Disease specificity of kinase domains: the src-encoded catalytic domain converts erbB into a sarcoma oncogene.

Chang, Chi Ming; Shu, Hui; Kung, Hsing Jien

doi:10.1073/pnas.92.9.3928

Cited by 6 publications

(6 citation statements)

References 51 publications

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“…The src kinase domain of the chimera converted the erbB into a sarcoma oncogene. The chimeric oncogene produced sarcomas, but not leukemias, in young birds (19). Thus, it is plausible that erbB-2 may interact with the src oncogene to yield a sarcoma, or may undergo a mutation in its catalytic domain that induces the development of sarcoma.…”

Section: Discussionmentioning

confidence: 99%

Lack of ErbB-2 Oncogene Product Overexpression in Soft Tissue Sarcomas

Merimsky¹,

Issakov²,

Schwartz³

et al. 2002

Acta Oncologica

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Section: Discussionmentioning

confidence: 99%

Lack of ErbB-2 Oncogene Product Overexpression in Soft Tissue Sarcomas

Merimsky¹,

Issakov²,

Schwartz³

et al. 2002

Acta Oncologica

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“…These kinases share common sequence motifs in their catab¢ic domain [6]. Many PTKs have been shown to be oncogenic once they have lost their biological regulation either by gene amplification, somatic mutation or viral activation [2,3,22,24]. Many PTKs have been shown to be oncogenic once they have lost their biological regulation either by gene amplification, somatic mutation or viral activation [2,3,22,24].…”

Section: Introductionmentioning

confidence: 99%

Protein-tyrosine kinase and protein-serine/threonine kinase expression in human gastric cancer cell lines

Lin

Huang

et al. 1998

J Biomed Sci

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Protein kinases play key roles in cellular functions. They are involved in many cellular functions including; signal transduction, cell cycle regulation, cell division, and cell differentiation. Alterations of protein kinase by gene amplification, mutation or viral factors often induce tumor formation and tumor progression toward malignancy. The identification and cloning of kinase genes can provide a better understanding of the mechanisms of tumorigenesis as well as diagnostic tools for tumor staging. In this study, we have used degenerated polymerase-chain-reaction primers according to the consensus catalytic domain motifs to amplify protein kinase genes (protein-tyrosine kinase, PTK, and protein-serine/threonine kinase, PSK) from human stomach cancer cells. Following amplification, the protein kinase molecules expressed in the gastric cancer cells were cloned into plasmid vectors for cloning and sequencing. Sequence analysis of polymerase-chain-reaction products resulted in the identification of 25 protein kinases, including two novel ones. Expression of several relevant PTK/PSK genes in gastric cancer cells and tissues was further substantiated by RT-PCR using gene-specific primers. The identification of protein kinases expressed or activated in the gastric cancer cells provide the framework to understand the oncogenic process of stomach cancer.

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“…PKs are related by the presence of a conserved kinase domain (or catalytic domain), which consists of 250-300 amino acid residues [16][17][18]. Many PK genes have been shown to be oncogenic once they become constitutively active by overexpression, translocation, point mutation or rearrangement [5,6]. Tyrosine phosphorylation catalyzed by PTKs is a key step in transducing signals from external stimuli to the nucleus.…”

Section: Introductionmentioning

confidence: 99%

Isolation and identification of novel protein kinase genes from the round-spotted pufferfish(Tetraodon fluviatilis) genomic DNA

et al. 1998

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The round-spotted pufferfish Tetraodon fluviatilis has a genome size of 380 Mb which is slightly smaller than that of another pufferfish, Fugu rubripes rubripes (Fugu). Due to their compact genome and small introns, both pufferfishes have been proposed as model organisms for genome studies. In this study, we have used genomic DNA as template to perform PCR to screen for protein kinase (pk) genes. Forty-one T. fluviatilis pk genes encoding 7 receptor tyrosine kinases, 14 nonreceptor tyrosine kinases, 16 serine/threonine kinases, 1 dual kinase and 3 novel kinases have been identified. The success of this approach depends on the size and location of the introns. Most of the identified pk gene fragments contain introns, ranging from 71 to 300 bp, with an average of 120 bp. It is noteworthy that the intron/exon boundaries of certain genes which belong to the same family are identical. We also analyzed by specific RT-PCR primers the expression profile of those 3 novel genes as well as some selected pk genes in a variety of tissues. We found that erbB3, pku a, mrk, CaMK I, CaMKIIgamma, and two novel kinase genes (133 and 3-26) are expressed in all tissues examined. However, the novel clone 146 is strongly expressed in the brain and weakly in the intestine, kidney and heart.

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Disease specificity of kinase domains: the src-encoded catalytic domain converts erbB into a sarcoma oncogene.

Cited by 6 publications

References 51 publications

Lack of ErbB-2 Oncogene Product Overexpression in Soft Tissue Sarcomas

Lack of ErbB-2 Oncogene Product Overexpression in Soft Tissue Sarcomas

Protein-tyrosine kinase and protein-serine/threonine kinase expression in human gastric cancer cell lines

Isolation and identification of novel protein kinase genes from the round-spotted pufferfish(Tetraodon fluviatilis) genomic DNA

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