Inhibition of DNA binding of purified p55v-myc in vitro by antibodies against bacterially expressed myc protein and a synthetic peptide.

Bunte, T.; Donner, Peter; Pfaff, Eberhard; Reis, Bettina; Greiser‐Wilke, I.; Schaller, Heinz; Moelling, Karin

doi:10.1002/j.1460-2075.1984.tb02068.x

Cited by 26 publications

(23 citation statements)

References 26 publications

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“…These lanes also show additional virus structural proteins precipitated by anti-p30 as expected for helpervirus-producing cells. Expression of v-myc was determined by immunoprecipitation with two different anti-myc sera, a synthetic peptide serum [Sl] and a serum raised against myc protein produced in Escherichia coli [53]. v-myc-specific bands corresponding to a 62K protein were detected only in 5-2 virus-transformed cells (panel A, lanes b 4-6).…”

Section: Expression Of V-raf-and V-myc-specific Products In Cells Tramentioning

confidence: 99%

Interaction between Raf and Myc oncogenes in transformation in vivo and in vitro

Cleveland

Jansen

Bister

et al. 1986

J of Cellular Biochemistry

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3611 MSV, a raf-oncogene-transducing murine retrovirus, induces fibrosarcomas and erythroid hyperplasia in newborn mice after a latency of 4-8 wk. In contrast, new recombinant murine retroviruses carrying the myc oncogene (J-3, J-5 construct viruses) do not induce tumors before greater than 9 wk. A combination of both oncogenes in an infectious murine retrovirus (J-2) induces hematopoietic neoplasms in addition to less prominent fibrosarcomas and pancreatic adenocarcinoma 1-3 wk after inoculation. The hematologic neoplasms consist of immunoblastic lymphomas of T and B cell lineage and erythroblastosis. If animals were inoculated with a variant of the J-3 virus, which induces altered foci in cultures of NIH 3T3 cells, carcinoma developed in the pancreas with a 2-6 mo latency. In parallel to the synergistic action of both oncogenes on hematopoietic cells in vivo, we find that raf-oncogene-induced transformation of bone marrow cells in culture is enhanced by the addition of myc, which by itself does not transform these cells when grown in standard media. We conclude that concomitant expression of raf and myc oncogenes in hematopoietic and epithelial cells alters their respective transforming activities. The contribution of v-myc in this synergism was examined by use of a series of recombinant murine retroviruses capable of expressing the avian v-myc to study the effect of altered myc expression on hematopoietic/lymphoid cells. With either interleukin 3- or interleukin 2-dependent cell lines, introduction of the recombinant viruses abrogated the requirement for IL 3 or IL 2 for growth, and associated with this was the suppression of c-myc expression. The findings suggest that myc is a component in the signal transduction pathway for IL 3 and IL 2 and support an autoregulatory mechanism of c-myc expression. In contrast to v-myc, expression of v-raf in primary lymphoid/hematopoietic cells has an immortalizing function without abrogating the requirement for IL 3 for growth. This suggests that v-raf and v-myc affect different components of growth regulation, as, for example, commitment (v-myc) and cell cycle progression (v-raf).

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Section: Expression Of V-raf-and V-myc-specific Products In Cells Tramentioning

confidence: 99%

Interaction between Raf and Myc oncogenes in transformation in vivo and in vitro

Cleveland

Jansen

Bister

et al. 1986

J of Cellular Biochemistry

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“…Little is known about the proteins encoded by the c-myc gene, and antibodies raised against c-myc gene products or sequences have only recently been described (3,9,21,22,34,38). Like the virally encoded v-myc-transforming proteins (1,9,15,16), the c-myc gene product is a nuclear, DNA-binding protein (16,35).…”

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confidence: 99%

“…Like the virally encoded v-myc-transforming proteins (1,9,15,16), the c-myc gene product is a nuclear, DNA-binding protein (16,35). The antibodies described thus far recognize two or possibly three structurally related human proteins with an approximate molecular weight of 65,000 in sodium dodecyl sulfate (SDS)-polyacrylamide gels (22,34,38).…”

mentioning

confidence: 99%

Growth-dependent synthesis of c-myc-encoded proteins: early stimulation by serum factors in synchronized mouse 3T3 cells.

Persson¹,

Gray²,

Godeau³

1985

Mol. Cell. Biol.

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Synthesis of the c-myc gene product was measured during the entire cell cycle of subconfluent mouse 3T3 cells with an antibody raised against a human c-myc synthetic peptide. The antiserum recognized two mouse c-myc-encoded proteins with apparent molecular weights in sodium dodecyl sulfate-polyacrylamide gels of 62,000 and 60,000. Cell-derived p62 was compared with the mouse c-myc gene product synthesized in vitro. Immunoprecipitation, electrophoretic analyses, and peptide mapping provided evidence that p62 is encoded by the mouse c-myc gene. The rate of synthesis of the c-myc proteins was tightly coupled to the cellular growth state of nontransformed A31 3T3 cells, but not to that of their benzo(a)pyrene-transformed derivative (BPA31). Furthermore, the synthesis of the c-myc proteins was stimulated by the exposure of confluent, density-arrested A31 cells to platelet-derived growth factor or fibroblast growth factor. Tightly synchronized cell populations were obtained on the addition of serum factors to subconfluent, serum-deprived A31 cells, and c-myc expression could be monitored for more than one complete cell cycle. One hour after stimulation the steady-state level of the 2.2 kilobase c-myc transcript increased 30-fold relative to that of quiescent cells and decreased thereafter to the level observed during exponential growth. The rate of synthesis of c-myc-encoded proteins was determined by immunoprecipitation after a 2-h labeling period. After an initial sevenfold increase detectable 2 h after serum addition, the rate of synthesis remained constant throughout the rest of the cell cycle. No further changes associated with the late prereplicative period, S phase, G2, or mitosis could be demonstrated. Pulse-chase and long-term labeling experiments revealed different half-lives for the two c-myc-encoded proteins. The half-lives of the c-myc proteins, however, were independent of the cellular growth state. The sustained expression observed throughout the cell cycle suggests that the growth-related function of c-myc may be required during the GO-GI transition and in all phases of the cycle of the growing cell.

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“…1 and 2 and reference 28). In (3,9,12,15), the apparent molecular masses in SDS-PAGE were 10 to 15 kDa larger than expected from the predicted nucleotide sequence. This paradox can result from posttranslational modifications of the v-and c-myc proteins, anomalous protein migration during SDS-PAGE, or both.…”

Section: Discussionmentioning

confidence: 64%

Multiple growth-associated nuclear proteins immunoprecipitated by antisera raised against human c-myc peptide antigens.

Persson¹,

Gray²,

Godeau³

et al. 1986

Mol. Cell. Biol.

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Different antisera raised against various regions of the human c-myc protein were used to identify four human c-myc proteins with apparent molecular masses in sodium dodecyl sulfate-polyacrylamide gels ranging from 64 to 68 kilodaltons (phosphoproteins pp64 and pp67 and nonphosphorylated proteins p65 and p68). pp64 and p65 were the major detectable c-myc proteins, and pp67 and p68 were minor but specific components of the immunoprecipitates. The c-myc proteins were all localized in the cell nucleus. Accumulation of[35S]methionine-labeled p65 was observed after pulse-labeling and chase, suggesting that the stable p65 c-myc protein is generated posttranslationally from short-lived precursors. pp64, pp67, and p68 possessed short half-lives and may therefore be precursors of the stable p65. Confirmation of the nuclear localization of the human c-myc proteins was obtained by immunofluorescent staining. The human c-myc proteins were revealed as a pattern of punctate nuclear staining with, particularly for p65, nucleolar enhancement that left an unstained annulus surrounding the nucleolus.

show abstract

Inhibition of DNA binding of purified p55v-myc in vitro by antibodies against bacterially expressed myc protein and a synthetic peptide.

Cited by 26 publications

References 26 publications

Interaction between Raf and Myc oncogenes in transformation in vivo and in vitro

Interaction between Raf and Myc oncogenes in transformation in vivo and in vitro

Growth-dependent synthesis of c-myc-encoded proteins: early stimulation by serum factors in synchronized mouse 3T3 cells.

Multiple growth-associated nuclear proteins immunoprecipitated by antisera raised against human c-myc peptide antigens.

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