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10.1097/PAS.0000000000000398

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25724000Sox10?AmarkerfornotonlySchwannianandmelanocyticneoplasmsbutalsomyoepithelialcelltumorsofsofttissue.Asystematicanalysisof5134tumors.!4431945!25724000; 10; 5134
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suck abstract from ncbi


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pmid25724000; 10; 5134      Am+J+Surg+Pathol;+Biochem+Pharmacol;+Biochim+Biophys+Acta 2015 ; 39; 24; 427 (6; 17; 2): 826-35; 1639-41; 663-78
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  • Sox10--a marker for not only schwannian and melanocytic neoplasms but also myoepithelial cell tumors of soft tissue: a systematic analysis of 5134 tumors ; Digitoxin metabolism by rat liver microsomes ; The fluorescence decay of tryptophan residues in native and denatured proteins #MMPMID25724000; 10; 5134
  • Miettinen M; McCue PA; Sarlomo-Rikala M; Biernat W; Czapiewski P; Kopczynski J; Thompson LD; Lasota J; Wang Z; Fetsch JF; Schmoldt A; Benthe HF; Haberland G; Grinvald A; Steinberg IZ
  • Am J Surg Pathol; Biochem Pharmacol; Biochim Biophys Acta 2015[Jun]; 39; 24; 427 (6; 17; 2): 826-35; 1639-41; 663-78 PMID25724000; 10; 5134show ga
  • Sox10 transcription factor is expressed in schwannian and melanocytic lineages and is important in their development and can be used as a marker for corresponding tumors. In addition, it has been reported in subsets of myoepithelial/basal cell epithelial neoplasms, but its expression remains incompletely characterized. In this study, we examined Sox10 expression in 5134 human neoplasms spanning a wide spectrum of neuroectodermal, mesenchymal, lymphoid, and epithelial tumors. A new rabbit monoclonal antibody (clone EP268) and Leica Bond Max automation were used on multitumor block libraries containing 30 to 70 cases per slide. Sox10 was consistently expressed in benign Schwann cell tumors of soft tissue and the gastrointestinal tract and in metastatic melanoma and was variably present in malignant peripheral nerve sheath tumors. In contrast, Sox10 was absent in many potential mimics of nerve sheath tumors such as cellular neurothekeoma, meningioma, gastrointestinal stromal tumors, perivascular epithelioid cell tumor and a variety of fibroblastic-myofibroblastic tumors. Sox10 was virtually absent in mesenchymal tumors but occasionally seen in alveolar rhabdomyosarcoma. In epithelial tumors of soft tissue, Sox10 was expressed only in myoepitheliomas, although often absent in malignant variants. Carcinomas, other than basal cell-type breast cancers, were only rarely positive but included 6% of squamous carcinomas of head and neck and 7% of pulmonary small cell carcinomas. Furthermore, Sox10 was often focally expressed in embryonal carcinoma reflecting a primitive Sox10-positive phenotype or neuroectodermal differentiation. Expression of Sox10 in entrapped non-neoplastic Schwann cells or melanocytes in various neoplasms has to be considered in diagnosing Sox10-positive tumors. The Sox10 antibody belongs in a modern immunohistochemical panel for the diagnosis of soft tissue and epithelial tumors.; The fluorescence decay kinetics at different ranges of the emission spectrum is reported for 17 proteins. Out of eight proteins containing a single tryptophan residue per molecule, seven proteins display multiexponential decay kinetics, suggesting that variability in protein structure may exist for most proteins. Tryptophan residues whose fluorescence spectrum is red shifted may have lifetimes longer than 7 ns. Such long lifetimes have not been detected in any of the denatured proteins studied, indicating that in native proteins the tryptophans having a red-shifted spectrum are affected by the tertiary structure of the protein. The fluorescence decay kinetics of ten denatured proteins studied obey multiexponential decay functions. It is therefore concluded that the tryptophan residues in denatured proteins can be grouped in two classes. The first characterized by a relatively long lifetime of about 4 ns and the second has a short lifetime of about 1.5 ns. The emission spectrum of the group which is characterized by the longer lifetime is red shifted relative to the emission spectrum of the group characterized by the shorter lifetime. A comparison of the decay data with the quantum yield of the proteins raises the possibility that a subgroup of the tryptophan residues is fully quenched. It is noteworthy that despite this heterogeneity in the environment of tryptophan residues in each denatured protein, almost the same decay kinetics has been obtained for all the denatured proteins studied in spite of the vastly different primary structures. It is therefore concluded that each tryptophan residue interacts in a more-or-less random manner with other groups on the polypeptide chain, and that on the average the different tryptophan residues in denatured proteins have a similar type of environment.
  • |*Proteins[MESH]
  • |Animals[MESH]
  • |Biomarkers, Tumor/*analysis[MESH]
  • |Chromatography, Thin Layer[MESH]
  • |Digitoxigenin/metabolism[MESH]
  • |Digitoxin/*metabolism[MESH]
  • |Humans[MESH]
  • |Hydrogen-Ion Concentration[MESH]
  • |Hydroxylation[MESH]
  • |Immunohistochemistry[MESH]
  • |In Vitro Techniques[MESH]
  • |Kinetics[MESH]
  • |Male[MESH]
  • |Mathematics[MESH]
  • |Melanoma/metabolism/pathology[MESH]
  • |Microsomes, Liver/*metabolism[MESH]
  • |Myoepithelioma/metabolism/pathology[MESH]
  • |NADP/metabolism[MESH]
  • |Neurilemmoma/metabolism/pathology[MESH]
  • |Protein Conformation[MESH]
  • |Protein Denaturation[MESH]
  • |Rats[MESH]
  • |SOXE Transcription Factors/*metabolism[MESH]
  • |Soft Tissue Neoplasms/*metabolism[MESH]
  • |Spectrometry, Fluorescence[MESH]
  • |Time Factors[MESH]
  • |Tissue Array Analysis[MESH]


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