p53 deficiency increases transformation by v-Abl and rescues the ability of a C-terminally truncated v-Abl mutant to induce pre-B lymphoma in vivo - PubMed (original) (raw)
p53 deficiency increases transformation by v-Abl and rescues the ability of a C-terminally truncated v-Abl mutant to induce pre-B lymphoma in vivo
X Zou et al. Mol Cell Biol. 2000 Jan.
Abstract
Abelson murine leukemia virus (A-MuLV) is an acute transforming retrovirus that preferentially transforms early B-lineage cells both in vivo and in vitro. Its transforming protein, v-Abl, is a tyrosine kinase related to v-Src but containing an extended C-terminal domain. Many mutations affecting the C-terminal portion of the molecule block the pre-B-transforming activity of v-Abl without affecting the fibroblast-transforming ability. In this study we have determined the abilities of both wild-type and C-terminally truncated (p90) forms of v-Abl to transform cells from p53(-/-) mice. Lack of p53 increases the susceptibility of bone marrow cells to transformation by v-Abl by a factor of more than 7 but does not alter v-Abl's preference for B220(+) IgM(-) pre-B cells. p53-deficient mice have earlier tumor onset, more rapid tumor progression, and decreased survival time following A-MuLV infection, but all of the tumors are pre-B lymphomas. Thus, p53-dependent pathways inhibit v-Abl transformation but play no role in conferring preferential transformation of pre-B cells. Surprisingly, the C-terminally truncated form of v-Abl (p90) transforms pre-B cells very efficiently in mice lacking p53, thus demonstrating that the C terminus of v-Abl does not determine preB tropism but is necessary to overcome p53-dependent inhibition of transformation.
Figures
FIG. 1
Influence of p53 phenotype on the survival of mice infected with A-MuLV-P160 or A-MuLV-P90A. (A) Neonatal mice were injected intraperitoneally with approximately 5 × 104 FFU of A-MuLV-P160. Infected mice were monitored daily for the appearance of disease symptoms. When disease became terminal, mice were sacrificed. The plot shows the probability of survival as a function of time (days) after infection. A total of 27 wild-type, 47 heterozygous, and 24 p53-deficient mice are represented. (B) Neonatal mice were injected intraperitoneally with approximately 5 × 104 FFU of A-MuLV-P90A. The infected mice were analyzed as for panel A. The plot shows the probability of survival as a function of time (days) after infection. A total of 16 wild-type, 21 heterozygous, and 12 p53-deficient mice are represented. (C) Schematic diagram of wild-type p160 v-Abl and C-terminally truncated mutant p90 v-Abl proteins. GAG, retroviral Gag domain; SH2, Src homology domain 2; SH1, tyrosine kinase domain; DB, DNA binding domain; AB, actin binding domain.
FIG. 2
v-Abl expression in tumors raised in p53-wild-type and -deficient mice injected with A-MuLV-P90A and clonality analyses of v-Abl-induced tumors in p53−/− mice. (A) Whole-cell extracts were prepared from tumor cells and control cells. Ten micrograms of each sample was resolved by SDS-PAGE on a 6% gel and subjected to Western blot analysis using antibody against Abl protein. Lanes: 1, A-MuLV-P160-induced tumor cells; 2, 1881 cells, which express p120v-abl; 3, NIH 3T3 cells (negative control); 4 to 9, six different tumors induced by A-MuLV-P90A in p53-deficient mice. (B) Samples were prepared and analyzed as for panel A. Lanes: 1, tumor induced by A-MuLV-P90A in p53−/− mice; 2 to 6, five different tumors induced by A-MuLV-P90A in p53+/+ mice. (C) Genomic DNA was prepared from primary A-MuLV-induced tumor tissue and subjected to Southern blot analysis. DNA (20 μg) was digested with _Eco_RI, electrophoresed through 0.8% agarose gel, blotted to nitrocellulose paper, and hybridized to the 32P-labeled _abl_-specific probe. Lanes: 1, A-MuLV-P160-induced tumor in p53−/− mouse; 2 to 4, A-MuLV-P90A-induced p53−/− tumors from different individual mice. An arrow indicates the 27-kb c-_abl_-specific band present in all cells.
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