scholarly journals Inhibition of PHLPP2/cyclin D1 protein translation contributes to the tumor suppressive effect of NFκB2 (p100)

Oncotarget ◽  
2016 ◽  
Vol 7 (23) ◽  
pp. 34112-34130 ◽  
Author(s):  
Jiawei Xu ◽  
Yulei Wang ◽  
Xiaohui Hua ◽  
Jiheng Xu ◽  
Zhongxian Tian ◽  
...  
Keyword(s):  
Cyclin D1 ◽  
D1 Protein ◽  
Protein Translation ◽  
Suppressive Effect ◽  
Cyclin D1 Protein ◽  
Tumor Suppressive Effect

Cyclin D1 Protein Tissue Detection in Laryngeal Cancer

ORL ◽  
2005 ◽  
Vol 67 (6) ◽  
pp. 319-325 ◽  
Author(s):  
John V. Segas ◽  
Andreas C. Lazaris ◽  
Thomas P. Nikolopoulos ◽  
Nikolaos G. Kavantzas ◽  
Irene E. Lendari ◽  
...  
Keyword(s):  
Cyclin D1 ◽  
Laryngeal Cancer ◽  
D1 Protein ◽  
Cyclin D1 Protein

mTOR function in skeletal muscle hypertrophy: increased ribosomal RNA via cell cycle regulators

2005 ◽  
Vol 289 (6) ◽  
pp. C1457-C1465 ◽  
Author(s):  
Gustavo A. Nader ◽  
Thomas J. McLoughlin ◽  
Karyn A. Esser
Keyword(s):  
Cell Cycle ◽  
Protein Expression ◽  
Cyclin D1 ◽  
Ribosomal Rna ◽  
Molecular Mechanisms ◽  
D1 Protein ◽  
Rna Content ◽  
Cyclin D1 Protein ◽  
Rb Phosphorylation ◽  
Myotube Hypertrophy

The purpose of this study was to identify the potential downstream functions associated with mammalian target of rapamycin (mTOR) signaling during myotube hypertrophy. Terminally differentiated myotubes were serum stimulated for 3, 6, 12, 24, and 48 h. This treatment resulted in significant myotube hypertrophy (protein/DNA) and increased RNA content (RNA/DNA) with no changes in DNA content or indices of cell proliferation. During myotube hypertrophy, the increase in RNA content was accompanied by an increase in tumor suppressor protein retinoblastoma (Rb) phosphorylation and a corresponding increase in the availability of the ribosomal DNA transcription factor upstream binding factor (UBF). Serum stimulation also induced an increase in cyclin D1 protein expression in the differentiated myotubes with a concomitant increase in cyclin D1-dependent cyclin-dependent kinase (CDK)-4 activity toward Rb. The increases in myotube hypertrophy and RNA content were blocked by rapamycin treatment, which also prevented the increase in cyclin D1 protein expression, CDK-4 activity, Rb phosphorylation, and the increase in UBF availability. Our findings demonstrate that activation of mTOR is necessary for myotube hypertrophy and suggest that the role of mTOR is in part to modulate cyclin D1-dependent CDK-4 activity in the regulation of Rb and ribosomal RNA synthesis. On the basis of these results, we propose that common molecular mechanisms contribute to the regulation of myotube hypertrophy and growth during the G1 phase of the cell cycle.

scholarly journals Immunohistochemical Analysis of Cyclin D1 Protein in Hematopoietic Neoplasms with Special Reference to Mantle Cell Lymphoma

1994 ◽  
Vol 85 (12) ◽  
pp. 1270-1279 ◽  
Author(s):  
Shigeo Nakamura ◽  
Masao Seto ◽  
Shogo Banno ◽  
Susumu Suzuki ◽  
Takashi Koshikawa ◽  
...  
Keyword(s):  
Special Reference ◽  
Cyclin D1 ◽  
Mantle Cell Lymphoma ◽  
Cell Lymphoma ◽  
D1 Protein ◽  
Immunohistochemical Analysis ◽  
Cyclin D1 Protein ◽  
Mantle Cell

Overexpression of cyclin D1 protein in pancreatic endocrine tumors

1998 ◽  
Vol 114 ◽  
pp. A448
Author(s):  
DC Chung ◽  
SB Brown ◽  
F Graeme-Cook ◽  
AL Warshaw ◽  
M Seto ◽  
...  
Keyword(s):  
Cyclin D1 ◽  
D1 Protein ◽  
Endocrine Tumors ◽  
Pancreatic Endocrine Tumors ◽  
Cyclin D1 Protein

scholarly journals Gamma Interferon and Cadmium Treatments Modulate Eukaryotic Initiation Factor 4E-Dependent mRNA Transport of Cyclin D1 in a PML-Dependent Manner

2002 ◽  
Vol 22 (17) ◽  
pp. 6183-6198 ◽  
Author(s):  
Ivan Topisirovic ◽  
Allan D. Capili ◽  
Katherine L. B. Borden
Keyword(s):  
Cyclin D1 ◽  
D1 Protein ◽  
Nuclear Bodies ◽  
Initiation Factor ◽  
Eukaryotic Initiation Factor ◽  
Mrna Transport ◽  
Protein Levels ◽  
Eukaryotic Initiation Factor 4E ◽  
Cadmium Treatment ◽  
Cyclin D1 Protein

ABSTRACT The eukaryotic initiation factor 4E (eIF4E), when dysregulated, transforms cells. A substantial fraction of eIF4E forms nuclear bodies that colocalize with those associated with the promyelocytic leukemia protein PML. Overexpression studies indicate that nuclear eIF4E promotes the transport of cyclin D1 mRNA from the nucleus to the cytoplasm and that PML is a key negative regulator of this function. Since previous studies used overexpression methods, the physiological relevance of eIF4E mRNA transport function or its interaction with PML remained unknown. Therefore, we monitored whether eIF4E-dependent transport could be modulated in response to environmental conditions. Here we report that cadmium treatment, which disperses PML nuclear bodies, leaves eIF4E bodies intact, leading to increased transport of cyclin D1 mRNA and increased cyclin D1 protein levels. Removal of cadmium allows PML to reassociate with eIF4E nuclear bodies, leading to decreased cyclin D1 transport and reduced cyclin D1 protein levels. In contrast, we show that treating cells with interferon increased the levels of PML protein at the PML-eIF4E nuclear body, leading to nuclear retention of cyclin D1 transcripts and reduced cyclin D1 protein levels. Neither interferon nor cadmium treatment altered cyclin D1 levels in PML−/− cells. Consistently, overexpression of a series of PML and eIF4E mutant proteins established that PML eIF4E interaction is required for the observed effects of cadmium and interferon treatment. The present study provides the first evidence that physiological factors modulate the mRNA transport functions of eIF4E and that this regulation is PML dependent.

Iron chelation regulates cyclin D1 expression via the proteasome: a link to iron deficiency–mediated growth suppression

Blood ◽  
2006 ◽  
Vol 109 (9) ◽  
pp. 4045-4054 ◽  
Author(s):  
Effie Nurtjahja-Tjendraputra ◽  
Dong Fu ◽  
Juanita M. Phang ◽  
Des R. Richardson
Keyword(s):  
Cell Cycle ◽  
Cyclin D1 ◽  
Cell Cycle Control ◽  
D1 Protein ◽  
Iron Chelation ◽  
Growth Suppression ◽  
Dependent Manner ◽  
Critical Function ◽  
Cyclin D1 Protein

Abstract Iron (Fe) plays an important role in proliferation, and Fe deficiency results in G1/S arrest. Despite this, the precise role of Fe in cell-cycle control remains unclear. Cyclin D1 plays a critical function in G1 progression by interacting with cyclin-dependent kinases. Previously, we examined the effect of Fe depletion on the expression of cell-cycle control molecules and identified a marked decrease in cyclin D1 protein, although the mechanism involved was unknown. In this study, we showed that cyclin D1 was regulated posttranscriptionally by Fe depletion. Iron chelation of cells in culture using desferrioxamine (DFO) or 2-hydroxy-1-naphthylaldehyde isonicotinoyl hydrazone (311) decreased cyclin D1 protein levels after 14 hours and was rescued by the addition of Fe. Cyclin D1 half-life in control cells was 80 ± 15 minutes (n = 5), while in chelator-treated cells it was significantly (P < .008) decreased to 38 ± 3 minutes (n = 5). Proteasomal inhibitors rescued the Fe chelator–mediated decrease in cyclin D1 protein, suggesting the role of the proteasome. In Fe-replete cells, cyclin D1 was degraded in an ubiquitin-dependent manner, while Fe depletion induced a ubiquitin-independent pathway. This is the first report linking Fe depletion–mediated growth suppression at G1/S to a mechanism inducing cyclin D1 proteolysis.

Translocation (11;14)(q13;q32) and Overexpression of Cyclin D1 Protein in a CD23-Positive Low-Grade B-Cell Neoplasm

1998 ◽  
Vol 106 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Gouri Nanjangud ◽  
K.N. Naresh ◽  
Chandrika N. Nair ◽  
Bhavna Parikh ◽  
Priyanka H. Dixit ◽  
...  
Keyword(s):  
B Cell ◽  
Cyclin D1 ◽  
D1 Protein ◽  
Low Grade ◽  
Cyclin D1 Protein ◽  
Cell Neoplasm

Expression of cyclin D1 protein in centrocytic/mantle cell lymphomas with and without rearrangement of the BCL1/Cyclin D1 gene*1, *2

1995 ◽  
Vol 26 (9) ◽  
pp. 999-1004 ◽  
Author(s):  
S SWERDLOW ◽  
W YANG ◽  
L ZUKERBERG ◽  
N HARRIS ◽  
A ARNOLD ◽  
...  
Keyword(s):  
Cyclin D1 ◽  
D1 Protein ◽  
Cyclin D1 Protein ◽  
Mantle Cell

Cyclin D1 protein expression and function in human breast cancer

1994 ◽  
Vol 57 (3) ◽  
pp. 353-361 ◽  
Author(s):  
Jirina Bartkova ◽  
Jiri Lukas ◽  
Heiko Müller ◽  
Dorrit Lützhøt ◽  
Michael Strauss ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Expression ◽  
Cyclin D1 ◽  
Human Breast Cancer ◽  
D1 Protein ◽  
Human Breast ◽  
Cyclin D1 Protein ◽  
And Function
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