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首页> 外文期刊>Molecular and Cellular Biology >Activation of the c-abl oncogene by viral transduction or chromosomal translocation generates altered c-abl proteins with similar in vitro kinase properties.
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Activation of the c-abl oncogene by viral transduction or chromosomal translocation generates altered c-abl proteins with similar in vitro kinase properties.

机译：通过病毒转导或染色体易位激活c-abl癌基因会产生具有相似的体外激酶特性的c-abl蛋白改变。

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摘要

The v-abl protein of Abelson murine leukemia virus is a tyrosine-specific kinase. Its normal cellular homolog, murine c-abl, does not possess detectable tyrosine kinase activity in vitro. Previously, we have detected tyrosine kinase activity in vitro for an altered c-abl gene product (c-abl P210) in the K562 human chronic myelogenous leukemia cell line. The expression of this variant c-abl gene product correlates with chromosomal translocation and amplification of the c-abl gene in K562 cells. Like v-abl, c-abl P210 is a fusion protein containing non-abl sequences near the amino terminus of c-abl. We compared the in vitro tyrosine kinase activity of c-abl P210 with that of wild-type murine v-abl. The remarkable similarities of these two proteins with respect to cis-acting autophosphorylation, trans-acting phosphorylation of exogenous substrates, and kinase inhibition, using site-directed abl-specific antisera, suggested that c-abl P210 could function similarly to v-abl in vivo. In addition, c-abl P210 possessed an associated serine kinase activity in immunoprecipitates. The serine kinase activity was not inhibited by site-directed, abl-specific antisera that inhibit the tyrosine kinase activity, suggesting that the serine kinase activity is not an intrinsic property of c-abl P210. Thus, the activation of the c-abl gene in a human leukemia cell line may have functional consequences analogous to activation of the c-abl gene in Abelson murine leukemia virus.
机译：Abelson鼠白血病病毒的v-abl蛋白是酪氨酸特异性激酶。它的正常细胞同源物，鼠c-abl，在体外不具有可检测的酪氨酸激酶活性。以前，我们已经在K562人慢性粒细胞性白血病细胞系中检测到了改变的c-abl基因产物（c-abl P210）的酪氨酸激酶活性。这种变异的c-abl基因产物的表达与K562细胞中的染色体易位和c-abl基因的扩增有关。像v-abl一样，c-abl P210是一种融合蛋白，在c-abl的氨基末端附近包含非abl序列。我们比较了c-abl P210与野生型鼠v-abl的体外酪氨酸激酶活性。这两种蛋白质在使用定点abl特异性抗血清的顺式作用自磷酸化，外源底物的反式作用磷酸化和激酶抑制方面具有显着相似性，这表明c-abl P210的功能与v-abl相似。体内。另外，c-abl P210在免疫沉淀物中具有相关的丝氨酸激酶活性。丝氨酸激酶活性不受抑制酪氨酸激酶活性的定点，abl特异性抗血清的抑制，表明丝氨酸激酶活性不是c-abl P210的固有特性。因此，人白血病细胞系中c-abl基因的激活可能具有类似于Abelson鼠白血病病毒中c-abl基因的激活的功能后果。

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