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  • 1
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    The product of the mos proto-oncogene as a candidate "initiator" for oocyte maturation (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-08-11
    Description: The endogenous c-mos product, pp39mos, is required for progesterone-induced meiotic maturation in Xenopus oocytes. Treatment of oocytes with progesterone induced a rapid increase in pp39mos that preceded both the activation of maturation promoting factor (MPF) and germinal vesicle breakdown (GVBD). Microinjection of synthetic mos RNA into oocytes activated MPF and induced GVBD in the absence of progesterone. Thus, the mos proto-oncogene product may qualify as a candidate "initiator" protein of MPF and is at least one of the "triggers" for G2 to M transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sagata, N -- Daar, I -- Oskarsson, M -- Showalter, S D -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1989 Aug 11;245(4918):643-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BRI-Basic Research Program, National Cancer Institute, Frederick Cancer Research Facility, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2474853" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cycloheximide/pharmacology ; Female ; Growth Substances/physiology ; Kinetics ; Maturation-Promoting Factor ; Meiosis/drug effects ; Microinjections ; Oocytes/*physiology ; Progesterone/pharmacology ; Protein Biosynthesis ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins c-mos ; RNA/genetics ; Transcription, Genetic ; Transfection ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Ability of the c-mos product to associate with and phosphorylate tubulin (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-02-08
    Description: The mos proto-oncogene product, pp39mos, is a protein kinase and has been equated with cytostatic factor (CSF), an activity in unfertilized eggs that is thought to be responsible for the arrest of meiosis at metaphase II. The biochemical properties and potential substrates of pp39mos were examined in unfertilized eggs and in transformed cells in order to study how the protein functions both as CSF and in transformation. The pp39mos protein associated with polymers under conditions that favor tubulin oligomerization and was present in an approximately 500-kilodalton "core" complex under conditions that favor depolymerization. beta-Tubulin was preferentially coprecipitated in pp39mos immunoprecipitates and was the major phosphorylated product in a pp39mos-dependent immune complex kinase assay. Immunofluorescence analysis of NIH 3T3 cells transformed with Xenopus c-mos showed that pp39mos colocalizes with tubulin in the spindle during metaphase and in the midbody and asters during telophase. Disruption of microtubules with nocodazole affected tubulin and pp39mos organization in the same way. It therefore appears that pp39mos is a tubulin-associated protein kinase and may thus participate in the modification of microtubules and contribute to the formation of the spindle. This activity expressed during interphase in somatic cells may be responsible for the transforming activity of pp39mos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhou, R P -- Oskarsson, M -- Paules, R S -- Schulz, N -- Cleveland, D -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Feb 8;251(4994):671-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ABL-Basic Research Program, NCI-Frederick Cancer Research and Development Center, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1825142" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal ; Cell Line ; Cell Transformation, Neoplastic/metabolism ; Macromolecular Substances ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Phosphoproteins/metabolism ; Precipitin Tests ; Protein Binding ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-mos ; Tubulin/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor (1998)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1998-05-23
    Description: Anthrax lethal toxin, produced by the bacterium Bacillus anthracis, is the major cause of death in animals infected with anthrax. One component of this toxin, lethal factor (LF), is suspected to be a metalloprotease, but no physiological substrates have been identified. Here it is shown that LF is a protease that cleaves the amino terminus of mitogen-activated protein kinase kinases 1 and 2 (MAPKK1 and MAPKK2) and that this cleavage inactivates MAPKK1 and inhibits the MAPK signal transduction pathway. The identification of a cleavage site for LF may facilitate the development of LF inhibitors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Duesbery, N S -- Webb, C P -- Leppla, S H -- Gordon, V M -- Klimpel, K R -- Copeland, T D -- Ahn, N G -- Oskarsson, M K -- Fukasawa, K -- Paull, K D -- Vande Woude, G F -- New York, N.Y. -- Science. 1998 May 1;280(5364):734-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Advanced BioScience Laboratories-Basic Research Program, National Cancer Institute-Frederick Cancer Research and Development Center, Post Office Box B, Frederick, MD 21702.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9563949" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, Bacterial ; *Bacillus anthracis/enzymology ; Bacterial Toxins/metabolism/*toxicity ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cell Line, Transformed ; Enzyme Activation ; Enzyme Inhibitors/toxicity ; Humans ; MAP Kinase Kinase 1 ; MAP Kinase Kinase 2 ; Metalloendopeptidases/metabolism/toxicity ; Mice ; *Mitogen-Activated Protein Kinase Kinases ; Myelin Basic Protein/metabolism ; Oocytes/physiology ; Phosphorylation ; Protein-Serine-Threonine Kinases/*antagonists & ; inhibitors/chemistry/genetics/metabolism ; Protein-Tyrosine Kinases/*antagonists & inhibitors/chemistry/genetics/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Deletion ; Signal Transduction ; Xenopus laevis
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 4
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    Properties of a normal mouse cell DNA sequence (sarc) homologous to the src sequence of Moloney sarcoma virus (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-03-14
    Description: A 15.0-kilobase (kb) Eco RI DNA fragment from normal mouse Balb/c genomic DNA that contains sequences (sarc) homologous to the acquired cell sequences (src) of Moloney sarcoma virus (MSV) has been cloned in phage lambda. The sarc region (1.2 to 1.3 kb) of the 15.0-kb cell fragment is indistinguishable from the src region of two isolates of MSV as judged by heteroduplex and restriction endonuclease analyses. The cellular sequences flanking sarc show no homology to other MSV sequences. Whereas cloned subgenomic portions of MSV that contain src transformed NIH-3T3 cells in vitro, the cloned sarc fragment is inactive.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Oskarsson, M -- McClements, W L -- Blair, D G -- Maizel, J V -- Vande Woude, G F -- New York, N.Y. -- Science. 1980 Mar 14;207(4436):1222-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6243788" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Chromosome Mapping ; DNA Restriction Enzymes ; *Genes ; *Genes, Viral ; Mice ; Mice, Inbred BALB C/*genetics ; Moloney murine leukemia virus/*genetics ; Nucleic Acid Hybridization
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 5
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    New method for detecting cellular transforming genes (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-12-10
    Description: Tumor induction in athymic nude mice can be used to detect dominant transforming genes in cellular DNA. Mouse NIH 3T3 cells freshly transfected with either cloned Moloney sarcoma proviral DNA or cellular DNA's derived from virally transformed cells induced tumors when injected into athymic nu/nu mice. Tumors were also induced by cells transfected with DNA from two tumor-derived and one chemically transformed human cell lines. The mouse tumors induced by human cell line DNA's contained human DNA sequences, and DNA derived from these tumors was capable of inducing both tumors and foci on subsequent transfection. Tumor induction in nude mice represents a useful new method for the detection and selection of cells transformed by cellular oncogenes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blair, D G -- Cooper, C S -- Oskarsson, M K -- Eader, L A -- Vande Woude, G F -- New York, N.Y. -- Science. 1982 Dec 10;218(4577):1122-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6293052" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Transformation, Viral ; DNA, Neoplasm/*genetics ; DNA, Viral/genetics ; Mice ; Mice, Nude/*physiology ; Moloney murine leukemia virus/genetics ; Neoplasms, Experimental/*genetics ; *Oncogenes ; Sarcoma Viruses, Murine/genetics
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 6
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    Activation of the transforming potential of a normal cell sequence: a molecular model for oncogenesis (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-05-22
    Description: The molecularly cloned, long terminal repeat (LTR) of the Moloney sarcoma virus (M-MSV) provirus has been covalently linked to c-mos, the cellular homolog of the M-MSV-specific sequence, v-mos. These newly constructed clones lack any M-MSV-derived sequences other than the LTR, but in DNA transfection assays they transform cells as efficiently as cloned subgenomic M-MSV fragments containing both v-mos and LTR. Cells transformed by LTR:c-mos hybrid molecules contain additional copies of mos DNA, and several size classes of polyadenylated RNA's with sequence homology to mos. The activation of the transforming potential of c-mos by the proviral LTR suggests a model whereby LTR-like elements could activate other normal cell sequences with oncogenic potential.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blair, D G -- Oskarsson, M -- Wood, T G -- McClements, W L -- Fischinger, P J -- Vande Woude, G G -- New York, N.Y. -- Science. 1981 May 22;212(4497):941-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7233190" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Transformation, Viral ; Cells, Cultured ; DNA, Recombinant ; Defective Viruses/genetics ; Gene Expression Regulation ; *Genes, Viral ; Mice ; Moloney murine leukemia virus/*genetics ; Nucleic Acid Hybridization ; Operon ; Plasmids
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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