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Article ; Online: Fer and FerT: A New Regulatory Link between Sperm and Cancer Cells.

Nir, Uri / Grinshtain, Elina / Breitbart, Haim

International journal of molecular sciences

2023 Volume 24, Issue 6

Abstract: Fer and its sperm and cancer specific variant, FerT, are non-receptor tyrosine kinases which play roles in cancer progression and metastasis. Recent studies have shed light on the regulatory role of these kinases in ensuring proper sperm function. ... ...

Abstract	Fer and its sperm and cancer specific variant, FerT, are non-receptor tyrosine kinases which play roles in cancer progression and metastasis. Recent studies have shed light on the regulatory role of these kinases in ensuring proper sperm function. Comparison of the regulatory cascades in which Fer and FerT are engaged in sperm and cancer cells presents an interesting picture, in which similar regulatory interactions of these enzymes are integrated in a similar or different regulatory context in the two cell types. These diverse compositions extend from the involvement of Fer in modulation of actin cytoskeleton integrity and function, to the unique regulatory interactions of Fer with PARP-1 and the PP1 phosphatase. Furthermore, recent findings link the metabolic regulatory roles of Fer and FerT in sperm and cancer cells. In the current review, we discuss the above detailed aspects, which portray Fer and FerT as new regulatory links between sperm and malignant cells. This perspective view can endow us with new analytical and research tools that will deepen our understanding of the regulatory trajectories and networks that govern these two multi-layered systems.
MeSH term(s)	Male ; Humans ; Protein-Tyrosine Kinases/metabolism ; Semen/metabolism ; Spermatozoa/metabolism ; Phosphorylation ; Neoplasms/metabolism
Chemical Substances	Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2023-03-09
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms24065256
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Article ; Online: Loss of Fer Jeopardizes Metabolic Plasticity and Mitochondrial Homeostasis in Lung and Breast Carcinoma Cells.

Mehazri, Linoy / Shpungin, Sally / Bel, Shai / Nir, Uri

International journal of molecular sciences

2021 Volume 22, Issue 7

Abstract: Metabolic plasticity is a hallmark of the ability of metastatic cancer cells to survive under stressful conditions. The intracellular Fer kinase is a selective constituent of the reprogramed mitochondria and metabolic system of cancer cells. In the ... ...

Abstract	Metabolic plasticity is a hallmark of the ability of metastatic cancer cells to survive under stressful conditions. The intracellular Fer kinase is a selective constituent of the reprogramed mitochondria and metabolic system of cancer cells. In the current work, we deciphered the modulatory roles of Fer in the reprogrammed metabolic systems of metastatic, lung (H358), non-small cell lung cancer (NSCLC), and breast (MDA-MB-231), triple-negative breast cancer (TNBC), carcinoma cells. We show that H358 cells devoid of Fer (H358ΔFer), strictly depend on glucose for their proliferation and growth, and fail to compensate for glucose withdrawal by oxidizing and metabolizing glutamine. Furthermore, glucose deficiency caused increased reactive oxygen species (ROS) production and induction of a DNA damage response (DDR), accompanied by the onset of apoptosis and attenuated cell-cycle progression. Analysis of mitochondrial function revealed impaired respiratory and electron transport chain (ETC) complex 1 (comp. I) activity in the Fer-deficient H358ΔFer cells. This was manifested by decreased levels of NAD
MeSH term(s)	Alleles ; Animals ; Breast Neoplasms/metabolism ; Carcinoma/metabolism ; Carcinoma, Non-Small-Cell Lung/metabolism ; Cell Line, Tumor ; DNA Damage ; Homeostasis ; Humans ; Lung Neoplasms/metabolism ; Mice ; Mice, Nude ; Mitochondria/metabolism ; Neoplasm Metastasis ; Neoplasm Transplantation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Reactive Oxygen Species/metabolism
Chemical Substances	Reactive Oxygen Species ; proto-oncogene protein c-fes-fps (110736-90-8) ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2021-03-25
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22073387
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Article ; Online: The Fer tyrosine kinase protects sperm from spontaneous acrosome reaction.

Grinshtain, Elina / Shpungin, Sally / Baum, Micha / Nir, Uri / Breitbart, Haim

Developmental biology

2022 Volume 487, Page(s) 24–33

Abstract: The physiological acrosome reaction occurs after mammalian spermatozoa undergo a process called capacitation in the female reproductive tract. Only acrosome reacted spermatozoon can penetrate the egg zona-pellucida and fertilize the egg. Sperm also ... ...

Abstract	The physiological acrosome reaction occurs after mammalian spermatozoa undergo a process called capacitation in the female reproductive tract. Only acrosome reacted spermatozoon can penetrate the egg zona-pellucida and fertilize the egg. Sperm also contain several mechanisms that protect it from undergoing spontaneous acrosome reaction (sAR), a process that can occur in sperm before reaching proximity to the egg and that abrogates fertilization. We previously showed that calmodulin-kinase II (CaMKII) and phospholipase D (PLD) are involved in preventing sAR through two distinct pathways that enhance F-actin formation during capacitation. Here, we describe a novel additional pathway involving the tyrosine kinase Fer in a mechanism that also prevents sAR by enhancing actin polymerization during sperm capacitation. We further show that protein-kinase A (PKA) and the tyrosine-kinase Src, as well as PLD, direct Fer phosphorylation/activation. Activated Fer inhibits the Ser/Thr phosphatase PP1, thereby leading to CaMKII activation, actin polymerization, and sAR inhibition.
MeSH term(s)	Acrosome ; Acrosome Reaction/physiology ; Actins/metabolism ; Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism ; Female ; Male ; Mammals/metabolism ; Phospholipase D ; Protein-Tyrosine Kinases/metabolism ; Sperm Capacitation/physiology ; Spermatozoa/metabolism
Chemical Substances	Actins ; proto-oncogene protein c-fes-fps (110736-90-8) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 (EC 2.7.11.17) ; Phospholipase D (EC 3.1.4.4)
Language	English
Publishing date	2022-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2022.04.006
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Article: The Fer tyrosine kinase protects sperm from spontaneous acrosome reaction

Grinshtain, Elina / Shpungin, Sally / Baum, Micha / Nir, Uri / Breitbart, Haim

Developmental biology. 2022 Apr. 13,

2022

Abstract	The physiological acrosome reaction occurs after mammalian spermatozoa undergo a process called capacitation in the female reproductive tract. Only acrosome reacted spermatozoon can penetrate the egg zona-pellucida and fertilize the egg. Sperm also contain several mechanisms that protect it from undergoing spontaneous acrosome reaction (sAR), a process that can occur in sperm before reaching proximity to the egg and that abrogates fertilization. We previously showed that calmodulin-kinase II (CaMKII) and phospholipase D (PLD) are involved in preventing sAR through two distinct pathways that enhance F-actin formation during capacitation. Here, we describe a novel additional pathway involving the tyrosine kinase Fer in a mechanism that also prevents sAR by enhancing actin polymerization during sperm capacitation. We further show that protein-kinase A (PKA) and the tyrosine-kinase Src, as well as PLD, direct Fer phosphorylation/activation. Activated Fer inhibits the Ser/Thr phosphatase PP1, thereby leading to CaMKII activation, actin polymerization, and sAR inhibition.
Keywords	acrosome reaction ; actin ; calcium-calmodulin-dependent protein kinase ; eggs ; female reproductive system ; mammals ; phospholipases ; phosphorylation ; polymerization ; sperm capacitation ; tyrosine ; zona pellucida
Language	English
Dates of publication	2022-0413
Publishing place	Elsevier Inc.
Document type	Article
Note	Pre-press version
ZDB-ID	1114-9
ISSN	1095-564X ; 0012-1606
ISSN (online)	1095-564X
ISSN	0012-1606
DOI	10.1016/j.ydbio.2022.04.006
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Article ; Online: A Novel Score-Based Approach by Using Routine Laboratory Tests for Accurate Diagnosis of Spontaneous Bacterial Peritonitis (SBP) in Cirrhotic Patients.

Abdo, George / Nir, Uri / Rawajdey, Rasha / Abu Dahoud, Wadie / Massalha, Jammal / Hajouj, Taleb / Assadi, Mohammad H / William, Nseir

EJIFCC

2023 Volume 34, Issue 4, Page(s) 297–304

Abstract: Background: Spontaneous Bacterial Peritonitis (SBP) poses a significant risk to cirrhosis patients with ascites, emphasizing the critical need for early detection and intervention. This retrospective observational study spanning a decade aimed to devise ...

Abstract	Background: Spontaneous Bacterial Peritonitis (SBP) poses a significant risk to cirrhosis patients with ascites, emphasizing the critical need for early detection and intervention. This retrospective observational study spanning a decade aimed to devise predictive models for SBP using routine laboratory tests. Additionally, it aimed to propose a novel scoring system to aid SBP diagnosis. Methods: Data analysis encompassed 229 adult cirrhotic patients hospitalized for ascites between 2012 and 2021. Exclusions eliminated cases of secondary ascites unrelated to liver cirrhosis. Patients were categorized into SBP-positive (n=110) and SBP-negative (n=119) groups. Comparative analysis of demographic details and various laboratory indicators (Neutrophil-to-Lymphocyte Ratio (NLR), Mean Platelet Volume (MPV), C-Reactive Protein (CRP), Platelet (PLT), Alanine Transaminase (ALT), Aspartate Amino Transferase (AST), Potassium (K), Sodium (Na), Total Bilirubin (TB) and International Normalized Ratio (INR) was performed between the groups. The study presented effective SBP prediction models for prompt diagnosis and treatment: a multivariate logistic regression model and a simple scoring system. Findings: The study advocates early diagnosis and rapid treatment for all cirrhotic patients with ascites, regardless of cirrhosis stage. Furthermore, it recommends initiating SBP treatment for patients scoring 2-3 in the proposed scoring system while excluding SBP findings for those scoring zero. Conclusion: Combining age, sex, and specific laboratory tests (MPV, NLR, CRP, TB, and INR) within random forest models and a simple scoring system enables swift and accurate SBP diagnosis.
Language	English
Publishing date	2023-12-21
Publishing country	Italy
Document type	Journal Article
ISSN	1650-3414
ISSN (online)	1650-3414
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Article ; Online: Fer and FerT Govern Mitochondrial Susceptibility to Metformin and Hypoxic Stress in Colon and Lung Carcinoma Cells.

Marciano, Odeya / Mehazri, Linoy / Shpungin, Sally / Varvak, Alexander / Zacksenhaus, Eldad / Nir, Uri

Cells

2021 Volume 10, Issue 1

Abstract: Aerobic glycolysis is an important metabolic adaptation of cancer cells. However, there is growing evidence that reprogrammed mitochondria also play an important metabolic role in metastatic dissemination. Two constituents of the reprogrammed ... ...

Abstract	Aerobic glycolysis is an important metabolic adaptation of cancer cells. However, there is growing evidence that reprogrammed mitochondria also play an important metabolic role in metastatic dissemination. Two constituents of the reprogrammed mitochondria of cancer cells are the intracellular tyrosine kinase Fer and its cancer- and sperm-specific variant, FerT. Here, we show that Fer and FerT control mitochondrial susceptibility to therapeutic and hypoxic stress in metastatic colon (SW620) and non-small cell lung cancer (NSCLC-H1299) cells. Fer- and FerT-deficient SW620 and H1299 cells (SW∆Fer/FerT and H∆Fer/FerT cells, respectively) become highly sensitive to metformin treatment and to hypoxia under glucose-restrictive conditions. Metformin impaired mitochondrial functioning that was accompanied by ATP deficiency and robust death in SW∆Fer/FerT and H∆Fer/FerT cells compared to the parental SW620 and H1299 cells. Notably, selective knockout of the
MeSH term(s)	Cell Hypoxia/drug effects ; Cell Line, Tumor ; Colonic Neoplasms/metabolism ; Colonic Neoplasms/pathology ; Humans ; Lung Neoplasms/metabolism ; Lung Neoplasms/pathology ; Metformin/pharmacology ; Mitochondria/drug effects ; Mitochondria/metabolism ; Neoplasm Metastasis ; Protein-Tyrosine Kinases/deficiency ; Protein-Tyrosine Kinases/metabolism ; Stress, Physiological/drug effects
Chemical Substances	proto-oncogene protein c-fes-fps (110736-90-8) ; Metformin (9100L32L2N) ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2021-01-07
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells10010097
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Article ; Online: TMF1 is upregulated by insulin and is required for a sustained glucose homeostasis.

Rahimi, Roni / Malek, Israel / Lerrer-Goldshtein, Tali / Elkis, Yoav / Shoval, Irit / Jacob, Avi / Shpungin, Sally / Nir, Uri

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2021 Volume 35, Issue 2, Page(s) e21295

Abstract: Insulin-regulated glucose homeostasis is a critical and intricate physiological process, of which not all regulatory components have been deciphered. One of the key players in modulating glucose uptake by cells is the glucose transporter-GLUT4. In this ... ...

Abstract	Insulin-regulated glucose homeostasis is a critical and intricate physiological process, of which not all regulatory components have been deciphered. One of the key players in modulating glucose uptake by cells is the glucose transporter-GLUT4. In this study, we aimed to explore the regulatory role of the trans-Golgi-associated protein-TATA Element Modulatory Factor (TMF1) in the GLUT4 mediated, insulin-directed glucose uptake. By establishing and using TMF1-/- myoblasts and mice, we examined the effect of TMF1 absence on the insulin driven functioning of GLUT4. We show that TMF1 is upregulated by insulin in myoblasts, and is essential for the formation of insulin responsive, glucose transporter GLUT4-containing vesicles. Absence of TMF1 leads to the retention of GLUT4 in perinuclear compartments, and to severe impairment of insulin-stimulated GLUT4 trafficking throughout the cytoplasm and to the cell plasma membrane. Accordingly, glucose uptake is impaired in TMF1-/- cells, and TMF1-/- mice are hyperglycemic. This is reflected by the mice impaired blood glucose clearance and increased blood glucose level. Correspondingly, TMF1-/- animals are leaner than their normal littermates. Thus, TMF1 is a novel effector of insulin-regulated glucose homeostasis, and dys-functioning of this protein may contribute to the onset of a diabetes-like disorder.
MeSH term(s)	Animals ; Blood Glucose/drug effects ; Cells, Cultured ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Female ; Flow Cytometry ; Glucose Tolerance Test ; Homeostasis/drug effects ; Immunoblotting ; Insulin/pharmacology ; Male ; Mice ; Mice, Knockout ; Microscopy, Fluorescence ; Transcription Factors/genetics ; Transcription Factors/metabolism
Chemical Substances	Blood Glucose ; DNA-Binding Proteins ; Insulin ; Tmf1 protein, mouse ; Transcription Factors
Language	English
Publishing date	2021-02-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.202001995R
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Article: Down-regulation of Fer induces ROS levels accompanied by ATM and p53 activation in colon carcinoma cells

Makovski, Adar / Yaffe, Etai / Shpungin, Sally / Nir, Uri

Cellular signalling. 2012 July, v. 24, no. 7

2012

Abstract: Fer is an intracellular tyrosine kinase which resides in both the cytoplasm and nucleus of mammalian cells. This kinase was also found in all malignant cell-lines analyzed and was shown to support cell-cycle progression in cancer cells. Herein we show ... ...

Abstract	Fer is an intracellular tyrosine kinase which resides in both the cytoplasm and nucleus of mammalian cells. This kinase was also found in all malignant cell-lines analyzed and was shown to support cell-cycle progression in cancer cells. Herein we show that knock-down of Fer, both, impairs cell-cycle progression and imposes programmed cell death in colon carcinoma (CC) cells. The cell-cycle arrest and apoptotic death invoked by the depletion of Fer were found to depend on the activity of p53. Accordingly, down regulation of Fer led to the activation of the Ataxia Telangiectasia Mutated protein (ATM) and its down-stream effector-p53. Knock-down of Fer also increased the level of Reactive-Oxygen Species (ROS) in CC cells, and subjection of Fer depleted cells to ROS neutralizing scavengers significantly decreased the induced phosphorylation and activation of ATM and p53. Notably, over-expression of Fer opposed the Doxorubicin driven activation of ATM and p53, which can be mediated by ROS. Collectively, our findings imply that Fer sustains low ROS levels in CC cells, thereby restraining the activation of ATM and p53 in these cells.
Keywords	apoptosis ; cell cycle ; cell lines ; colorectal neoplasms ; cytoplasm ; doxorubicin ; mammals ; neoplasm cells ; neutralization ; phosphorylation ; tyrosine
Language	English
Dates of publication	2012-07
Size	p. 1369-1374.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1002702-6
ISSN	0898-6568
ISSN	0898-6568
DOI	10.1016/j.cellsig.2012.03.004
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Article ; Online: Intronic promoter drives the BORIS-regulated expression of FerT in colon carcinoma cells.

Makovski, Adar / Yaffe, Etai / Shpungin, Sally / Nir, Uri

The Journal of biological chemistry

2012 Volume 287, Issue 9, Page(s) 6100–6112

Abstract: Fer is an intracellular tyrosine kinase that accumulates in most mammalian tissues. A truncated variant of Fer, FerT, is uniquely detected in spermatogenic cells and is absent from normal somatic tissues. Here, we show that in addition to Fer, FerT also ... ...

Abstract	Fer is an intracellular tyrosine kinase that accumulates in most mammalian tissues. A truncated variant of Fer, FerT, is uniquely detected in spermatogenic cells and is absent from normal somatic tissues. Here, we show that in addition to Fer, FerT also accumulates in CC cells and in metastases derived from colorectal tumors, but not in normal human cells. Thus, FerT is a new member of the CTA protein family. Transcription of the ferT gene in CC cells was found to be driven by an intronic promoter residing in intron 10 of the fer gene and to be regulated by another CTA, the Brother of the Regulator of Imprinted Sites (BORIS) transcription factor. BORIS binds to the ferT promoter and down-regulation of BORIS significantly decreases the expression of ferT in CC cells. Accumulation of the ferT RNA was also regulated by the DNA methylation status and paralleled the expression profile of the boris transcript. Accordingly, the intronic ferT promoter was found to be hypomethylated in cancer cells expressing the FerT protein, by comparison with non-expressers. Collectively, we show here that FerT is a new CTA whose accumulation in CC cells, commonly considered low CTA expressers, is controlled by a novel transcription regulatory mechanism.
MeSH term(s)	Amino Acid Sequence ; Base Sequence ; Cell Cycle/physiology ; Colonic Neoplasms/genetics ; Colonic Neoplasms/pathology ; Colonic Neoplasms/physiopathology ; DNA Methylation/genetics ; DNA-Binding Proteins/genetics ; Down-Regulation/genetics ; Gene Expression Regulation, Neoplastic/physiology ; HCT116 Cells ; Humans ; Introns/genetics ; Molecular Sequence Data ; Promoter Regions, Genetic/genetics ; Protein-Tyrosine Kinases/genetics ; RNA, Small Interfering/pharmacology ; Transcription Factors/genetics
Chemical Substances	CTCFL protein, human ; DNA-Binding Proteins ; RNA, Small Interfering ; Transcription Factors ; proto-oncogene protein c-fes-fps (110736-90-8) ; Protein-Tyrosine Kinases (EC 2.7.10.1)
Language	English
Publishing date	2012-01-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.327106
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Article ; Online: Down-regulation of Fer induces ROS levels accompanied by ATM and p53 activation in colon carcinoma cells.

Makovski, Adar / Yaffe, Etai / Shpungin, Sally / Nir, Uri

Cellular signalling

2012 Volume 24, Issue 7, Page(s) 1369–1374

Abstract	Fer is an intracellular tyrosine kinase which resides in both the cytoplasm and nucleus of mammalian cells. This kinase was also found in all malignant cell-lines analyzed and was shown to support cell-cycle progression in cancer cells. Herein we show that knock-down of Fer, both, impairs cell-cycle progression and imposes programmed cell death in colon carcinoma (CC) cells. The cell-cycle arrest and apoptotic death invoked by the depletion of Fer were found to depend on the activity of p53. Accordingly, down regulation of Fer led to the activation of the Ataxia Telangiectasia Mutated protein (ATM) and its down-stream effector-p53. Knock-down of Fer also increased the level of Reactive-Oxygen Species (ROS) in CC cells, and subjection of Fer depleted cells to ROS neutralizing scavengers significantly decreased the induced phosphorylation and activation of ATM and p53. Notably, over-expression of Fer opposed the Doxorubicin driven activation of ATM and p53, which can be mediated by ROS. Collectively, our findings imply that Fer sustains low ROS levels in CC cells, thereby restraining the activation of ATM and p53 in these cells.
MeSH term(s)	Apoptosis ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle ; Cell Cycle Proteins/genetics ; Cell Cycle Proteins/metabolism ; Cell Line, Tumor ; Colonic Neoplasms/genetics ; Colonic Neoplasms/metabolism ; DNA-Binding Proteins/genetics ; DNA-Binding Proteins/metabolism ; Gene Expression Regulation, Neoplastic ; HCT116 Cells ; Humans ; Mutation ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Protein-Tyrosine Kinases/genetics ; Protein-Tyrosine Kinases/metabolism ; RNA, Small Interfering/genetics ; Reactive Oxygen Species/metabolism ; Signal Transduction ; Tumor Suppressor Protein p53/genetics ; Tumor Suppressor Protein p53/metabolism ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism
Chemical Substances	Cell Cycle Proteins ; DNA-Binding Proteins ; RNA, Small Interfering ; Reactive Oxygen Species ; TP53 protein, human ; Tumor Suppressor Protein p53 ; Tumor Suppressor Proteins ; proto-oncogene protein c-fes-fps (110736-90-8) ; Protein-Tyrosine Kinases (EC 2.7.10.1) ; ATM protein, human (EC 2.7.11.1) ; Ataxia Telangiectasia Mutated Proteins (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2012-07
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1002702-6
ISSN	1873-3913 ; 0898-6568
ISSN (online)	1873-3913
ISSN	0898-6568
DOI	10.1016/j.cellsig.2012.03.004
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