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Cheryl L. Willman - One of the best experts on this subject based on the ideXlab platform.
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identification of the chimeric Protein Product of the cbfb myh11 fusion gene in inv 16 leukemia cells
Genes Chromosomes and Cancer, 1996Co-Authors: Cisca Wijmenga, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Cheryl L. Willman, Trevor Blake, Adam Bagg, Robert S. Adelstein, Francis S. CollinsAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant form in all five cases studied. Genes Chromosom Cancer 16:77–87 (1996). © 1996 Wiley-Liss, Inc.
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Identification of the chimeric Protein Product of the CBFB-MYH11 fusion gene in inv(16) leukemia cells.
Genes chromosomes & cancer, 1996Co-Authors: Pu Paul Liu, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Trevor Blake, Adam Bagg, Cisca Wijmenga, Robert S. Adelstein, Cheryl L. WillmanAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant from in all five cases studied.
Francis S. Collins - One of the best experts on this subject based on the ideXlab platform.
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identification of the chimeric Protein Product of the cbfb myh11 fusion gene in inv 16 leukemia cells
Genes Chromosomes and Cancer, 1996Co-Authors: Cisca Wijmenga, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Cheryl L. Willman, Trevor Blake, Adam Bagg, Robert S. Adelstein, Francis S. CollinsAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant form in all five cases studied. Genes Chromosom Cancer 16:77–87 (1996). © 1996 Wiley-Liss, Inc.
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the neurofibromatosis type 1 gene and its Protein Product neurofibromin
Neuron, 1993Co-Authors: David H Gutmann, Francis S. CollinsAbstract:Von Recklinghausen neurofibromatosis, or neurofibromatosis type 1 (NFI), affects approximately 1 in 3500 individuals of all ethnic backgrounds. It is inherited as an autosomal dominant disease and is manifested clinically by abnormalities that predominantly affect tissues which derive from the neural crest (Riccardi, 1981,199l; Riccardi and Eichner, 1986). Affected individuals are often noted to have multiple cafeau-lait spots during the first year of life. These pigmented birthmarks contain melanocytes harboring macromelanosomes, but have noclinical significance other than as a diagnostic clue. Similarly, another important clinical feature, the presence of Lisch nodules of the iris, has no associated morbidity. However, these hamartomas appear during childhood and are eventually present in close to 100% of affected adults. Neurofibromas, which give the disease its name and usually make their appearance just before or during adolescence, are benign cutaneous tumors consisting of Schwann cells, fibroblasts, and other cellular elements. They increase in size and number with age, but at an unpredictable rate. More deeply placed neurofibromas, called plexiform lesions, usually appear in childhood and can lead to significant complications due to associated overgrowth of nearby tissues. Furthermore, such plexiform lesions have a modest but significant risk of degenerating into malignant neurofibrosarcoma, a highly invasive soft tissue tumor that is frequently fatal. This potential, plus the risk of optic glioma (which affects 2%-S% of all individuals with NFI) justifies placing this disease on the list of familial cancer syndromes (Bader, 1986). Other features of NFI arevariable but can be significant in a given patient. Approximately half of affected individuals have at least some degree of learning disability, and a small percentage have frank mental retardation (Riccardi, 1981). Seizures are present in about 5% of individuals, and megalencephaly is a typical finding. The diagnosis is usually not difficult to make in an adolescent or adult, but can occasionally present difficulties in a very young child. NFI is characterized by extreme variability, even among individuals within the same family who carry the same mutation. Approximately two-thirds of individuals with NFI lead relatively normal lives, with occasional interruptions for surgical management of their disease, often to remove neurofibromas that are causing cosmetic or physical distress. About one-third of individuals suffer a severe complication sometime during their lifetime. NFI has occasionally been erroneously referred to as “the elephant man disease”; while the gross facial distortion and other deformities present in Joseph Merrick, the Elephant Man, in some ways resemble the most severe end of the spectrum of NFI, subsequent evaluation of Merrick’s skeleton indicates that he probably had another disorder known as Proteus syndrome (Tibbles and Cohen, 1986).
K C Robbins - One of the best experts on this subject based on the ideXlab platform.
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wiskott aldrich syndrome Protein physically associates with nck through src homology 3 domains
Molecular and Cellular Biology, 1995Co-Authors: Octavio M Riverolezcano, Antonio Marcilla, J H Sameshima, K C RobbinsAbstract:In the second of a series of experiments designed to identify p47nck-Src homology 3 (SH3)-binding molecules, we report the cloning of SAKAP II (Src A box Nck-associated Protein II) from an HL60 cDNA expression library. This molecule has been identified as a cDNA encoding the Protein Product of WASP, which is mutated in Wiskott-Aldrich syndrome patients. Studies in vivo and in vitro demonstrated a highly specific interaction between the SH3 domains of p47nck and Wiskott-Aldrich syndrome Protein. Furthermore, anti-Wiskott-Aldrich syndrome Protein antibodies recognized a Protein of 66 kDa by Western blot (immunoblot) analysis. In vitro translation studies identified the 66-kDa Protein as the Protein Product of WASP, and subcellular fractionation experiments showed that p66WASP is mainly present in the cytosol fraction, although significant amounts are also present in membrane and nuclear fractions. The main p47nck region implicated in the association with p66WASP was found to be the carboxy-terminal SH3 domain.
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physical association between src homology 3 elements and the Protein Product of the c cbl proto oncogene
Journal of Biological Chemistry, 1994Co-Authors: Octavio M Riverolezcano, Antonio Marcilla, J H Sameshima, K C RobbinsAbstract:Abstract To investigate the nature of Proteins recognized by Src homology 3 (SH3) domains, a cDNA expression library was prepared from macrophages and screened with a probe representing the three SH3 domains of p47nck. Two clones were isolated, and one, designated SAKAP I (for Src A box Nck-associated Protein I), contained the carboxyl-terminal half of the cbl proto-oncogene Product. Studies in vitro demonstrated reactivity between SAKAP I and SH3 domains derived from a variety of molecules. Wide variations in this assay suggested a high degree of specificity inherent in SAKAP I binding. Moreover, it was possible to demonstrate an in vivo association between p47nck and p120c-cbl in HL60 cells. These findings suggest that Proteins containing SH3 elements regulate Cbl function.
Cisca Wijmenga - One of the best experts on this subject based on the ideXlab platform.
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identification of the chimeric Protein Product of the cbfb myh11 fusion gene in inv 16 leukemia cells
Genes Chromosomes and Cancer, 1996Co-Authors: Cisca Wijmenga, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Cheryl L. Willman, Trevor Blake, Adam Bagg, Robert S. Adelstein, Francis S. CollinsAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant form in all five cases studied. Genes Chromosom Cancer 16:77–87 (1996). © 1996 Wiley-Liss, Inc.
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Identification of the chimeric Protein Product of the CBFB-MYH11 fusion gene in inv(16) leukemia cells.
Genes chromosomes & cancer, 1996Co-Authors: Pu Paul Liu, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Trevor Blake, Adam Bagg, Cisca Wijmenga, Robert S. Adelstein, Cheryl L. WillmanAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant from in all five cases studied.
Adam Bagg - One of the best experts on this subject based on the ideXlab platform.
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identification of the chimeric Protein Product of the cbfb myh11 fusion gene in inv 16 leukemia cells
Genes Chromosomes and Cancer, 1996Co-Authors: Cisca Wijmenga, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Cheryl L. Willman, Trevor Blake, Adam Bagg, Robert S. Adelstein, Francis S. CollinsAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant form in all five cases studied. Genes Chromosom Cancer 16:77–87 (1996). © 1996 Wiley-Liss, Inc.
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Identification of the chimeric Protein Product of the CBFB-MYH11 fusion gene in inv(16) leukemia cells.
Genes chromosomes & cancer, 1996Co-Authors: Pu Paul Liu, Amitav Hajra, James T Rector, James D. Cotelingam, Christine A. Kelley, Trevor Blake, Adam Bagg, Cisca Wijmenga, Robert S. Adelstein, Cheryl L. WillmanAbstract:An expressed gene formed by fusion between the CBFB transcription factor gene and the smooth muscle myosin heavy chain gene MYH11 is consistently detected by reverse transcription polymerase chain reaction (RT-PCR) in patients who have acute myeloid leukemia (AML) subtype M4Eo with an inversion of chromosome 16. We have previously shown that a CBFB-MYH11 cDNA construct can produce a chimeric Protein and transform NIH 3T3 cells. However, the presence of the chimeric Protein in patient cells has not been demonstrated previously. Here, we show that such chimeric Proteins can be identified in vivo, primarily in the nuclei of the leukemic cells, by use of antibodies against the C-terminus of the smooth muscle myosin heavy chain and the fusion junction peptide. A very high molecular weight Protein/DNA complex is generated when nuclear extracts from patient cells are used in electrophoretic mobility shift assays, as seen in NIH 3T3 cells transfected with the CBFB-MYH11 cDNA. Immunofluorescence staining shows that the Proteins are organized in vivo into novel structures within cell nuclei. One isoform of the transcript of the CBFB-MYH11 fusion gene, containing the MHC204 C-terminus, was the predominant from in all five cases studied.
