A novel crosstalk between calcium/calmodulin kinases II and IV regulates cell proliferation in myeloid leukemia cells

Matarazzo, Sara; Rusciano, Maria Rosaria; Maione, Angela Serena; Soprano, Maria; Gomathinayagam, Rohini; Todd, Lance R.; Campiglia, Pietro; Salzano, Salvatore; Pastore, Lucio; Leggiero, Eleonora; Wilkerson, Donald C.; Rocco, Monia; Selleri, Carmine; Iaccarino, Guido; Sankar, Uma; Illario, Maddalena

doi:10.1016/j.cellsig.2014.11.007

Cited by 30 publications

(30 citation statements)

References 50 publications

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“…The role for the different isoforms of CaM Kinases in oncogenesis is rapidly emerging and evidence supports the involvement for CaM KK, CaM KI, CaM KIV, CaM KII as well as their various substrates and cellular targets in cancer development [60,[68][69][70][71][72][73][74]. Consistent with our data, Iglewski et al demonstrated that urotensin treatment of primary smooth muscle cells activated a CaM KK/CaM KI/ERK proliferation pathway although the ability of other hormones to inhibit this process was not examined [75].…”

Section: Discussionsupporting

confidence: 81%

Estrogen Activation of CaM Kinases and Transcription Is Blocked by Vitamin D in MCF-7 Breast Cancer Cells

John¹,

Do²,

Amanda³

et al. 2017

JAMB

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Abstract. Calcium/calmodulin-dependent protein kinase (CaM Kinase) proteins are targets of hormones and growth factors and regulate cancer cell growth, apoptosis and migration. The hormone estrogen (E2) utilizes CaM Kinases to activate the Extracellular-signal regulated kinase (ERK) leading to MCF-7 breast cancer cell growth. The hormone Vitamin D (Vit D) may inhibit breast cancer cell growth however the cellular mechanisms of Vit D action remain to be elucidated. Within the present study we provide data that E2 stimulation of MCF-7 cells activates CaM Kinase Kinase (CaM KK), CaM KI, and ERK and the transcription factors Elk-1 and SRF. E2 treatment of MCF-7 cells potently stimulated Elk-1/SRF directed transcription of SRE-luciferase reporters. E2 activation of ERK, Elk-1, SRF and SRE-dependent luciferase activities were blocked by treating cells with the CaM KK inhibitor, STO-609, and the ERK inhibitor, U0126. Moreover, siRNAs directed against CaM KK and ERK blocked transcription factor phosphorylation and luciferase activity. Treatment of cells with Vit D, the hormone Epinephrine (Epi), or Forskolin, prevented E2 activation of CaM KK and ERK. Interestingly, Vit D promoted a PKA-dependent phosphorylation and inhibition of CaM KK as well as its association with 14-3-3. Epi and Vit D treatment of cells blocked the ability of E2 to active Elk-1 and SRE-luciferase activity. This data suggests an important role for CaM KK and ERK in regulating transcription downstream of E2 in MCF-7 cells. Our results also suggest that Vit D treatment of MCF-7 cells utilizes a unique PKA-dependent mechanism to block E2 activation of CaM KK, ERK and transcription.

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Section: Discussionsupporting

confidence: 81%

Estrogen Activation of CaM Kinases and Transcription Is Blocked by Vitamin D in MCF-7 Breast Cancer Cells

John¹,

Do²,

Amanda³

et al. 2017

JAMB

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“…The inhibitory effect of CaMKIIγ related to multiple signaling pathways, including mitogen-activated protein kinase (MAPK), signal transducer and activator of transcription 3(Stat3)/Stat5, and glycogen synthase kinase 3β (GSK3β)/β-catenin pathways [ 23 ]. Recently, Monaco et al [ 24 ] reported that inhibition of CaMKII activity resulted in an upregulation of CaMKIV mRNA and protein in myeloid leukemia cell lines. Conversely, expression of CaMKIV inhibited autophosphorylation and activation of CaMKII, and elicited G 0 /G 1 cell cycle arrest, impairing cell proliferation.…”

Section: The Role Of Camkii In Cancer Progressionmentioning

confidence: 99%

The emerging role of CaMKII in cancer

2015

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Ca2+/calmodulin-dependent protein kinase II (CaMKII) is a multifunctional serine/threonine kinases best known for its critical role in learning and memory. Recent studies suggested that high levels of CaMKII also expressed in variety of malignant diseases. In this review, we focus on the structure and biology properties of CaMKII, including the role of CaMKII in the regulation of cancer progression and therapy response. We also describe the role of CaMKII in the diagnosis of different kinds of cancer and recent progress in the development of CaMKII inhibitors. These data establishes CaMKII as a novel target whose modulation presents new opportunities for cancer diagnosis and treatment.

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“…IP3/Ca 2+ /CaMK II axis is involved in regulating cholangiocyte growth [ 25 ]. CaMK II suppresses the expression of CaMK IV to promote leukemia cell proliferation [ 26 ]. TNF-α induced CD44 expression is regulated by AP-1 through the activation of the CaMK-II pathway to mediate cell migration in human monocytic cells [ 27 ].…”

Section: Discussionmentioning

confidence: 99%

DAG/PKCδ and IP3/Ca2+/CaMK IIβ Operate in Parallel to Each Other in PLCγ1-Driven Cell Proliferation and Migration of Human Gastric Adenocarcinoma Cells, through Akt/mTOR/S6 Pathway

Dai

Zhuang

Zhang

et al. 2015

IJMS

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Phosphoinositide specific phospholipase Cγ (PLCγ) activates diacylglycerol (DAG)/protein kinase C (PKC) and inositol 1,4,5-trisphosphate (IP3)/Ca2+/calmodulin-dependent protein kinase II (CaMK II) axes to regulate import events in some cancer cells, including gastric adenocarcinoma cells. However, whether DAG/PKCδ and IP3/Ca2+/CaMK IIβ axes are simultaneously involved in PLCγ1-driven cell proliferation and migration of human gastric adenocarcinoma cells and the underlying mechanism are not elucidated. Here, we investigated the role of DAG/PKCδ or CaMK IIβ in PLCγ1-driven cell proliferation and migration of human gastric adenocarcinoma cells, using the BGC-823 cell line. The results indicated that the inhibition of PKCδ and CaMK IIβ could block cell proliferation and migration of BGC-823 cells as well as the effect of inhibiting PLCγ1, including the decrease of cell viability, the increase of apoptotic index, the down-regulation of matrix metalloproteinase (MMP) 9 expression level, and the decrease of cell migration rate. Both DAG/PKCδ and CaMK IIβ triggered protein kinase B (Akt)/mammalian target of rapamycin (mTOR)/S6 pathway to regulate protein synthesis. The data indicate that DAG/PKCδ and IP3/Ca2+/CaMK IIβ operate in parallel to each other in PLCγ1-driven cell proliferation and migration of human gastric adenocarcinoma cells through Akt/mTOR/S6 pathway, with important implication for validating PLCγ1 as a molecular biomarker in early gastric cancer diagnosis and disease surveillance.

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A novel crosstalk between calcium/calmodulin kinases II and IV regulates cell proliferation in myeloid leukemia cells

Cited by 30 publications

References 50 publications

Estrogen Activation of CaM Kinases and Transcription Is Blocked by Vitamin D in MCF-7 Breast Cancer Cells

Estrogen Activation of CaM Kinases and Transcription Is Blocked by Vitamin D in MCF-7 Breast Cancer Cells

The emerging role of CaMKII in cancer

DAG/PKCδ and IP3/Ca2+/CaMK IIβ Operate in Parallel to Each Other in PLCγ1-Driven Cell Proliferation and Migration of Human Gastric Adenocarcinoma Cells, through Akt/mTOR/S6 Pathway

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