Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027819 (neuroblastoma)
 27,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neuroblastoma x glioma hybrid cells (NG108-15) were used as a model system to characterize neuronal-glial type angiotensin (ANG) receptors by covalent crosslinking analysis. After differentiation with 1.5% DMSO and 0.5% fetal bovine serum for four to five days, saturation analysis revealed a single high affinity site with a Kd = 1.35 +/- 0.42 nM and a Bmax = 468 +/- 106 fmol/mg protein. Using the homobifunctional crosslinking reagent bis(sulfosuccinimidyl) suberate (BS3), a site with an estimated Mr of 78 kDa was specifically labeled with 125I-ANG II as determined by SDS-polyacrylamide gel electrophoresis. Both ANG II and ANG III (10(-6) M) inhibited specific labeling. The Ki for ANG III binding was similar by both pharmacologic (Ki = 3.33 +/- 0.98 nM) and gel densitometric (Ki = 2.65 +/- 0.32 nM) analyses. We conclude that the 78 kDa protein represents a high affinity ANG binding site with similar affinities for both ANG II and ANG III.
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PMID:Covalent crosslinking analysis of angiotensin receptors on differentiated NG108-15 cells. 239 77

A pool of ten monoclonal antibodies to SDS-insoluble epitopes of Alzheimer neurofibrillary tangles (NFT) was used to screen an adult human brain cDNA expression library. Fourteen clones were isolated, two of which are described. The largest of the clones encodes 80 kD, or approximately 600 amino acids, of microtubule-associated protein 2 (MAP 2). The MAP 2 region encoded by the clone shares at least two epitopes with human tau, another microtubule-associated protein which cross-reacts with NFT. In rat brain mRNA, the MAP 2 cDNA hybridizes to a single transcript of 9.5 kb. In human neuroblastoma mRNA, the MAP 2 cDNA hybridizes, at high stringency, to two transcripts of 9.5 kb and 6 kb. The 6-kb transcript comigrates with the transcript for tau, as detected by a human tau cDNA. The properties of the MAP 2 cDNA suggest that, in humans, MAP 2 and tau have a common domain which may play a role in NFT formation. Another clone isolated with the anti-NFT antibodies shares epitopes, but not nucleic acid homology, with the MAP 2 cDNA. This clone detects a single abundant transcript of 1 kb present in RNA from human neuroblastoma and from several non-neuronal human cell lines. The properties of this cDNA suggest that it encodes a protein other than those previously reported to cross-react with NFT.
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PMID:Isolation and characterization of cDNA clones encoding epitopes shared with Alzheimer neurofibrillary tangles. 244 45

The high molecular weight subunit of neurofilaments (NF-H) in mouse NB2a/d1 neuroblastoma cells is extensively phosphorylated and exhibits an apparent molecular weight of 200 kDa by SDS gel electrophoresis. In this study, we observed that extensively phosphorylated NF-H variants exist as both Triton-soluble and -insoluble forms, which display different cellular distributions. Perikarya and neurites of differentiated NB2a/d1 cells were immunostained by a polyclonal antiserum (anti-NF-H) that specifically recognizes the extensively phosphorylated NF-H forms and a monoclonal antibody (SMI-31) that recognizes phosphorylated epitopes of neurofilament proteins (NFPs). When cells were extracted with Triton X-100 to remove soluble proteins, however, only axonal neurites remained immunoreactive. Immunoblot analyses established the specificity of anti-NF-H and SMI-31 and demonstrated that both Triton-soluble and -insoluble NF-H subunits exhibit an apparent molecular weight of 200 kDa. Incorporation of radiolabeled phosphate into Triton-soluble NF-H following incubation of intact NB2a/d1 cells with 32P-orthophosphate confirmed that the Triton-soluble form of NF-H is a phosphoprotein. Most NF-H subunits in the Triton-soluble fraction sedimented after centrifugation at 100,000 g for 1 h, indicating that they may be present as oligomers. The implications of these data for the development of neurofibrillary pathology are discussed.
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PMID:Soluble, phosphorylated forms of the high molecular weight neurofilament protein in perikarya of cultured neuronal cells. 246 97

A monoclonal antibody, 6H7, was produced by the immunization of small cell carcinoma of the lung (SCCL). Immunohistochemical examination indicated that 6H7 reacted not only with SCCL but also various neuronal and/or endocrine tumors such as neuroblastoma, pheochromocytoma, carcinoid and adrenal cortical tumors. 6H7 was also reactive with normal neuroendocrine tissues including brain, spinal cord, thyroid follicular cells, pancreatic islet cells and adrenal cells. 6H7 did not react with squamous cell carcinomas, one large cell carcinoma or most adenocarcinomas of the lung, or carcinomas of the stomach, colon, pancreas, breast and esophagus. The antigen recognized by 6H7 was analyzed on gel filtration after purification of the antigen by liquid chromatography which indicated the molecular weight of the antigen to be 270,000-300,000. From SDS-PAGE analysis the antigen reactive with 6H7 appeared to consist of polypeptide dimers of 128,000.
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PMID:Monoclonal antibody directed against neuroendocrine properties of both normal and malignant cells. 246 61

The Pasteur strain of fixed rabies virus (Pasteur Institute Paris, passage 2061 in rabbit brain) was adapted by alternate passages to primary dog kidney cells. The adapted rabies virus designated as "Pasteur Potsdam" developed no CPE and yielded four harvests with a titre of 5.5-7.0 (log MICLD50/ml). The strain could be grown in BHK 21/S13, CER and N2a neuroblastoma cells. In the cultures of BHK 21/S13 cells the virus titered 6.0-8.5 (log MICLD50/ml). In SDS PAGE its G protein migrated faster than that of the ERA strain. The inactivated antigen induced interferon in mice. The strain was identified by anti-rabies immunoglobulin. The harvested material showed an antigenic value of 0.4 IU/ml. The virus was not pathogenic after s.c. and i.p. inoculations to mice, rats, Syrian hamsters, and rabbits and after i.m. inoculation to Syrian hamsters and rats.
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PMID:Properties of rabies strain ("Pasteur Potsdam") adapted to primary dog kidney cells. 248 5

Protease nexin-II (PN-II) is a protease inhibitor that forms SDS-resistant inhibitory complexes with the epidermal growth factor (EGF)-binding protein, the gamma-subunit of nerve growth factor, and trypsin. The properties of PN-II indicate that it has a role in the regulation of certain proteases in the extracellular environment. Here we describe more of the amino-acid sequence of PN-II and its identity to the deduced sequence of the amyloid beta-protein precursor (APP). Amyloid beta-protein is present in neuritic plaques and cerebrovascular deposits in individuals with Alzheimer's disease and Down's syndrome. A monoclonal antibody against PN-II (designated mAbP2-1) recognized PN-II in immunoblots of serum-free culture medium from human glioblastoma cells and neuroblastoma cells, as well as in homogenates of normal and Alzheimer's disease brains. In addition, mAbP2-1 stained neuritic plaques in Alzheimer's disease brain. PN-II was a potent inhibitor of chymotrypsin with an inhibition constant Ki of 6 x 10(-10)M. Together, these data demonstrate that PN-II and APP are probably the same protein. The regulation of extracellular proteolysis by PN-II and the deposition of at least parts of the molecule in senile plaques is consistent with previous reports that implicate altered proteolysis in the pathogenesis of Alzheimer's disease.
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PMID:Protease nexin-II, a potent antichymotrypsin, shows identity to amyloid beta-protein precursor. 250 28

The microtubule associated protein called tau, found primarily in neurons, was detected in a human neuroblastoma cell line, LAN-5. Cells treated with retinoic acid (2.0 x 10(-5) M) differentiate and acquire processes similar to neurons. Differentiated and logarithmically growing undifferentiated cells were exposed to varying doses of doxorubicin (an anthracycline chemotherapeutic antibiotic). While doxorubicin was lethal to many undifferentiated dividing cells, it was not as damaging to differentiated cells. After 2 to 4 days of doxorubicin treatment, the cells were harvested, the protein concentration determined and SDS-PAGE performed. Proteins were blotted onto nitrocellulose paper and immunostained with either a rabbit antiserum or mouse monoclonal antibody to tau. Undifferentiated LAN-5 cells treated with 4.0 x 10(-8) M doxorubicin for 4 days and cells treated with 8.0 x 10(-8) M doxorubicin for 2 days displayed a distinct lower band (just below the 50 kd marker) that was either absent or very faint in untreated controls.
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PMID:Doxorubicin affects tau protein metabolism in human neuroblastoma cells. 251 86

Bordetella pertussis produces a calmodulin-sensitive adenylate cyclase that is associated with the whole bacteria and released into its culture media. Preparations of this enzyme invade animal cells, causing elevations in intracellular cAMP levels. Cell-associated adenylate cyclase accounted for 28% of the total adenylate cyclase activity while 72% was released into the culture supernatant. Over 90% of the cell-associated adenylate cyclase activity was sensitive to trypsin treatment of whole cells, indicating that the catalytic domain of the enzyme is localized on the outer surface of the bacterial cells. Enzyme activity was released from whole cells by treatment with SDS. This activity was resolved as a large form (Mr 215,000) by SDS-polyacrylamide gel electrophoresis. In contrast, the culture supernatant contained only the 45,000-dalton catalytic subunit. Enzyme activity released from spheroplasts by sonication was resolved into a large form (Mr 215,000) and a small form (Mr 45,000). The appearance of the small form with spheroplast formation was probably the result of proteolytic degradation. Antibodies generated against the catalytic subunit purified from culture supernatants cross-reacted with and immunoprecipitated both the large and small forms of adenylate cyclase isolated from bacterial cells. Furthermore, incubation of the cell-associated enzyme with a crude bacterial extract resulted in a time-dependent disappearance of the 215,000-dalton form and a concomitant increase in the amount of the smaller 45,000-dalton form. There was also a parallel increase in the ability of the cell-associated preparation to elevate intracellular cAMP levels in N1E-115 mouse neuroblastoma cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Characterization of the bacterial cell associated calmodulin-sensitive adenylate cyclase from Bordetella pertussis. 254 Jul 97

Distinct sets of cellular proteins were labeled with [3H]myristic and [3H]palmitic acids in primary (rat neurons and astroglia) and continuous (murine N1E-115 neuroblastoma and rat C6 glioma) cell cultures derived from the nervous system. Both soluble and membrane proteins were modified by myristate in a hydroxylamine-stable (amide) linkage, while palmitoylated proteins were ester-linked and almost exclusively membrane bound. Chain elongation of both labeled fatty acids prior to acylation was observed, but no protein amide-linked [3H]myristate originating from [3H]palmitate was detected. Fatty acylation profiles differed considerably among most of the cell lines, except for rat astroglial and glioma cells in which myristoylated proteins appeared to be almost identical based on SDS gel electrophoresis. An unidentified 47 kDa myristoylated protein was labeled to a significantly greater extent in astroglial than in glioma cells; the expression of this protein could be related to transformation or development in cells of glial origin.
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PMID:Cell-specific fatty acylation of proteins in cultured cells of neuronal and glial origin. 254 6

Here we report that the mouse neuroblastoma-glioma hybrid cell line NG108-15 possess high-affinity binding sites for the nonapeptide bradykinin, as revealed by competitive displacement of 125I-8Tyr bradykinin by various bradykinin analogs. These binding sites were further characterized by covalent cross-linking of 125I-8Tyr bradykinin to intact NG108-15 grown as a monolayer, using dithiobis-succinimidylpropionate (DTSP) as a cross-linking reagent. Sodium dodecyl sulfate (SDS) electrophoresis after solubilization of the cross-linked cells, demonstrated the preferential and specific labeling of two polypeptides with apparent molecular weights of Mr = 36,000 and Mr = 47,000. A third polypeptide of Mr = 69,000 was labeled less intensely.
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PMID:Molecular characteristics and peptide specificity of bradykinin binding sites in intact neuroblastoma-glioma cells in culture (NG 108-15). 255 Aug 44


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