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PubMedDate not supplied

[Evolutionary variants of the mos gene].

The occurence of members of mos oncogene family in the vertebrates genome has been studied with the help of highly labeled single-stranded DNA probes. These included subgenic v-mos clones as well as the unique sequence--specific recombinants from mos-related human locus gp5 and the K51 locus from rat genome. The probe from gp5 (mos pseudogene) interacts only with DNA of primates and of rodents. On the other hand, mos gene and the gene from K51 locus are present in all vertberates tested. Recent duplication of the main mos gene in Artiodactyla and Perissodactyla orders of mammals was identified. The persistence of K51 and mos genes during evolution indicates their importance. The segregation of three mos-related genes in human-hamster hybrids points to their location on different human chromosomes.

Animals↗

PubMed1997

Effects of gonadotropin, estrogen, and progesterone on c-mos gene expression in mouse oocytes in vivo and in vitro.

OBJECTIVE: To analyze the effects of gonadotropin and ovarian steroid hormones on the gene expression of c-mos in mouse oocytes. METHODS: The changes of c-mos messenger RNA (mRNA) levels in oocytes were examined after the administration of pregnant mare's serum gonadotropin (PMSG) in vivo, or after incubation with estrogen and/or progesterone in vitro. Five IU PMSG was injected intraperitoneally to female immature mice, and human chorionic gonadotropin was also injected intraperitoneally 48 hours after the PMSG injection, with or without mating with male mice. The oocytes were collected from follicles or oviducts at 24, 30, 36, 42, 48, 60, 72, and 84 hours after the injection. The RNAs were extracted from 5 oocytes at each time point, and a reverse-transcription polymerase chain reaction using specific primers to c-mos DNA was performed to measure the relative amount of c-mos mRNA. RESULTS: The c-mos mRNA in oocytes at 36 hours after the injection was 2.7 times higher than that at 24 hours. The c-mos mRNA level gradually decreased thereafter, and after ovulation the level was only 1/10 of the peak level. When the oocytes that were retrieved 24 hours after PMSG injection were incubated with 800 ng/ml estradiol 17-beta or 600 ng/ml progesterone for 120 minutes, the c-mos gene expression was significantly suppressed or stimulated, respectively, in comparison with the absence of these substances. CONCLUSION: Although the regulatory mechanism of c-mos gene expression in oocytes is still unclear because the result obtained from the in vitro study, that estrogen suppressed the c-mos gene expression directly, was inconsistent with the result of the in vivo study, that increases of both c-mos mRNA and estrogen occurred simultaneously with PMSG stimulation in the early phase of preovulatory oocytes, our present study revealed that gonadotropin and steroid hormones might affect c-mos gene expression in mouse oocytes indirectly and/or directly.

Animals↗

PubMed1998

Paclitaxel-induced apoptosis is associated with expression and activation of c-Mos gene product in human ovarian carcinoma SKOV3 cells.

The c-Mos gene product is a component of the cytostatic factor and, as such, stabilizes the maturation-promoting factor causing cell-cycle blockade at metaphase II in unfertilized eggs. The potential role of c-Mos in regulating cell-cycle progression and cell death in somatic cells remains unknown. We studied whether paclitaxel-induced M-phase arrest and apoptosis are associated with c-Mos gene expression and activation in SKOV3 ovarian carcinoma cells. The first cellular effect observed with continuous exposure to 50 ng/ml paclitaxel (ID50) was mitotic arrest with an increase in the accumulation of cyclin B1 and stimulation of cdc2/cyclin B1 kinase in a time-dependent manner during a 36-h incubation. DNA fragmentation determined by agarose gel electrophoresis and quantitation of [3H]thymidine-prelabeled genomic DNA was a later event, first detected at 24 h and peaking at 48 h (later time points were not studied). Induction of the c-Mos gene expression and activation were determined by Western blot analysis, immunoprecipitation using a polyclonal anti-mos antibody, reverse transcription-PCR assay, and 32P-ATP incorporation into c-Mos protein or the substrate of glutathione S-transferase mitogen-activated protein kinase kinase, respectively. Both induction and activation were clearly detected after 24 h of exposure to paclitaxel concentrations of >50 ng/ml, coinciding with drug-induced apoptosis. Mitogen-activated protein kinase activation preceded c-Mos gene induction. Paclitaxel-induced c-Mos gene expression was completely abrogated by cycloheximide and actinomycin D. Mos gene expression was also induced in SKOV3 cells that were treated with vinblastine but not in those that were treated with camptothecin, etoposide, or cisplatin. We concluded that tubulin-disturbing agents induce c-Mos gene expression and activation in SKOV3 ovarian carcinoma cells and that such an effect occurs after mitotic blockade and coincides with drug-induced apoptosis.

Antineoplastic Agents, Phytogenic↗

PubMed1985

Recognition of mos-related proteins with an antiserum to a peptide of the v-mos gene product.

A mos-specific antiserum was generated by injection of rabbits with a peptide predicted from the sequence of the v-mos gene of Moloney murine sarcoma virus (MuSV) strain 124. The peptide is composed of amino acids 37-55 (cyclized at the cysteine residues) conjugated to keyhole limpet haemocyanin. This serum [anti-mos(37-55c)] specifically recognized p37mos in MuSV-124 acutely infected NIH-3T3 cells, P85gag-mos in 6m2 cells, an NRK clone infected with the temperature-sensitive mutant (ts110) of Moloney MuSV, and P100gag-mos in 54-5A4 cells, an NRK clone infected with a spontaneous revertant of ts110. An additional protein of Mr 55000 from uninfected cells was recognized by this serum. Reactivity of the serum toward the v-mos-containing proteins and the 55K protein was completely inhibited by prior incubation with free peptide. The 55K protein was not recognized by antisera made from synthetic peptides prepared from the C-terminal eight or 12 amino acids of v-mos.

Animals↗

PubMedDate not supplied

[Regions of human genome containing analogs of oncogenes and retrovirus genes. I. A family of c-mos genes and unusual structure of ORA-gp5 locus].

The structural organization of a number of recombinant phages previously selected from the human gene library has been studied. On the basis of comparison of physical maps and hybridization to cloned probes it was deduced that different human loci with the homology to v-mos are represented in lambda recombinants. The physical map of the cloned region of the human genome designated as ORA-gp5 was constructed. The sequences of three different genetical elements v-mos-related oncogene, mammalian type C retrovirus and Alu type repeat are interspersed in this structure. The hypothesis concerning the probable origin of this locus has been proposed. The mosaical structure of ORA-gp5 could be the result of the integration of mammalian retrovirus in the vicinity to c-mos gene with subsequent recombination and transposition. The resulting potentially oncogenic structure was later inactivated by the integration of Alu-type repeats.

Animals↗

PubMed1995

Mutations in the v-mos gene abolish its ability to induce differentiation but not transformation.

The v-mos oncogene product has the ability to induce differentiation in human monocytic leukemia U937 cells, thereby arresting cell proliferation, and also exhibits transforming activity in mouse NIH3T3 cells. Mutation in the v-mos gene consisting of one or two amino acid substitutions in the putative ATP-binding domain impaired its differentiation-inducing activity although mutant proteins showed rather higher levels of autophosphorylation in vitro. Macrophage-specific characteristics such as their morphology, expression of C3b receptor and Fc receptor, and production of interleukin-1 beta and tumor necrosis factor alpha, were equally diminished in cells transfected with mutant mos genes when compared to those with intact v-mos. The ability of the gene to arrest the proliferation of U937 cells was likewise diminished, while the transforming efficiency of the intact and mutant mos genes were essentially the same. These results suggest that the mos product functions differently in cell differentiation and transformation.

3T3 Cells↗

PubMed1985

Nucleotide sequence and biochemical activities of the Moloney murine sarcoma virus strain HT-1 mos gene.

The nucleotide sequence of the Moloney murine sarcoma virus strain HT-1 (HT1MSV) mos gene differs from that of the cellular mos gene in three positions, but these are silent changes, and the amino acid sequence of the v-mos and c-mos open reading frames are identical. We have overproduced the mos HT1MSV (equivalent to c-mos) in Escherichia coli under the control of phage lambda promoter (pL). The E. coli p40mos protein thus obtained was partially purified and examined for several biochemical activities. We show that the p40mos binds ATP analog p-fluorosulfonylbenzoyladenosine and exhibits ATPase activity.

Adenosine Triphosphatases↗

PubMed1982

Demonstration of biological activity and nucleotide sequence of an in vitro synthesized clone of the Moloney murine sarcoma virus mos gene.

A clone of the Moloney murine sarcoma virus mos gene derived by in vitro reverse transcription was characterized. When assayed for focus formation by DNA transfection on NIH/3T3 cells, this clone was biologically inactive, presumably due to the absence of a long terminal repeat sequence. Therefore, a long terminal repeat was inserted into the clone by in vitro recombination, after which the most gene was able to transform NIH/3T3 cells efficiently. The nucleotide sequence encompassing the transforming region of this clone was determined. A single long open reading frame was observed, which potentially encodes a polypeptide of 41,000 daltons. This open reading frame initiates with the first five amino acids of the murine leukemia virus env gene, after which it enters the mos sequence, where it terminates. The nucleotide sequence described in this paper was compared with other sequences of mos in an effort to resolve discrepancies in the position of the long open reading frame. Although Moloney murine sarcoma virus retains the 3' splicing site of the murine leukemia virus env gene, a mos-specific mRNA which corresponds structurally to the murine leukemia virus env mRNA was not identified. The sequence described here revealed a single nucleotide change in the proposed env gene 3' splicing site which was retained in Moloney murine sarcoma virus. This deviation from the consensus 3' splicing sequence may underlie the observed absence of mos expression via the env gene splicing pathway.

Animals↗

PubMed1983

Tight linkage of retroviral-like sequences to a variant human c-mos gene in the human genome.

Chumakov et al. [Gene 17 (1982) 19-26] identified in the human gene library a number of recombinant phages that possess a homology to the v-mos gene. Here we report the unusual structure of one of these recombinants, lambda gp5. The 14.3-kb stretch of human DNA from this phage contains at least three regions of homology to the v-mos gene, together with multiple copies of Alu-family repeats. Moreover, we have shown the presence of retrovirus-related sequences in the close vicinity of the mos-homologous regions. These data point to the possibility of involvement of retrovirus in the process of c-mos gene amplification during the formation of a multigene family.

Gene Amplification↗

PubMed1991

mos gene transforming efficiencies correlate with oocyte maturation and cytostatic factor activities.

The mos proto-oncogenes from different vertebrate species transform mouse NIH 3T3 cells with markedly different efficiencies. v-mos, mouse (c-mosmu), and chicken (c-mosch) mos transform NIH 3T3 cells 10- to 100-fold more efficiently than do human (c-moshu) and Xenopus (c-mosxc) mos. The mos genes with the highest transforming activity efficiently induce maturation in Xenopus oocytes and mimic cytostatic factor (CSF) by causing mitotic cleavage arrest in embryos. Chimeric v-mos/c-moshu proteins that had high transforming efficiencies in NIH 3T3 cells were also effective in the induction of oocyte maturation and CSF cleavage arrest. We measured the in vitro autophosphorylation activities of the different mos proteins and found that the levels of kinase activity of v-mos, c-mosmu, and c-mosch were much higher than that of c-mosxc. These data indicate that mos gene transforming efficiency and the ability to induce oocyte maturation or mimic CSF activity are correlated with in vitro autophosphorylation activity and suggest that the mos protein plays a similar role in transformed cells and normal oocytes.

Animals↗

PubMed1995

[Interaction between genes Mos and mwh expressed in somatic cells of Drosophila melanogaster].

Gene Mosaic (Mos) of chromosome 3 of Drosophila melanogaster was located by means of dominant markers Ly, Sb, and Dr. This gene was shown to be located between Ly and Sb in the centromeric region (45-50 map units). An analysis of interaction between Mos and mwh genes in cis and trans-heterozygotes showed a significant effect of the Mos gene on mutability (recombinogenesis) of chromosome mwh in somatic cells. In the cis heterozygote mwh Mos/++, the frequency of small mutant clones on wings of flies increased. In mwh/Mos heterozygotes, the Mos gene caused a significant reduction of dorsocentral and scutellar bristles (78% in mwh/Mos, 85% in mwh +/+ Mos, and 98% in mwh Mos/mwh +).

Animals↗

PubMed1997

R7, a spontaneous mutant of Moloney murine sarcoma virus 124 with three direct repeats and an in-frame truncated gag-mos gene, induces brain lesions.

We have isolated Recombinant 7 (R7), a spontaneous mutant of SV7, a molecular clone of MoMuSV124. Like SV7, R7 induces subcutaneous fibrosarcomas, spleen tumors, and mesentery tumors infiltrated by proliferating vessels lined by transformed endothelial cells. However, it also induces brain lesions. We have molecularly cloned and sequenced the R7 proviral DNA and shown that the R7 genome consists of 3401 bp. It has three direct repeats in each enhancer. Its coding sequence consists of only 176 bp of p15, 263 bp of p30, a 7-bp insertion, and 853 bp of an N-terminally truncated mos gene. From the sequence of R7 we have deduced that the truncated mos sequence is in-frame with all of the gag sequence and the 7-bp insertion. The incorporation of the 3' end of the p15 sequence further suggests that the R7 Gag-Mos is myristylated. We have also shown that the molecularly cloned R7 virus transformed NIH/3T3 fibroblasts about sevenfold better than the parental SV7. We have also confirmed that molecularly cloned R7 induces the same disease phenotype as that induced by the nonmolecularly cloned R7.

Amino Acid Sequence↗

PubMed1983

Expression of cellular myc and mos genes in undifferentiated B cell lymphomas of Burkitt and non-Burkitt types.

Burkitt lymphomas contain reciprocal translocations between chromosome 8 and one of the chromosomes containing the immunoglobulin gene loci, prompting speculation that consequent activation of a crucial gene(s) on chromosome 8 might be involved in the generation of these tumors. Recently the human counterparts of the retroviral oncogenes v-myc and v-mos have been mapped to chromosome 8. We have, therefore, analyzed the level of transcription of the cellular myc and mos genes in a variety of undifferentiated B cell lymphomas of Burkitt and non-Burkitt type that possess either an 8;14 or an 8;22 translocation. These lines expressed 2- to 5-fold more myc-specific RNA than do B cell lines without a translocation. Tumor cell lines of American origin with an 8;14 or 8;22 translocation expressed similar amounts of myc-specific RNA. Tumor cell lines of African origin contained slightly higher levels of myc-specific RNA than did those of American origin. However, level of expression does not appear to correlate with the presence or absence of Epstein-Barr virus. Therefore, a major increase in the transcription of this gene secondary to translocation is unlikely to be the cause of Burkitt lymphoma. There was no evidence of mos-related transcripts in any of the cell lines tested.

Burkitt Lymphoma↗

PubMed1987

Synthesis of specific transformation-associated proteins (TAPs) in two rat cell lines is closely related to the expression of the v-mos gene product of Moloney murine sarcoma virus (Mo-MSV).

The 6M2 cell line was established by transformation of normal rat kidney cells with the ts110 mutant of Moloney murine sarcoma virus (Mo-MSV). P85gag-mos was found to be the only known viral-transforming protein in this cell system. Previously, we described the detection in 6M2 cells of rat-specific transformation-associated proteins (TAPs) using a monoclonal antibody (MC). In this study, we used MC to investigate further the expression of TAPs at different temperatures and the time course of turn-on and shut-off of TAPs upon temperature shifting. It was found that TAPs were expressed at 24, 28 and 33 degrees C, but not at 37 and 39 degrees C. In experiments of temperature shifting, TAPs reappeared in about 6 h in 6M2 cells after the temperature was shifted from 39 to 33 degrees C, following closely the reappearance of P85gag-mos. The data in this communication support the notion that TAPs might be activated by the v-mos gene product during the process of transformation.

Animals↗

PubMed2006

Extensive intraspecific polymorphism detected by SSCP at the nuclear C-mos gene in the endemic Iberian lizard Lacerta schreiberi.

C-mos is a highly conserved intronless gene that has proved useful in the analysis of ancient phylogenetic relationships within vertebrates. We selected the Iberian endemic Schreiber's green lizard (Lacerta schreiberi) that persisted in allopatric refugia since the late Pliocene to investigate the utility of the C-mos nuclear gene for intraspecific phylogeographic studies. Our combination of DNA sequencing with the high resolving power of single-strand conformational polymorphism (SSCP) effectively discriminated four common alleles showing strong population structuring (F(ST) = 0.46). In addition, reconstruction of allele phylogenetic relationships further improved our understanding of C-mos spatial patterns of variation and allowed a comparison with previously described mitochondrial DNA data. Finally, limited sequencing of an extended C-mos fragment in six additional Lacerta species showed extensive polymorphism, to our knowledge representing a rare example of variation in a highly conserved nuclear gene.

Amino Acid Sequence↗

PubMed1992

Characterization of activated and normal mouse Mos gene in murine 3T3 cells.

We have characterized the mouse Mos proto-oncogene product, pp39Mos, in murine fibroblasts. When expressed in NIH3T3 cells under the influence of the long terminal repeat regulatory element from Moloney murine sarcoma virus [NIH(pTS-1) cells], the Mos protein was present in low levels and had a half-life of about 30 min. In extracts from NIH(pTS-1) cells, we detected additional forms of Mos protein that apparently arose from internal initiation codons (p24Mos and p29Mos) or from upstream non-AUG initiation codons (p42Mos and p44Mos). The Mos protein was found to exist in these cells as a phosphoprotein, pp39Mos, and, when immunoprecipitated with an antiserum specific for the Mos N-terminus [anti-Mos(6-24)], had autophosphorylating kinase activity. We found that anti-Mos(6-24) also detected non-Mos protein kinase activity and non-Mos phosphoproteins in addition to p39Mos. We present evidence, on both the RNA and protein levels, that non-transformed mouse 3T3 cells do not express endogenous Mos.

3T3 Cells↗

PubMed1986

Expression of the v-mos gene alters a Mr 55,000 protein during acute infection by Moloney murine sarcoma virus.

Infection of the rat myoblast cell line, L6E9, with Moloney murine sarcoma virus (Mo-MuSV) clone 124, altered a cellular protein of Mr 55,000 (P55) within 2 days of infection. The alteration of P55 was observed as a reduction in its steady-state level in cell extracts. The reduction of P55 correlated with the appearance of p37mos in infected cells. Except for P55 and one other protein, no change was detected in the total protein pattern of infected cells compared to uninfected cells, as judged by either immunoblots of one-dimensional NaDodSO4 gels or direct two-dimensional gel analysis. P55 levels were unchanged when L6E9 cells were infected with Moloney murine leukemia virus or several different transforming retroviruses. To determine the specificity of this v-mos-induced effect on P55, L6E9 cells were acutely infected with a temperature-sensitive variant (ts110) of Mo-MuSV. When these cells were shifted from 39 degrees C to 33 degrees C, which activates the gag-mos gene product, the P55 level dropped by greater than 50% within 2-3 hr. Conversely, with a shift in temperature from 33 degrees C to 39 degrees C, the cells' P55 level returned to normal within 5 hr, starting at 30 min after shift. These results clearly show that v-mos expression in acutely infected L6E9 cells alters the cellular protein, P55.

Animals↗

PubMed1985

The role of the c-mos gene in the 8;21 translocation in human acute myeloblastic leukemia.

The human c-mos proto-oncogene is located on chromosome 8 at band q22, close to the breakpoint in the t(8;21) (q22;q22) chromosome rearrangement. This translocation is associated with acute myeloblastic leukemia, subgroup M2. The c-myc gene, another proto-oncogene, has been mapped to 8q24. The breakpoint at 8q22 separates these genes, as determined by in situ hybridization of c-mos and c-myc probes. The c-mos gene remains on the 8q-chromosome and the c-myc gene is translocated to the 21q+ chromosome. Southern blot analysis of DNA from bone marrow cells of four patients with this translocation showed no rearrangement of c-mos.

Chromosome Mapping↗