 Apr 14

Two cases of hypothalamic hamartoma are presented. The first patient was a 4-year-old boy with precocious puberty, and the second was a 6-year-old boy with epileptic seizures. In both patients, clinical symptoms and signs appeared at the age of 2 years and progressed thereafter. Computerized tomography and magnetic resonance imaging in both cases disclosed a suprasellar mass lesion in continuity with the hypothalamus. Removal of the lesions affected the endocrinological status and/or seizure control. Pathological examination revealed the lesions to be composed of well-differentiated neuronal and glial cells. Immunohistochemical study demonstrated the presence of beta-endorphin, corticotropin-releasing factor, oxytocin, and neurofilament protein (210 kD) in the neuronal cells of the first patient, but no neuropeptides were detected in the second. Electron microscopic examination on the second patient disclosed the presence of many nonmyelinated and some myelinated neuronal processes containing dense-core and clear vesicles. The morphological characteristics and the role of surgery for this lesion are discussed.
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PMID:Hypothalamic hamartoma. Report of two cases. 292 5

Neuroendocrine (NE) neoplasms of the human bronchopulmonary tract were examined by electron microscopy, immunocytochemistry, and gel electrophoresis of cytoskeletal proteins from microdissected tissue samples. All samples (carcinoids, well-differentiated NE carcinoma, NE carcinomas of intermediate type, NE carcinomas of the small cell type) contained significant numbers of cells that immunostained for one or more of the following neuroendocrine markers tested: bombesin, calcitonin, ACTH, leu-enkephalin, gastrin, serotonin, somatostatin, alpha-melanocyte-stimulating hormone, vasoactive intestinal peptide, glucagon, insulin, substance P, and neuron-specific enolase. Electron microscopy revealed typical NE cell features, including variable abundant and frequently heterogeneous neurosecretory granules. Tumor cells contained filaments specifically stained with different conventional and monoclonal antibodies to cytokeratins and displayed punctate plasma membrane staining with antibodies to desmoplakins, in agreement with the electron microscopic demonstration of tonofilament bundles and desmosomes. Immunocytochemistry for NE markers and cytoskeletal proteins on consecutive sections revealed both cytokeratins and neuroendocrine substances in single cells. Using gel electrophoresis of cytoskeletal proteins of tissue regions extracted with high salt buffer and detergent, we could detect, in the tumors tested, appreciable amounts of cytokeratin polypeptides 8, 18, and 19, i.e., major cytokeratins also found in certain other lung carcinomas such as adenocarcinomas. Tumor cells were not significantly stained with antibodies to other intermediate filament proteins such as vimentin, desmin, glial filament protein, and neurofilament protein. The results show that NE substances can be synthesized in cells containing a typical epithelial cytoskeleton, i.e., cytokeratin filaments and desmosomes. These findings support the notion of an epithelial character of these tumors and appear in contrast with recent reports that neurofilaments are the only type of intermediate filaments present in carcinoids and other pulmonary NE tumors. These observations may have important implications for the histogenesis of NE carcinomas and for diagnostic pathology.
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PMID:Coexpression of neuroendocrine markers and epithelial cytoskeletal proteins in bronchopulmonary neuroendocrine neoplasms. 298 72

Antibodies binding to the 150 kDa neurofilament protein NF150 have been purified from a serum raised by immunizing a rabbit with alpha-MSH. The NF150-binding antibodies were purified by affinity chromatography on a column of cytoskeletal proteins coupled to CNBr-activated Sepharose-4B. Immunocytochemical application of these antibodies, followed by a FITC-coupled second antibody, labels axons in intact and regenerating nerves and provides a means of identifying and counting small regenerating sprouts from 48 h after nerve crush. We have been able to demonstrate that treatment with the neurotrophic melanocortin analog, Org.2766, increases the number of regenerating axons present in the nerve as early as 72 h after nerve crush.
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PMID:Early effect of an ACTH4-9 analog (Org.2766) on regenerative sprouting demonstrated by the use of neurofilament-binding antibodies isolated from a serum raised by alpha-MSH immunization. 303 30

An antiserum to alpha-melanocyte-stimulating hormone (alpha-MSH) was found to contain antibodies to at least two types of determinants on the alpha-MSH peptide: one is present only on the free peptide, the other is shared with neurofilaments. Immunoblots from mouse brain showed the neurofilament crossreactivity to be located on proteins in the Mr 140,000 range. The neurofilament-crossreactive portion of the antiserum could be selectively absorbed out with a cytoskeletal preparation, which abolished all affinity of the antiserum to the retina but did not affect the labeling pattern in the pituitary. Absorptions with desacetyl-alpha-MSH and corticotropin seemed to indicate that the determinant shared with neurofilaments is not located at either end of the alpha-MSH peptide, but somewhere in between. The immunohistochemical labeling of the retina with the alpha-MSH antiserum was compared to the labeling with monoclonal antibodies against Mr 200,000 neurofilaments. In the adult retina the alpha-MSH-like immunoreactivity was found to be slightly more widespread; most consistently it was detectable in cell bodies of large ganglion cells, whereas the heavy neurofilament subunit was absent from somata and proximal axons of these cells. In the developing mouse brain, expression of the heavy subunit was found to lag 2-3 wk behind expression of the Mr 140,000 proteins. This confirms previous reports of a more restricted distribution and late expression of high molecular weight neurofilaments as compared to the lower subunits.
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PMID:Neurofilaments contain alpha-melanocyte-stimulating hormone (alpha-MSH)-like immunoreactivity. 619 32

The ability of alpha-MSH to facilitate the recovery of sensorimotor nerve function following crush lesion is restricted to a critical period following such a lesion. This period coincided with the initiation of sprouting and the disappearance of the 150 kD neurofilament protein from the degenerating distal stump of the nerve. Degenerating nerve contains a factor that is active in a bioassay system for MSH. This factor could not be detected in control nerves. The hypothesis is forwarded that a neurotrophic factor known to be present in degenerating nerve stumps is an alpha-MSH-like peptide formed by the breakdown of the 150 kD neurofilament protein.
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PMID:Evidence that the neurotrophic actions of alpha-MSH may derive from its ability to mimick the actions of a peptide formed in degenerating nerve stumps. 643 63

A 75-year-old female presented with a suprasellar granular cell tumor. Computed tomography (CT) revealed a high dense suprasellar mass with strong postcontrast enhancement. Magnetic resonance imaging showed a round suprasellar mass, which was hyperintense on the T1-weighted images with nonhomogeneous enhancement after the administration of gadolinium-diethylenetriaminepenta- acetic acid, and hypointense on the T2-weighted images. Cerebral angiography demonstrated no abnormal findings. The tumor was partially removed via a right frontotemporal craniotomy. The histological diagnosis was suprasellar granular cell tumor. Her postoperative course was uneventful other than mild and transient diabetes insipidus. She has remained asymptomatic without CT evidence of tumor regrowth for 20 months after the surgery. Immunohistochemical studies showed positive reaction for S-100 protein in the tumor cell nuclei, but no reaction for glial fibrillary acidic protein, neurofilament protein, Leu-7, oxytocin, beta-endorphin, adrenocorticotropic hormone, and vimentin. This case provides additional evidence for the astrocytic origin of suprasellar granular cell tumor.
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PMID:Suprasellar granular cell tumor. 874 Dec 54

Two cases of duodenal gangliocytic paraganglioma were studied by means of immunocytochemical methods using 41 kinds of antibodies. The tumors consisted of three histological types; carcinoid, ganglioneuroma and paraganglioma. Tumors of both cases exhibited immunoreactivity to at least one or as many as three of the following: calcitonin, calcitonin-gene related peptide, endocrine granule constituent, Leu7, neuropeptide Y and basic fibroblast growth factor. In addition, these tumors were also immunopositive for neuron specific enolase, S-100 protein, neurofilament protein, pancreatic polypeptide, chromogranin A, somatostatin, leuenkephalin, substance P and vasoactive intestinal peptide, as has been described in previous reports. In one case, tumor cells were immunopositive for adrenocorticotropin, bombesin, gastrin releasing peptide, myelin basic protein, neuroendocrine marker and tyrosine hydroxylase. Moreover, paraganglioma cells of tumors showed both argyrophilia and argentaffinity. These results suggest that duodenal gangliocytic paraganglioma may originate from embryonic neuroinsular complex.
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PMID:Two cases of duodenal gangliocytic paraganglioma: immunocytochemical characteristics. 882 94

A pituitary mass was removed by the transsphenoidal approach from a 63-year-old man with the clinical history and laboratory findings characteristic of Cushing's disease with partial hypopituitarism. Histological, immunohistochemical, ultrastructural and immunoelectron microscopic investigation demonstrated a periodic acid-Schiff-positive, adrenocorticotropic hormone (ACTH)-immunoreactive, pituitary corticotroph adenoma with the formation of neural tissue resembling neuropil within the tumor. The neural elements showed immunopositivity for neurofilament protein and ACTH, but were immunonegative for other adenohypophysial hormones and for corticotropin-releasing hormone. Although the molecular mechanism accounting for neural transformation in this corticotroph adenoma remained obscure, based on the clinical, histological and morphological findings it appears that formation of neural tissue most likely indicate a favorable prognosis.
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PMID:Neural transformation in a pituitary corticotroph adenoma. 1220 Jun 32


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