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基因组变异性和可变剪接产生多种PML/RARα转录本,这些转录本在急性早幼粒细胞白血病中编码异常的PML蛋白和PML/RARα异构体。

Genomic variability and alternative splicing generate multiple PML/RAR alpha transcripts that encode aberrant PML proteins and PML/RAR alpha isoforms in acute promyelocytic leukaemia.

作者信息

Pandolfi P P, Alcalay M, Fagioli M, Zangrilli D, Mencarelli A, Diverio D, Biondi A, Lo Coco F, Rambaldi A, Grignani F

机构信息

Istituto Clinica Medica I, University of Perugia, Italy.

出版信息

EMBO J. 1992 Apr;11(4):1397-407. doi: 10.1002/j.1460-2075.1992.tb05185.x.

Abstract

The acute promyelocytic leukaemia (APL) 15;17 translocation generates a PML/RAR alpha chimeric gene which is transcribed as a fusion PML/RAR alpha mRNA. Molecular studies on a large series of APLs revealed great heterogeneity of the PML/RAR alpha transcripts due to: (i) variable breaking of chromosome 15 within three PML breakpoint cluster regions (bcr1, bcr2 and bcr3), (ii) alternative splicings of the PML portion and (iii) alternative usage of two RAR alpha polyadenylation sites. Nucleotide sequence analysis predicted two types of proteins: multiple PML/RAR alpha and aberrant PML. The PML/RAR alpha proteins varied among bcr1, 2 and 3 APL cases and within single cases. The fusion proteins contained variable portions of the PML N terminus joined to the B-F RAR alpha domains; the only PML region retained was the putative DNA binding domain. The aberrant PML proteins lacked the C terminus, which had been replaced by from two to ten amino acid residues from the RAR alpha sequence. Multiple PML/RAR alpha isoforms and aberrant PML proteins were found to coexist in all APLs. These findings indicate that two potential oncogenic proteins are generated by the t(15;17) and suggest that the PML activation pathway is altered in APLs.

摘要

急性早幼粒细胞白血病(APL)的15;17易位产生了PML/RARα嵌合基因,该基因转录为融合的PML/RARα mRNA。对大量APL病例的分子研究显示,由于以下原因,PML/RARα转录本具有很大的异质性:(i)15号染色体在三个PML断点簇区域(bcr1、bcr2和bcr3)内的可变断裂;(ii)PML部分的可变剪接;(iii)两个RARα聚腺苷酸化位点的交替使用。核苷酸序列分析预测了两种类型的蛋白质:多种PML/RARα和异常PML。PML/RARα蛋白在bcr1、2和3的APL病例之间以及单个病例内存在差异。融合蛋白包含与B-F RARα结构域相连的PML N末端可变部分;唯一保留的PML区域是假定的DNA结合结构域。异常PML蛋白缺乏C末端,该末端已被RARα序列中的两到十个氨基酸残基取代。发现多种PML/RARα异构体和异常PML蛋白在所有APL中共同存在。这些发现表明,t(15;17)产生了两种潜在的致癌蛋白,并提示APL中PML激活途径发生了改变。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/77c5/556589/5f2f74e2d7da/emboj00089-0176-a.jpg

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