The Presence of Parvalbumin in a Nonmuscle Cell Line Attenuates Progression through Mitosis

Rasmussen, Colin D.; Means, Anthony R.

doi:10.1210/mend-3-3-588

Cited by 27 publications

(13 citation statements)

References 22 publications

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“…A study of a PV knockout mouse has shown that the Ca 2ϩ buffering action of PV also is important for the regulation of short term synaptic plasticity in gamma-amino butyric acid-responsive neurons (81). Furthermore, ectopic expression of PV in nonmuscle cell types attenuates cell cycle progression (54,55). However, the current work is the first demonstration that targeted expression of PV can be used to examine the effects of Ca 2ϩ in distinct subcellular regions.…”

Section: Discussionmentioning

confidence: 84%

“…We took an alternative approach to block Ca 2ϩ in distinct subcellular compartments by using the Ca 2ϩ -binding protein PV fused to targeting sequences that direct its subcellular localization to either the nucleus or cytosol. Although PV has been demonstrated to inhibit Ca 2ϩ signaling when expressed in mammalian cells (54,55), targeted expression of PV to discrete subcellular compartments to locally buffer Ca 2ϩ has not been reported. Nuclear expression of PV was established by generating an in-frame fusion of PV with the nuclear localization signal derived from the SV40 large T antigen (56) (Fig.…”

Section: Expression and Subcellular Localization Of Targeted Parvalbumentioning

confidence: 99%

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Epidermal Growth Factor-mediated Activation of the ETS Domain Transcription Factor Elk-1 Requires Nuclear Calcium

Pusl¹,

Wu²,

Zimmerman³

et al. 2002

Journal of Biological Chemistry

104

109

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Cytosolic and nuclear Ca2؉ have been shown to differentially regulate transcription. However, the impact of spatially distinct Ca 2؉ signals on mitogen-activated protein kinase-mediated gene expression remains unknown. Here we investigated the role of nuclear and cytosolic Ca 2؉ signals in epidermal growth factor (EGF)-induced transactivation of the ternary complex factor Elk-1 using a GAL4-Elk-1 construct. EGF increased Ca

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Section: Discussionmentioning

confidence: 84%

Section: Expression and Subcellular Localization Of Targeted Parvalbumentioning

confidence: 99%

Epidermal Growth Factor-mediated Activation of the ETS Domain Transcription Factor Elk-1 Requires Nuclear Calcium

Pusl¹,

Wu²,

Zimmerman³

et al. 2002

Journal of Biological Chemistry

104

109

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“…Nucleoplasmic Ca 2ϩ signals have distinct effects on activation of transcription factors (9,10) and kinases (11,12), but it is not known whether nuclear Ca 2ϩ signals also regulate more global aspects of cell function. Because cell proliferation (13,14) and progression through the cell cycle (15,16) are Ca 2ϩ -dependent, we investigated the relative roles of nuclear and cytoplasmic Ca 2ϩ on cell growth.…”

Section: Camentioning

confidence: 99%

Nucleoplasmic Calcium Is Required for Cell Proliferation

Rodrigues

Gomes

Leite

et al. 2007

Journal of Biological Chemistry

125

179

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Ca2؉ signals regulate cell proliferation, but the spatial and temporal specificity of these signals is unknown. Here we use selective buffers of nucleoplasmic or cytoplasmic Ca 2؉ to determine that cell proliferation depends upon Ca 2؉ signals within the nucleus rather than in the cytoplasm. Nuclear Ca 2؉ signals stimulate cell growth rather than inhibit apoptosis and specifically permit cells to advance through early prophase. Selective buffering of nuclear but not cytoplasmic Ca 2؉ signals also impairs growth of tumors in vivo. These findings reveal a major physiological and potential pathophysiological role for nucleoplasmic Ca 2؉ signals and suggest that this information can be used to design novel therapeutic strategies to regulate conditions of abnormal cell growth. Ca2ϩ is a ubiquitous second messenger that mediates a wide range of cellular responses such as contraction, fluid and electrolyte secretion, exocytosis, gene transcription, and apoptosis (1). This ability to simultaneously control multiple processes occurs by careful modulation of Ca 2ϩ signals, not only over time but in different subcellular regions as well (2). For example, polarized Ca 2ϩ waves direct apical secretion in epithelia (3), whereas presynaptic increases in Ca 2ϩ trigger neurotransmitter release (4) and mitochondrial increases in Ca 2ϩ regulate apoptosis (5, 6). Ca 2ϩ signals also can be regulated independently in the nucleoplasm relative to the cytoplasm (7,8), but the physiological significance of this aspect of spatial control is not entirely understood. Nucleoplasmic Ca 2ϩ signals have distinct effects on activation of transcription factors (9, 10) and kinases (11, 12), but it is not known whether nuclear Ca 2ϩ signals also regulate more global aspects of cell function. Because cell proliferation (13,14) and progression through the cell cycle (15, 16) are Ca 2ϩ -dependent, we investigated the relative roles of nuclear and cytoplasmic Ca 2ϩ on cell growth. EXPERIMENTAL PROCEDURESMaterials, Reagents, and Cell Lines-SKHep1, HepG2, and HEK-293 cell lines were obtained from the American Type Culture Collection (Manassas, VA) and were used for all experiments. The cells were grown at 37°C with 5% CO 2 :95% O 2 in Dulbecco's modified Eagle's medium supplemented with 1% penicillin-streptomycin and 10% heat-inactivated fetal bovine serum, all from Invitrogen. The cells were grown on glass coverslips overnight in the absence of serum before infection with each parvalbumin (PV) 2 construct. Generation of Parvalbumin Constructs and AdenoviralInfection-Constructs encoding red fluorescence protein (DsRed) from Clontech (Mountain View, CA) and targeted PV proteins (PV-NLS, PV-NES, and PV-NLS-CD) were PCR-amplified and subcloned into pShuttle-CMV (kindly provided by Bert Vogelstein, Johns Hopkins) by restriction digestion with XhoI and XbaI to generate pShuttle-CMV-PVNLS-DSR, pShuttle-CMV-PVNES-DSR, and pShuttle-CMV-PVNLS-CD-DSR. Recombinant adenoviruses were generated by transformation of pShuttle-CMV-PV-NLS-DSR into AdEasier-1 cells, a deri...

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“…The amount of PV was not directly assayed in the present studies, but it was detected by label incorporation and one-dimensional electrophoresis; and previous studies have shown that the expression of its gene is stable in PV-1 cells (Rasmussen and Means, 1989a). For all cell lines, repeat experiments were carried out within a defined passage number range (62-77,51-59, 68-79, and 49-58 for (2127, BPV-1, CM-1, and PV-1, respectively).…”

Section: Determination Of Cam and Pv Levels Inmentioning

confidence: 88%

Altered synthesis of the 26‐kDa heat stress protein family and thermotolerance in cell lines with elevated levels of calcium‐binding proteins

Evans

Simonette

Rasmussen

et al. 1990

Journal Cellular Physiology

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Using a bovine papilloma virus-based vector, mouse mammary adenocarcinoma cells have been transformed to express elevated amounts of functional calmodulin (CaM) (Rasmussen and Means, 1987) and another Ca2(+)-binding protein, parvalbumin (PV) (Rasmussen and Means, 1989) that is not normally synthesized in these cells. Parental cells (C127) and cells transformed by the vector alone (BPV-1), the vector containing a CaM gene (CM-1), or the vector containing parvalbumin (PV-1) were used to study the effect of increased synthesis of Ca2(+)-binding proteins on heat-stress protein (HSP) synthesis and cell survival following heating at 43 degrees C. The induction, stability, and repression of the synthesis of most HSPs after 43 degrees C heating was not significantly affected by increased amounts of Ca2(+)-binding proteins, but the rate of synthesis of all three isoforms of the 26-kDa HSP (HSP26) was greatly reduced. C127 cells, which have about one half as much CaM as do BPV-1 cells, synthesized the most HSP26. CM-1 cells, which have more than fourfold higher levels of CaM than do BPV-1 cells, had a rate of synthesis of HSP26 approaching that of unheated cells. BPV-1 cells, with a two-fold increase in CaM, were intermediate in HSP26 synthesis. This effect on HSP26 synthesis may be largely related to the Ca2(+)-binding capacity of CaM rather than to a specific CaM-regulated function, since PV-1 cells also showed reduced rates of HSP26 synthesis. Survival experiments showed that reduced HSP26 synthesis in cells with increased amounts of Ca2(+)-binding proteins did not significantly alter intrinsic resistance to continuous 43 degrees C heating. Thermotolerance was not reduced and appeared to develop more rapidly in CM-1 and PV-1 cells. These results suggest that (1) the signal for HSP26 synthesis can be largely abrogated by elevated Ca2+ binding protein levels, and (2) if these HSPs are involved in thermotolerance development, that function may be associated with intracellular Ca2+ homeostasis.

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The Presence of Parvalbumin in a Nonmuscle Cell Line Attenuates Progression through Mitosis

Cited by 27 publications

References 22 publications

Epidermal Growth Factor-mediated Activation of the ETS Domain Transcription Factor Elk-1 Requires Nuclear Calcium

Epidermal Growth Factor-mediated Activation of the ETS Domain Transcription Factor Elk-1 Requires Nuclear Calcium

Nucleoplasmic Calcium Is Required for Cell Proliferation

Altered synthesis of the 26‐kDa heat stress protein family and thermotolerance in cell lines with elevated levels of calcium‐binding proteins

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