Sialyl-Tn- and Neuron-specific Enolase-positive Minimally Differentiated Erythroleukemia.
Kazuo MuroiTakahisa TarumotoToshikazu AkiokaKeita KiritoTadashi NagaiTohru IzumiMitsuru NakamuraKiyohiko HatakeSen‐itiroh HakomoriYasusada MiuraKeiya Ozawa
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Flow cytometric, immunochemical and molecular studies were performed on leukemic blasts from a patient with minimally differentiated erythroleukemia (AML-M6v). The blasts expressed CD36 and CD71 but not lymphoid antigens, myeloid antigens, CD41 or glycophorin A. Analysis of carbohydrate antigens showed that the blasts expressed the sialyl-Tn antigen. Immunochemistry revealed that the blasts had neuron-specific enolase (NSE). Serum sialyl-Tn and NSE levels were markedly increased. Finally, an erythroid lineage was confirmed in the presence of alpha-globin messages in the blasts. Sialyl-Tn and NSE expression in leukemic blasts may be useful to identify AML-M6v.Keywords:
Enolase
Glycophorin
Immunochemistry
Flow cytometric, immunochemical and molecular studies were performed on leukemic blasts from a patient with minimally differentiated erythroleukemia (AML-M6v). The blasts expressed CD36 and CD71 but not lymphoid antigens, myeloid antigens, CD41 or glycophorin A. Analysis of carbohydrate antigens showed that the blasts expressed the sialyl-Tn antigen. Immunochemistry revealed that the blasts had neuron-specific enolase (NSE). Serum sialyl-Tn and NSE levels were markedly increased. Finally, an erythroid lineage was confirmed in the presence of alpha-globin messages in the blasts. Sialyl-Tn and NSE expression in leukemic blasts may be useful to identify AML-M6v.
Enolase
Glycophorin
Immunochemistry
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The immunohistochemical detection of neuron-specific enolase and b-amyloid percursor protein were used in the group of deceased on craniocerebral injury and those who died of prolonged hypoxy without mechanical injury of the brain. Neuron-specific enolase (NSE) is produced by nerve cells and is a suitable marker for both the damage of neurons and axons. While undamaged nerve cells show immunoreactivity with the antibody anti-NSE, a significant decrease of this protein substance was noticed within two hours both in mechanical injury and in cases of prolonged hypoxy. We noticed the presence of NSE in damaged axons already several minutes after the injury whereas the hypoxy of brain without mechanical injury didn't show any or a very slight reaction of axons when examined with anti-NSE without topographic link to axonal lesion. b-amyloid percursor protein (b-APP) is a low molecular protein which the normal values of are not to be found in axons detected by standard immunohistochemistry. We noticed an increased frequency of appearance of this protein substance in axons changed by injury, while a reactive positivity to anti-body b-APP was to be found only rarely at the brain hypoxy without mechanical injury CNS.
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Amyloid (mycology)
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Neuron-specific enolase (NSE) was studied by immunohistochemistry and radioimmunoassay in ten gastroenteropancreatic (GEP) neuroendocrine tumors. Tissue and serum levels of NSE from the same patients were also analyzed. In all cases, NSE was localized by immunohistochemistry as diffuse cytoplasmic staining to neuroendocrine cells. Tissue levels of NSE were elevated in eight of ten cases while the serum level of NSE was elevated only in one patient with a metastatic gastrinoma to the liver. Examination of the distribution of NSE in a wide range of tumors (n = 55) showed that it is relatively specific for neurons and neuroendocrine tumors. Eight of ten tumors analyzed immunohistochemically for nine poly-peptide hormones contained more than one hormone. Two of ten tumors with only one hormone were positive for NSE. The clinical syndrome in all cases was related to only one hormone. These results indicate that the immunohistochemical demonstration of NSE is a good general marker for the neuroendocrine system. While tissue levels of NSE in GEP neuroendocrine tumors are generally elevated, the serum levels of NSE may only be markedly elevated with extensive metastatic disease.
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17 commercially available antibodies were applied on formalin fixed and paraffin embedded tissues of neuroblastomas (NBLs, n = 20), ganglioneuroblastomas (GNBLs, n = 7) and ganglioneuromas (GNs, n = 7), to assess their reliability as markers for neuroendocrine differentiation and the degree of tumor cell maturation. Our results indicate, that antibodies directed to neuron specific enolase, HISL 19, dopamine beta-hydroxylase, neurofilament, EGC, LK2H10 and leucocyte common antigen may be useful in discrimination of neuroblastomas from non-neuroendocrine round and small cell tumors in routinely processed tissue. Antibodies to neuron specific enolase, EGC, PGP 9.5, VIP, and S 100 protein may contribute to the determination of the maturation grade of (ganglio)neuroblastomas.
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Neurofilament
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AbstractNeuron-specific enolase (NSE) is an isoenzyme of the widely distributed glycolytic enzyme 2-phospho-D-glycerate hydrolase expressed by neuronal and neuronendocrine cells of the central and peripheral nervous system. Brain extract contains three forms (α, β, and γ) of enolase, and each form is a dimer of the combination of two distinct subunits α and γ. NSE consists of the two dimers containing subunits, that is, αγ and γγ, existing mainly in neuronal cells an dneuroendocrine cells. Immunohistochemistry and radioimmunoassay have shown NSE in serum from patients with various tumors including neuroblastoma (NB).3.4 In the current study we tried the immunohistochemical staining of the enzyme on the NB cells.
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Enolase
Histology
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The quantification of antigens and proteins on RBCs has been achieved by different approaches. Flow cytometry allows the results of the earliest studies to be to reappraised because it offers the possibility of measuring the immunofluorescence intensity of single cells and integrating the individual data of a large number of cells within a very short time.Flow cytometry was used in this work to analyze the binding of four MoAbs to glycophorin A (GPA) and glycophorin B (GPB). RBCs in their native state (nonfixed) were utilized. To avoid the agglutination problem, cells were disaggregated before measurements, dates were taken on 20,000 events on the single-cell region, and the fluorescence intensity of the principal peak present in the fluorescence histograms was used for the analysis. The quantification of sites per RBC was estimated by applying the Langmuir adhesion model.The numbers of GPA and GPB sites obtained for samples from healthy donors were similar to those found in the literature (1.86-4.9) x 10(5) and (0.48-1.61) x 10(5) for GPA and (0.21-1.14) x 10(5) and (0.47-0.88) x 10(5) for GPB. Differences between antibodies were found that depend on the binding site of each one.A simple method to quantify antigen sites on RBCs was developed. It could be applied whenever one antibody is assumed to bind exactly one antigen.
Glycophorin
Agglutination (biology)
Cytometry
Immunofluorescence
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Objective To clone human neuron-specific enolase (NSE)gene and prepare the monoclonal antibodies against human neuron-specific enolase and to test the expression of NSE in tumor cell lines by immunocytochemistry (ICC).Methods The gene fragment of human NSE was amplified by RT-PCR and ligated to the pGEM vector. After the sequencing of recombinant NSE, it was ligated to the expression vector pMS-31b. The MS2-NSE fusion protein was expressed after higher temperature induction. The purified target protein was used for immunizing BALB/C mice to prepare McAbs against NSE.Results Full length of NSE gene with 1 305 bp was cloned. Molecular weight of MS2-NSE was 57 000. 1.42 mg/L of MS2-NSE fusion protein could be expressed. Two strains of hybridoma secreting NSE McAbs were obtained by ELISA screening. The subtypes of the NSE McAbs were IgG1and IgG2a. The two McAbs could react with A549 cell lines in ICC. NSE positive staining in ICC was mainly located in cytoplasm.Conclusions We clone human neuron-specific enolase gene, obtain the anti-NSE monoclonal antibodies and examine the expression of NSE in lung cancer tumor cell line.
Enolase
clone (Java method)
Cloning (programming)
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