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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Macromolecules 27 (1994), S. 4705-4713 
    ISSN: 1520-5835
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4919
    Keywords: mitogenesis ; insulin ; tyrosine phosphorylation ; phosphatase ; neoplastic transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Insulin selectively induces mitogenesis in quiescent SV40 large T antigen-transformed murine 3T3T (CSV3-1) cells but not in quiescent nontransformed 3T3T cells. This mitogenic effect induced by insulin in CSV3-1 cells requires an induction of AP-1 activity associated with c-Jun and JunB. To further investigate the mechanisms that are involved in insulin-induced mitogenesis in CSV3-1 cells, the current experiments were performed. The results show that following insulin stimulation, the insulin receptor β-subunit and the insulin receptor substrate-1 undergo a much more significant tyrosine phosphorylation in CSV3-1 cells than in 3T3T cells. Insulin also induces tyrosine phosphorylation of a 73 kDa protein that is coprecipitated with the tyrosine-phosphorylated insulin receptor in CSV3-1 cells but not in 3T3T cells. The increased tyrosine phosphorylation in response to insulin stimulation in CSV3-1 cells does not appear to be due to an increase in the level of expression of the insulin receptor and does not appear to result from a significant change in tyrosine phosphatase activity compared to nontransformed cells. The results also show that the insulin effect in CSV3-1 cells is not mediated by insulin-like growth factor 1 receptor because insulin at the concentrations that induce mitogenesis does not increase the tyrosine phosphorylation of the insulin-like growth factor 1 receptor and the expression level of the receptor is not significantly changed in CSV3-1 cells compared to nontransformed cells. These data together indicate that the selective mitogenic effect of insulin on CSV3-1 cells involves increased tyrosine phosphorylation of the insulin receptor, the insulin receptor substrate-1 and the 73 kDa protein, although the underlying mechanisms need to be further elucidated.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] FIG. 1 a, The cyclic macromolecule 1 is composed of randomly attached side chains of the mesogen cholesteryl-4-allylox-ybenzoate (80mol%) and the NLO-active chromophore 3-methyl-4-allyloxy-4'-nitrostilbene (20mol%), that is, (n) = 4, (m) = 1. The chromophore was prepared by reacting allyl bromide ...
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1573-4919
    Keywords: AP-1 ; insulin ; vanadate ; gene regulation ; cell proliferation ; protooncogenes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Insulin and vanadate function as complete mitogens for SV40-transformed murine 3T3T (CSV3-1) cells but not for nontransformed 3T3T cells. Mitogenesis induced by insulin and vanadate in CSV3-1 cells is associated with the induction of the expression of protooncogenes c-Jun and junB, two major AP-1 transcription factor components. We now report that both insulin and vanadate induce a significant increase in AP-1 DNA binding activity in CSV3-1 cells but not in 3T3T cells. Gel supershift assays and Western blot analysis using specific antibodies demonstrate that the increased AP-1 binding activity induced by insulin and vanadate in CSV3-1 cells is primarily contributed by an increase in the expression of c-Jun and JunB protein levels. Furthermore, treatment of CSV3-1 cells with antisense oligodeoxyribonucleotides to c-Jun or to junB blocks insulin- and vanadate-induced mitogenesis whereas antisense junD oligomers have no inhibitory effects. These results therefore demonstrate that the induction of AP-1 binding activity associated with c-Jun and JunB is required for insulin- and vanadate-induced rnitogenesis in SV40-transformed murine 3T3T cells. Additional data presented in this paper show that JunD/AP-1 binding activity, which is thought to play a negative role in regulating cell proliferation, is also slightly induced following insulin and vanadate stimulation in CSV3-1 cells. Nevertheless, the ratio of proliferation promoting c-Jun/AP-1 and JunB/AP-1 binding activities to proliferation inhibiting JunD/AP-1 binding activity is significantly increased following insulin and vanadate stimulation. These results therefore support the concept that modulation of the balance of positive Jun/AP-1 and negative Jun/AP-1 activities is important in regulating cell proliferation.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 153 (1995), S. 59-67 
    ISSN: 1573-4919
    Keywords: adipocyte differentiation ; neoplastic transformation ; insulin ; c-jun ; junB ; tyrosine phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Vanadate and insulin both function as unique complete mitogens for SV40-transformed 3T3T cells, designated CSV3-1, but not for nontransformed 3T3T cells. The mitogenic effects induced by vanadate and insulin in CSV3-1 cells are mediated by different signaling mechanisms. For example, vanadate does not stimulate the tyrosine phosphorylation of the insulin receptor β-subunit nor the 170 kDa insulin receptor substrate-1. Instead, vanadate induces a marked increase in tyrosine phosphorylation of 55 and 64 kDa proteins that is not observed in insulin-stimulated CSV3-1 cells. Perhaps most interestingly, vanadate-induced mitogenesis is associated with the selective induction ofc-jun andjunB expression without significantly inducingc-fos orc-myc. Furthermore, treatment of CSV3-1 cells with genistein abolishes the effects of vanadate on protein tyrosine phosphorylation andc-jun induction. These and related data suggest that modulation of protein tyrosine phosphorylation andc-jun andjunB expression may serve the critical roles in mediating vanadate-induced mitogenesis in SV40-transformed cells.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 158 (1994), S. 408-416 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Insulin and vanadate selectively induce mitogenesis in quiescent SV40 large T antigen-transformed 3T3 T cells (CSV3-1) but not in quiescent nontransformed 3T3 T cells. Insulin and vanadate mediate this effect in CSV3-1 cells by distinct signal transduction mechanisms that involve protein tyrosine kinase activity. To further study these processes, changes in protein tyrosine phosphorylation induced by insulin and vanadate were investigated. Using immunoprecipitation and Western blotting techniques with antiphosphotyrosine antibodies, we report distinct protein phosphorylation characteristics in insulin- and vanadate-stimulated CSV3-1 cells. The insulin receptor β-subunit is phosphorylated within 2 min after insulin stimulation of transformed CSV3-1 cells. Insulin also stimulates a rapid increase in tyrosine phosphorylation of the 170 kDa insulin receptor substrate-1 and complex formation between the phosphorylated insulin receptor substrate-1 and the 85 kDa subunit of phosphatidylinositol 3'-kinase. In contrast, vanadate does not initially increase detectable phosphorylation of any proteins, including neither the insulin receptor nor the insulin receptor substrate-1. After 60 min, however, a marked increase in tyrosine phosphorylation of 55 and 64 kDa proteins is observed in vanadate-treated CSV3-1 cells. Furthermore, treatment of CSV3-1 cells with genistein abolishes the effects of vanadate on protein tyrosine phosphorylation but only minimally inhibits the effects of insulin. Finally, insulin stimulates the phosphorytion of a 33 kDa protein, whereas vanadate does not. By comparison, in nontransformed 3T3 T cells, insulin induces a delayed and weaker tyrosine phosphorylation of the insulin receptor β-subunit and vanadate does not enhance the tyrosine phosphorylation of the 55 and 64 kDa proteins. These data together indicate that the mitogenic effects of insulin and vanadate are associated with distinct protein phosphorylation patterns that appear to be differentially regulated in SV40-transformed and nontransformed 3T3 T cells. © 1994 Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 147 (1991), S. 102-110 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Simian virus 40 (SV40) large T antigen-transformed cells typically show a markedly reduced serum requirement for growth and the inability to growth arrest and differentiate. An SV40 large T antigen-transformed 3T3 T cell line, CSV3-1, that can growth arrest and differentiate into adipocytes with high efficiency has, however, recently been described (Scott et al: Proc. Natl. Acad. Sci. U.S.A. 86: 1652-1656, 1989; Estervig et al: J. Virol. 63: 2718-2725, 1989; J. Cell. Physiol. 142:552-558, 1990). The results of the current studies using these cells show that whereas quiescent 3T3 T cells show no mitogenic response to insulin, quiescent CSV3-1 cells show a highly significant insulin-induced mitogenic responsiveness in the absence of other added growth factors. Maximum mito-genesis was observed at an insulin concentration of 1 μg/ml, which induced 40-70% of the cells to undergo DNA synthesis within 48 hours. The half maximum response was achieved with 1-10 ng/ml of insulin. Insulin's mitogenic effect on CSV3-1 cells was evident under several different culture conditions that induce quiescence and was not mediated by any detectable autocrine growth factors that might make CSV3-1 cells competent to respond to insulin. In CSV3-1 cells insulin appears to act on its own receptor rather than on the IGF-1 receptor, because at comparable dosages IGF-1 is 10-to 100-fold less effective than insulin. Insulin also is shown to be a mitogen for another SV40-transformed cell line, CSV3-35, which can be growth arrested; in contrast insulin has no mitogenic effect on two control cell lines that are stably transfected with pSV2neo, a plasmid containing SV40 early promoter/enhancer but lacking large T antigen gene. These results suggest a significant relationship between SV40 T antigen-associated transformation and the expression of mitogenic responsiveness to insulin.
    Additional Material: 7 Ill.
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 151 (1992), S. 50-55 
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: SV40 large T oncoprotein-transformed murine mesenchymal 3T3 T stem cells (CSV3 cells) can be induced to growth arrest and then differentiate into adipocytes. When differentiation occurs, SV40 T oncoprotein expression is repressed (Estervig et al., J Virol 63:2713, 1989). To determine if repression of T oncoprotein expression can also be induced pharmacologically, the effect of a variety of agents that have been reported to effect differentiation in various cell types but not in 3T3 T or CSV3 cells was tested. This rationale suggests that if any of these agents repress T oncoprotein expression in CSV3 cells, then the results would establish that repression of T oncoprotein expression can be mediated by mechanisms independent of overt differentiation. The results show that dimethylsulfoxide (DMSO) is the only agent tested that represses T oncoprotein expression in CSV3 cells. Repression occurs in a dosage-dependent manner within 24-96 hours after exposure to DMSO. The effect of DMSO on T oncoprotein expression is mediated by posttranslational mechanisms that decrease the stability of the T oncoprotein. DMSO-induced repression of T oncoprotein expression is also associated with reversion of the transformed phenotype in CSV3 cells as demonstrated by the loss of responsiveness to a specific transformation-associated mitogen. These data support the conclusion that the pharmacological repression of T oncoprotein expression represents a form of cancer suppressor activity that can be mediated by a distinct molecular mechanism. © 1992 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
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  • 9
    Publication Date: 2024-02-05
    Description: Pedogenic carbonate carbon isotope data, occluded organic matter carbon isotope data, and bulk magnetic susceptibility data are from the Jiaxian section of the Chinese Loess Plateau. Samples were collected from the field in July, 2017. Between 1 and 16 discrete pedogenic carbonate nodules were collected from 121 different depths over a 58-meter section. Separate bulk loess samples were collected every 10 cm for magnetic susceptibility analyses. 697 individual nodules were drilled and their carbonate δ13C values were measured at the University of Texas Stable Isotope Laboratory. Between 1 and 16 nodules were analyzed for each respective depth. When enough material was available (668 nodules), splits of the samples were acidified and rinsed before being analyzed for the δ13C values of occluded organic matter at the University of Texas Stable Isotope Laboratory. 17 and 109 replicate analyses are also included for carbonate and occluded organic matter, respectively. Magnetic susceptibility measurements were conducted at Nanjing University. Magnetic susceptibility data were used to correlate to previously published age models for the Jiaxian section that were based on paleomagnetic reversals.
    Keywords: Carbon isotopes; loess plateau; magnetic susceptibility; Miocene; occluded organic matter; paleosol; pedogenic carbonate; Pliocene
    Type: Dataset
    Format: application/zip, 5 datasets
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  • 10
    Publication Date: 2024-02-05
    Keywords: Age; Age model calibration; Carbon isotopes; CH17JX; DEPTH, sediment/rock; loess plateau; magnetic susceptibility; Miocene; occluded organic matter; OUTCROP; Outcrop sample; paleosol; pedogenic carbonate; Pliocene; Shaanxi
    Type: Dataset
    Format: text/tab-separated-values, 581 data points
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