The Nuclear Acidic Proteins in Cell Proliferation and Differentiation

LeStourgeon, Wallace M.; Totten, Roger E.; Forer, Arthur

doi:10.1016/b978-0-12-156930-3.50011-1

Cited by 23 publications

(12 citation statements)

References 82 publications

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“…The condensed form of chromatin which is recognized under the light microscope as heterochromatic may consist of large number of spheres closely packed together, while in the euchromatic state the spheres are more widely separated from each other. This model agrees with observations by Tschermak-Woess and Hasitschka (1953) on plant nuclei as well as more precise ones by LeStourgeon et al (1974) and other workers cited by them on nuclei of Physarum, human HeLa cells, and fibroblasts, showing a close correlation between condensation of chromatin and genetic as well as metabolic inactivity and decondensation in association with increased activity. Cook (1974) has suggested, the programmed activation of specific genes during development, as well as the activation and repression of cell proliferation, may be mediated by the establishment or removal of temporary or semipermanent states of the quaternary structure of chromatin, at a level above the supramolecular organization consisting of pellets and connecting strands.…”

Section: Fine Structure Of Chromatin At the Molecular Levelsupporting

confidence: 92%

“…Others are similar to the contractile proteins of muscle: actin, myosin, and tropomyosin. They may play active roles in the contraction of both the nuclear membrane and the chromosomes during the various stages of the cel1 cycle (LeStourgeon et al, 1974;Douvas et al, 1975). The third kind, which constitute almost certainly a small minority of the entire complement of acidic proteins, are involved in the differentiation of tissues, presumably through activation and repression of specific genes or gene complexes.…”

Section: Acidic Proteins As Regulators Of Gene Action and Cell Prolifmentioning

confidence: 99%

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Chromosome, DNA and Plant Evolution

Stebbins

1976

Evolutionary Biology

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Section: Fine Structure Of Chromatin At the Molecular Levelsupporting

confidence: 92%

Section: Acidic Proteins As Regulators Of Gene Action and Cell Prolifmentioning

confidence: 99%

Chromosome, DNA and Plant Evolution

Stebbins

1976

Evolutionary Biology

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“…Most probably, the reason these authors did not confirm the presence in chromatin of a protein group with such metabolic properties is that the Ehrlich-Lettre hyperdiploid ascites tumour cells they studieswere not stopped in thelate-resting state. In support of this, their electrophoregrams do not display a nonhistone protein pattern specific for a quiescent cell population, deeply entered into this state (see also [42,43]). …”

Section: Discussionmentioning

confidence: 93%

The Growth Inhibition in Friend Erythroleukemia Cells Induces Cycling of Preexisting Nonhistone Proteins

Yancheva¹,

Djondjurov²

1982

European Journal of Biochemistry

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The present investigation performed on Friend erythroleukemia cells provides evidence that the cellular reprogramming associated with transition of the cells from the growing to the resting state is accompanied by an intranuclear cycling of preexisting proteins migrating from the cytoplasm. The model system developed for this study affords an opportunity to follow these events in a conveniently short period. The flow microfluorometric analysis revealed that, with respect to DNA content, the quiescent nuclei exhibit distribution in GI, S and G2 phases, as do the nuclei of the control, exponentially growing cells. It was found further that thc induction of quiescence arouses two waves of migration of preexisting cytoplasmic proteins toward the nucleus : an early one, during the transition to quiescence clearly showing density dependence, and a late one, in the established resting state. While the early-cycled proteins are undetectable in mass and once they have reached the nucleus have a short life time and, thus, could be considered as regulatory molecules, the late-cycled proteins accumulate within the nucleus and are associated most probably with structural reorganization of the resting nuclei ; moreover, the late-cycled nonhistone proteins were found localized, at least partly, in the nuclear protein matrix structure. Control experiments confirmed that the early and late-cycled proteins have been synthesized in the cytoplasm in the proliferative state but are cycled intranuclearly only if the resting state has been induced. When finally the resting cells were stimulated to proliferate, the accumulated presynthesized and newly synthesized nonhistone proteins undergo a rapid degradation which suggests that the new cellular programme may require a complete elimination of the 'resting' nonhistone proteins.A number of reports indicate that the general changes in nuclear activity during cellular reprogramming are preceded by an influx into the nucleus of proteins that have been synthesized before the initial stimulus. For example, experiments on transplantation of 'differentiated' nuclei into eggs and oocytes demonstrate a migration of preformed proteins from the host cytoplasm to the grafted nucleus before reactivation of the chromatin [l]. Virtually the same result was found in experiments on cell fusion [2,3] and on 'puffing' in polytene chromosomes [4,5]. Many speculations have been made on the role of preexisting proteins in cellular reprogramming, but they are all finally limited to the idea that these proteins participate in the circuit of events which switch on certain repressed genes (for review see [6]). In this sense, the transition of a cell population from the proliferative to the resting state can be considered as the reverse process, switching off in particular cistrons required for DNA synthesis. In order to see if such a type of reprogramming is also accompanied by an intranuclear cycling of presynthesized proteins, a series of experiments with Friend erythroleukemia cells was carried out. The resul...

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“…This is consistent with the biochemical similarities of these proteins. Like protein A1 from mammalian cells, the Physarum protein is only present in major intranuclear concentrations in actively dividing cell states (LeStourgeon et al 1974(LeStourgeon et al , 1975. As discussed in the next section, this observation first aroused our interest in the protein as a possible homolog.…”

Section: Characterization Of the Basic Proteins Of Mammalian Hnrnp Pamentioning

confidence: 99%