scholarly journals Diagnosis of t(2;5)(p23;q35)-associated Ki-1 lymphoma with immunohistochemistry

Blood ◽  
1994 ◽  
Vol 84 (11) ◽  
pp. 3648-3652 ◽  
Author(s):  
M Shiota ◽  
J Fujimoto ◽  
M Takenaga ◽  
H Satoh ◽  
R Ichinohasama ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Chimeric Protein ◽  
Chromosomal Translocation ◽  
Kinase Domain ◽  
Positive Staining ◽  
Kinase Gene ◽  
Fusion Junction ◽  
Rabbit Polyclonal Antibody ◽  
Tyrosine Kinase Gene

Some Ki-1 lymphomas carry a specific chromosomal translocation, t(2;5)(p23;q35). We have recently found a novel hyperphosphorylated 80- kD protein tyrosine kinase, p80, in a human Ki-1 lymphoma with this translocation. Subsequent cDNA cloning showed that p80 is a fusion protein of two different genes on chromosome 2p23 and 5q35, the novel tyrosine kinase gene and nucleophosmin gene, respectively. In this study, we intended to detect p80 on lymphoma tissues with immunologic methods. Thus, we developed rabbit polyclonal antibody using a synthetic peptide corresponding to a part of its kinase domain. The antibody (anti-p80) immunoprecipitated and immunoblotted p80 specifically from AMS3. Then, to examine whether t(2;5)(p23;q35) was present on biopsied lymphomas, reverse transcriptase-polymerase chain reaction (RT-PCR) covering the fusion junction of p80 mRNA was performed. Among 10 Ki-1 lymphomas and 10 additional lymphomas other than the Ki-1 lymphomas, expression of p80 mRNA was detected in three cases exclusively. When these 20 cases and additional 30 lymphomas were immunostained with anti-p80, positive staining was noted exclusively in the three cases found by PCR to have harbored the p80 mRNA. Thus, the present immunostaining, as well as PCR, was shown to be efficient for detecting lymphomas producing this chimeric protein/mRNA.

scholarly journals Anaplastic large cell lymphomas expressing the novel chimeric protein p80NPM/ALK: a distinct clinicopathologic entity

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1954-1960 ◽  
Author(s):  
M Shiota ◽  
S Nakamura ◽  
R Ichinohasama ◽  
M Abe ◽  
T Akagi ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Cell Lymphoma ◽  
Chimeric Protein ◽  
Large Cell ◽  
The Novel ◽  
Paraffin Sections ◽  
Kinase Gene ◽  
Younger Patient ◽  
Tyrosine Kinase Gene

Anaplastic large cell lymphoma (ALCL) is a subtype of non-Hodgkin's lymphoma characterized by the CD30+ large neoplastic cells and sometimes carries a t(2;5)(p23;q35). Recently, we found a novel hyperphosphorylated 80-kD protein tyrosine kinase, p80, in ALCLs with t(2;5). Subsequent cDNA cloning showed p80 to be a fusion protein of two genes, the novel tyrosine kinase gene and the nucleophosmin gene, in accordance with the sequence of the NPM/ALK gene (Morris et al, Science 263:1281, 1994). Meanwhile, the clinicopathologic features of p80-carrying ALCLs have remained unclear. Paraffin sections of 105 cases of ALCL were immunostained using anti-p80 antibody, and 30 of them were shown to express p80. Clinicopathologic comparison between p80-positive and -negative ALCLs showed that p80-positive cases occurred in a far younger patient age group (16.2 +/- 12.9 years; p80- negative cases, 51.0 +/- 22.3 years; P < .0001) and the patients showed a far better 5-year survival rate (79.8%; p80-negative group, 32.9%; P < .01). These data showed that p80-positive ALCL is a distinct entity both clinically and pathogenetically and should be differentiated from p80-negative ALCL.

Diverse expression of dsrc29A, a gene related to src, during the life cycle of Drosophila melanogaster

Development ◽  
1990 ◽  
Vol 110 (4) ◽  
pp. 1169-1183
Author(s):  
A.L. Katzen ◽  
T. Kornberg ◽  
J.M. Bishop
Keyword(s):  
Life Cycle ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Phagocytic Cells ◽  
Kinase Gene ◽  
Protein Tyrosine ◽  
Tyrosine Kinase Gene

We used in situ hybridization to study the RNA expression of the dsrc29A gene during Drosophila development. This gene encodes two proteins differing at their amino termini. Both gene products contain a protein-tyrosine kinase domain and resemble the protein encoded by vertebrate src. We examined most stages of development in the Drosophila life cycle: embryos, third instar larvae, pupae and adults. Our results revealed that dsrc29A expression is specialized throughout development, being prominent at various times in neural tissue, phagocytic cells, dorsal vessel, ovaries, gut, developing salivary glands, imaginal discs and disc derivatives. These findings confirm and extend previous results for the distribution of dsrc29A protein, indicating that the regulation of this gene is primarily at the level of transcription. In some tissues expression is transient, whereas in others, it is continuous, and expression occurs in proliferative, differentiating and differentiated tissue. These patterns of expression demonstrate how a single protein-tyrosine kinase might play diverse roles at different times during development. Comparison of the expression of dsrc29A and other members of the protein-tyrosine kinase gene superfamily reveals that the genes are expressed in distinctive but sometimes overlapping patterns.

Evolution, expression, and chromosomal location of a novel receptor tyrosine kinase gene, eph

1988 ◽  
Vol 8 (9) ◽  
pp. 3770-3776
Author(s):  
Y Maru ◽  
H Hirai ◽  
M C Yoshida ◽  
F Takaku
Keyword(s):  
Tyrosine Kinase ◽  
Blot Analysis ◽  
Protein Tyrosine Kinase ◽  
Normal Liver ◽  
Cell Types ◽  
Kinase Domain ◽  
Kinase Gene ◽  
Preferential Expression ◽  
Cdna Sequences ◽  
Carboxy Terminal

Partial sequence analysis of the genomic eph locus revealed that the splicing points of kinase domain-encoding exons were completely distinct from those of the other protein tyrosine kinase members reported, suggesting that this is the earliest evolutionary split within this family. In Northern (RNA) blot analysis, the eph gene was expressed in liver, lung, kidney, and testis of rat, and screening of 25 human cancers of various cell types showed preferential expression in cells of epithelial origin. Overexpression of eph mRNA was found in a hepatoma and a lung cancer without gene amplification. Comparison of cDNA sequences derived from a normal liver and a hepatoma that overproduces eph mRNA demonstrated that two of them were completely identical throughout the transmembrane to the carboxy-terminal portions. Southern blot analysis of DNAs from human-mouse hybrid clones with an eph probe showed that this gene was present on human chromosome 7.

Structure and expression of STK, a src-related gene in the simple metazoan Hydra attenuata

1989 ◽  
Vol 9 (10) ◽  
pp. 4141-4151
Author(s):  
T C Bosch ◽  
T F Unger ◽  
D A Fisher ◽  
R E Steele
Keyword(s):  
Amino Acid ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Genomic Sequence ◽  
Cdna Clones ◽  
Kinase Gene ◽  
Protein Tyrosine ◽  
Acid Protein ◽  
Tyrosine Kinase Gene ◽  
Hydra Attenuata

Both cDNA clones and a genomic DNA clone encoding a 509-amino-acid protein that is 64% similar to chicken pp60c-src were isolated from the simple metazoan Hydra attenuata. We have designated this gene STK, for src-type kinase. Features of the amino acid sequence of the protein encoded by the STK gene suggest that it is likely to be myristoylated and regulated by phosphorylation in a manner similar to that found for pp60c-src. The genomic sequence encoding the protein was found to be interrupted by at least two introns, one of which was located in a position identical to that of one of the introns in the chicken src gene. The STK gene was expressed during early development of H. attenuata and at high levels in the epithelial cells of adult polyps. Probing of Hydra proteins with an antibody to phosphotyrosine indicated that the major phosphotyrosine-containing protein in H. attenuata may be the STK protein itself. H. attenuata is the simplest organism from which a protein-tyrosine kinase gene has been isolated. The presence of such a gene in the evolutionarily ancient phylum Cnidaria suggests that protein-tyrosine kinase genes arose concomitantly with or shortly after the appearance of multicellular organisms.

Isolation and sequence analysis of a novel human tyrosine kinase gene

1989 ◽  
Vol 9 (4) ◽  
pp. 1587-1593
Author(s):  
Q L Hao ◽  
N Heisterkamp ◽  
J Groffen
Keyword(s):  
Tyrosine Kinase ◽  
Kinase Domain ◽  
Protein Product ◽  
Transmembrane Region ◽  
Base Pairs ◽  
Kinase Gene ◽  
Protein Kinase Domain ◽  
Reading Frame ◽  
Tyrosine Protein Kinase ◽  
Tyrosine Kinase Gene

Using v-abl probes, we have identified and cloned a novel fes/fps-homologous human cDNA, which we have designated FER (pronounced "fair"). This apparently full-length cDNA of 3.0 kilobases has an open reading frame of 2,466 base pairs and the capacity to encode a protein of 94,000 molecular weight. The cDNA contains regions homologous to the highly conserved tyrosine protein kinase domain of other oncogenes and growth factor receptors but lacks a clear transmembrane region, indicating that it encodes a tyrosine kinase of the nonreceptor type. The deduced amino acid sequence of FER resembles that of c-fes/fps. Our data indicate that the protein product of FER, p94FER, corresponds to a previously reported cellular phosphoprotein, NCP94, detected with a v-fps-specific antipeptide antiserum.

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