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Article ; Online: Blockade of isoprenoids biosynthesis by simvastatin induces autophagy-mediated cell death via downstream c-Jun N-terminal kinase activation and cell cycle dysregulation in canine T-cell lymphoma cells.

Kobayashi, Kosuke / Baba, Kenji / Kambayashi, Satoshi / Okuda, Masaru

2024 Volume 169, Page(s) 105174

Abstract: ... of simvastatin in canine lymphoma cells. Simvastatin induced cell death via c-Jun N-terminal kinase (JNK ...

Abstract	Statins are inhibitors of the mevalonic acid pathway that mediates cellular metabolism by producing cholesterol and isoprenoids and are widely used in treating hypercholesterolaemia in humans. Lipophilic statins, including simvastatin, induce death in various tumour cells. However, the cytotoxic mechanisms of statins in tumour cells remain largely unexplored. This study aimed to elucidate the cytotoxic mechanisms of simvastatin in canine lymphoma cells. Simvastatin induced cell death via c-Jun N-terminal kinase (JNK) activation and autophagy in canine T-cell lymphoma cell lines Ema and UL-1, but not in B-cell lines. Cell death was mediated by induction of caspase-dependent apoptosis in UL-1 cells, but not in Ema cells. Blockade of autophagy by lysosomal inhibitors attenuated simvastatin-induced JNK activation and cell death. Isoprenoids, including farnesyl pyrophosphate and geranylgeranyl pyrophosphate, attenuated simvastatin-induced autophagy, JNK activation, and cell death. In UL-1 cells, simvastatin treatment resulted in the cell cycle arrest at the G2/M phase, which was altered to G0/1 phase cell cycle arrest by treatment with lysosomal inhibitors. These findings demonstrate that depletion of isoprenoids by simvastatin induces autophagy-mediated cell death via downstream JNK activation and cell cycle dysregulation in canine T-cell lymphoma cells.
MeSH term(s)	Animals ; Dogs ; Humans ; Simvastatin/pharmacology ; Hydroxymethylglutaryl-CoA Reductase Inhibitors/pharmacology ; JNK Mitogen-Activated Protein Kinases/metabolism ; Cell Line, Tumor ; Cell Cycle ; Cell Division ; Apoptosis ; Cell Death ; Antineoplastic Agents/pharmacology ; Autophagy ; Lymphoma, T-Cell/drug therapy ; Lymphoma, T-Cell/veterinary ; Terpenes/pharmacology ; Dog Diseases/drug therapy
Chemical Substances	Simvastatin (AGG2FN16EV) ; Hydroxymethylglutaryl-CoA Reductase Inhibitors ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Antineoplastic Agents ; Terpenes
Language	English
Publishing date	2024-02-06
Publishing country	England
Document type	Journal Article
ZDB-ID	840961-4
ISSN	1532-2661 ; 0034-5288
ISSN (online)	1532-2661
ISSN	0034-5288
DOI	10.1016/j.rvsc.2024.105174
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Article ; Online: GLP-1 reduces the migration of hepatocellular carcinoma cells via suppression of the stress-activated protein kinase/c-Jun N-terminal kinase pathway.

Yamada, Noriko / Matsushima-Nishiwaki, Rie / Kobayashi, Kaido / Tachi, Junko / Kozawa, Osamu

Archives of biochemistry and biophysics

2021 Volume 703, Page(s) 108851

Abstract: ... the suppressive effect of GLP-1. GLP-1 attenuated the phosphorylation of stress-activated protein kinase/c-Jun N ...

Abstract	Incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), are hormones secreted from small intestine accompanied with oral intake. We previously showed that transforming growth factor (TGF)-α stimulates the migration of hepatocellular carcinoma (HCC) cells via mitogen-activated protein (MAP) kinases, AKT and Rho-kinase. However, it remains to be elucidated whether incretins affect HCC cell functions. In the present study, therefore, we investigated whether incretins affect the migration of HCC cells using human HCC-derived HuH7 cells. GLP-1, but not GIP, reduced both TGF-α- and hepatocyte growth factor (HGF)-induced cell migration. IBMX, an inhibitor of cyclic nucleotide phosphodiesterase, enhanced the suppressive effect of GLP-1. GLP-1 attenuated the phosphorylation of stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) by TGF-α and HGF. Our results strongly suggest that GLP-1 suppresses TGF-α- and HGF-induced migration of HCC cells through inhibiting the SAPK/JNK signaling pathway, and that the inhibition by GLP-1 is due to cAMP production.
MeSH term(s)	Carcinoma, Hepatocellular/pathology ; Cell Line, Tumor ; Cell Movement/drug effects ; Cyclic AMP/biosynthesis ; Glucagon-Like Peptide 1/pharmacology ; Hepatocyte Growth Factor/pharmacology ; Humans ; JNK Mitogen-Activated Protein Kinases/metabolism ; Liver Neoplasms/pathology ; Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation/drug effects ; Transforming Growth Factor alpha/pharmacology
Chemical Substances	Transforming Growth Factor alpha ; Hepatocyte Growth Factor (67256-21-7) ; Glucagon-Like Peptide 1 (89750-14-1) ; Cyclic AMP (E0399OZS9N) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24)
Language	English
Publishing date	2021-03-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2021.108851
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Article: GLP-1 reduces the migration of hepatocellular carcinoma cells via suppression of the stress-activated protein kinase/c-Jun N-terminal kinase pathway

Yamada, Noriko / Matsushima-Nishiwaki, Rie / Kobayashi, Kaido / Tachi, Junko / Kozawa, Osamu

Archives of biochemistry and biophysics. 2021 May 30, v. 703

2021

Abstract: ... the suppressive effect of GLP-1. GLP-1 attenuated the phosphorylation of stress-activated protein kinase/c-Jun N ...

Abstract	Incretins, glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP), are hormones secreted from small intestine accompanied with oral intake. We previously showed that transforming growth factor (TGF)-α stimulates the migration of hepatocellular carcinoma (HCC) cells via mitogen-activated protein (MAP) kinases, AKT and Rho-kinase. However, it remains to be elucidated whether incretins affect HCC cell functions. In the present study, therefore, we investigated whether incretins affect the migration of HCC cells using human HCC-derived HuH7 cells. GLP-1, but not GIP, reduced both TGF-α- and hepatocyte growth factor (HGF)-induced cell migration. IBMX, an inhibitor of cyclic nucleotide phosphodiesterase, enhanced the suppressive effect of GLP-1. GLP-1 attenuated the phosphorylation of stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) by TGF-α and HGF. Our results strongly suggest that GLP-1 suppresses TGF-α- and HGF-induced migration of HCC cells through inhibiting the SAPK/JNK signaling pathway, and that the inhibition by GLP-1 is due to cAMP production.
Keywords	biophysics ; cell movement ; gastric inhibitory polypeptide ; glucagon-like peptide 1 ; hepatocyte growth factor ; hepatoma ; humans ; phosphorylation ; small intestine
Language	English
Dates of publication	2021-0530
Publishing place	Elsevier Inc.
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2021.108851
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Article ; Online: Role of c-Jun N-terminal kinase isoforms in the cellular activity of melanoma cell lines.

Kogushi-Nishi, H / Jinnin, M / Kobayashi, Y / Muchemwa, F C / Hirano, A / Makino, T / Fukushima, S / Masuguchi, S / Ishihara, T / Inoue, Y / Ihn, H

Clinical and experimental dermatology

2013 Volume 38, Issue 8, Page(s) 890–896

Abstract: Background: The c-Jun N-terminal kinase (JNK) is thought to be involved in inflammation ...

Abstract	Background: The c-Jun N-terminal kinase (JNK) is thought to be involved in inflammation, proliferation and apoptosis. Aim: To examine the role of JNK isoforms in metastasis, proliferation, migration and invasion of the malignant melanoma (MM) cell lines SK-MEL-28, SK-MEL-3 and WM164, using a kinase-specific inhibitor or isoform-specific small interfering (si)RNAs. Results: SK-MEL-3, a cell line established from metastatic MM, showed slightly increased phosphorylation of both JNK1 and JNK2, whereas WM164, a cell line derived from primary MM, showed significant phosphorylation of JNK1. A JNK inhibitor, SP600125, inhibited cell proliferation of SK-MEL-3 but not SK-MEL-28 or WM164. Transfection of JNK1-specific siRNA reduced the migratory activity of WM164 cells, while silencing of either JNK1 or JNK2 strongly suppressed the invasive activity of SK-MEL-3. Conclusions: Our study suggests that JNK isoforms have different roles in MM. Metastasis of MM may be regulated by JNK2, while invasion is regulated by both JNK1 and JNK2. JNK1 and JNK2 respectively mediate cell migration and cell proliferation. Further understanding of the specific roles of JNK isoforms in the pathogenesis of MM may lead to the development of therapies targeting specific isoforms.
MeSH term(s)	Anthracenes/pharmacology ; Cell Line, Tumor ; Cell Movement/drug effects ; Cell Proliferation/drug effects ; Humans ; Immunoblotting ; JNK Mitogen-Activated Protein Kinases/antagonists & inhibitors ; Melanoma/enzymology ; Melanoma/pathology ; Mitogen-Activated Protein Kinase 8/physiology ; Mitogen-Activated Protein Kinase 9/physiology ; Neoplasm Invasiveness ; Protein Isoforms/physiology ; Skin Neoplasms/enzymology ; Skin Neoplasms/pathology
Chemical Substances	Anthracenes ; Protein Isoforms ; pyrazolanthrone (1TW30Y2766) ; Mitogen-Activated Protein Kinase 9 (EC 2.7.1.24) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinase 8 (EC 2.7.11.24)
Language	English
Publishing date	2013-12
Publishing country	England
Document type	Journal Article
ZDB-ID	195504-4
ISSN	1365-2230 ; 0307-6938
ISSN (online)	1365-2230
ISSN	0307-6938
DOI	10.1111/ced.12102
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Zs.A 1278: Show issues

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Article: Activation mechanism of c-Jun amino-terminal kinase in the course of neural differentiation of P19 embryonic carcinoma cells.

Akiyama, Shoko / Yonezawa, Takayuki / Kudo, Tada-Aki / Li, Ming Guang / Wang, Hong / Ito, Michihiko / Yoshioka, Katsuji / Ninomiya-Tsuji, Jun / Matsumoto, Kunihiro / Kanamaru, Ryunosuke / Tamura, Shinri / Kobayashi, Takayasu

The Journal of biological chemistry

2004 Volume 279, Issue 35, Page(s) 36616–36620

Abstract: ... previously reported that the activation of c-Jun amino-terminal kinase (JNK) is required for the retinoic ...

Abstract	P19 embryonic carcinoma cells, a model system for studying early development and differentiation, can differentiate into neurons and primitive endoderm-like cells depending on the culture conditions. We have previously reported that the activation of c-Jun amino-terminal kinase (JNK) is required for the retinoic acid-induced neural differentiation of P19 cells. However, the signaling pathway(s) responsible for the activation of JNK has not been known. In this study, we demonstrated that activities of MAPK kinase 4 (MKK4) and TAK1, one of the upstream kinases of MKK4, were enhanced in the neurally differentiating cells. Inhibition of the neural differentiation by an overexpression of protein phosphatase 2Cepsilon, an inactivator of TAK1, suggested a critical role of the TAK1 signaling pathway during the differentiation. Confocal microscopic analysis indicated that TAK1, phospho-MKK4, and phospho-JNK were colocalized with tubulin in the neurites and localized also in the nuclei of the differentiating cells. In contrast, two TAK1-binding proteins, TAB1 and TAB2, which are involved in the activation of TAK1, were localized in the neurites and the nuclei of the differentiating cells, respectively. These results suggest that two distinct TAK1-MKK4-JNK signaling pathways are independently activated at the different intracellular locations and may participate in the regulation of the neural differentiation of P19 cells.
MeSH term(s)	Animals ; Blotting, Northern ; Carcinoma, Embryonal/metabolism ; Cell Differentiation ; Cell Line ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Enzyme Activation ; Fluorescent Antibody Technique, Indirect ; Gene Expression Regulation, Developmental ; JNK Mitogen-Activated Protein Kinases ; MAP Kinase Kinase Kinase 4 ; MAP Kinase Kinase Kinases/metabolism ; Mice ; Microscopy, Confocal ; Mitogen-Activated Protein Kinases/metabolism ; Neurons/metabolism ; Phosphoprotein Phosphatases/metabolism ; Precipitin Tests ; Protein Phosphatase 2C ; Signal Transduction ; Transfection ; Tretinoin/metabolism ; Tubulin/metabolism
Chemical Substances	Tubulin ; Tretinoin (5688UTC01R) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; MAP Kinase Kinase Kinase 4 (EC 2.7.11.25) ; MAP Kinase Kinase Kinases (EC 2.7.11.25) ; MAP kinase kinase kinase 7 (EC 2.7.11.25) ; Map3k4 protein, mouse (EC 2.7.11.25) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Protein Phosphatase 2C (EC 3.1.3.16)
Language	English
Publishing date	2004-06-24
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.M406610200
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Article ; Online: Activation of the transcription factor c-Jun in acute cellular and antibody-mediated rejection after kidney transplantation.

Kobayashi, Akimitsu / Takahashi, Takamune / Horita, Shigeru / Yamamoto, Izumi / Yamamoto, Hiroyasu / Teraoka, Satoshi / Tanabe, Kazunari / Hosoya, Tatsuo / Yamaguchi, Yutaka

Human pathology

2010 Volume 41, Issue 12, Page(s) 1682–1693

Abstract: c-Jun is a transcription factor that belongs to the activator protein-1 family of proteins ... In human kidney disease, c-Jun is activated in glomerular and tubular cells and plays a major role in renal ... We investigated whether c-Jun is activated in acute allograft rejection. c-Jun activation was assessed ...

Abstract	c-Jun is a transcription factor that belongs to the activator protein-1 family of proteins. In human kidney disease, c-Jun is activated in glomerular and tubular cells and plays a major role in renal pathophysiology. However, the contribution of this pathway to renal allograft rejection has not been determined. We investigated whether c-Jun is activated in acute allograft rejection. c-Jun activation was assessed with immunohistochemistry using phospho-specific c-Jun antibodies in control human renal tissue and renal tissue from patients with acute cellular rejection, acute antibody-mediated rejection, and no rejection in the month after transplantation. In patients with acute cellular rejection, c-Jun activation was observed primarily in infiltrated T cells associated with tubulitis, interstitial cell infiltration, and endarteritis. The number of infiltrated phosphorylated c-Jun-positive cells in the tubules and interstitium was correlated with the Banff classification "t" and "i" scores. In patients with acute antibody-mediated rejection, c-Jun activation was observed in injured endothelial cells as well as in infiltrated cells, including macrophages, in the glomerular and peritubular capillaries. Furthermore, the serum creatinine levels and changes in serum creatinine from the previous year were significantly correlated with the total tubulointerstitial phosphorylated c-Jun-positive score (representing the number of positive nuclei in the tubules, interstitium, and peritubular capillaries). In conclusion, c-Jun was activated in acute antibody-mediated rejection and acute cellular rejection and was associated with reduced graft function. These findings suggest that c-Jun plays a key role in pathological events and may represent a novel therapeutic target in acute renal allograft rejection.
MeSH term(s)	Acute Disease ; Adult ; Antibodies/immunology ; Biopsy ; Endothelial Cells/metabolism ; Endothelial Cells/pathology ; Female ; Fluorescent Antibody Technique, Indirect ; Graft Rejection/metabolism ; Graft Rejection/pathology ; Humans ; Kidney/metabolism ; Kidney Diseases/metabolism ; Kidney Diseases/pathology ; Kidney Transplantation ; MAP Kinase Kinase 4/metabolism ; Male ; Phosphorylation ; Proto-Oncogene Proteins c-jun/metabolism ; T-Lymphocytes/immunology ; T-Lymphocytes/pathology
Chemical Substances	Antibodies ; Proto-Oncogene Proteins c-jun ; MAP Kinase Kinase 4 (EC 2.7.12.2)
Language	English
Publishing date	2010-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	207657-3
ISSN	1532-8392 ; 0046-8177
ISSN (online)	1532-8392
ISSN	0046-8177
DOI	10.1016/j.humpath.2010.04.016
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Zs.A 722: Show issues

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Article: c-Jun N-terminal kinase pathway mediates Lactacystin-induced cell death in a neuronal differentiated Neuro2a cell line.

Sang, Chen / Kobayashi, Yasushi / Du, Jun / Katsumo, Masahisa / Adachi, Hiroaki / Doyu, Manabu / Sobue, Gen

Brain research. Molecular brain research

2002 Volume 108, Issue 1-2, Page(s) 7–17

Abstract: ... of c-Jun N-terminal kinase, p38 and caspase-3. A pan-caspase inhibitor, Z-VAD-FMK, or SB203580, a p38 ... expression of the dominant negative mutant of c-Jun N-terminal kinase showed a remarkable suppression ... of cell death. Lactacystin-induced cell death is mediated through the c-Jun N-terminal kinase pathway but not ...

Abstract	The ubiquitin-proteasome pathway is an intracellular protein degradation pathway responsible for degradation of many regulatory proteins that must be rapidly eliminated normally. Some recent studies reported that a proteasome dysfunction was involved in the pathogenesis of neurodegenerative diseases. Thus, there is now considerable interest in the possible role of proteasome in this regard. Here we show that inhibition of proteasomal function by Lactacystin-induced cell death in a neuronal differentiated Neuro2a (nN2a) cell line but not in an undifferentiated Neuro2a (N2a) cell line. Cell death was accompanied by both the activation of c-Jun N-terminal kinase, p38 and caspase-3. A pan-caspase inhibitor, Z-VAD-FMK, or SB203580, a p38 inhibitor could not inhibit cell death induced by Lactacystin, whereas nN2a cell lines with stable expression of the dominant negative mutant of c-Jun N-terminal kinase showed a remarkable suppression of cell death. Lactacystin-induced cell death is mediated through the c-Jun N-terminal kinase pathway but not the caspase-dependent pathway in a nN2a cell line. Our results shed light on the association among the proteasomal dysfunction, JNK pathway and neuronal cell death, leading to the elucidation of its possible role in the pathogenesis of neurodegenerative diseases.
MeSH term(s)	Acetylcysteine/analogs & derivatives ; Acetylcysteine/pharmacology ; Amino Acid Chloromethyl Ketones/pharmacology ; Animals ; Caspase 3 ; Caspase Inhibitors ; Caspases/metabolism ; Cell Death/physiology ; Cell Nucleus/metabolism ; Cysteine Endopeptidases/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation ; JNK Mitogen-Activated Protein Kinases ; Mice ; Mitogen-Activated Protein Kinases/genetics ; Mitogen-Activated Protein Kinases/metabolism ; Multienzyme Complexes/antagonists & inhibitors ; Multienzyme Complexes/metabolism ; Neurons/cytology ; Neurons/drug effects ; Neurons/metabolism ; Proteasome Endopeptidase Complex ; Tumor Cells, Cultured ; p38 Mitogen-Activated Protein Kinases
Chemical Substances	Amino Acid Chloromethyl Ketones ; Caspase Inhibitors ; Cysteine Proteinase Inhibitors ; Multienzyme Complexes ; benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone ; lactacystin (133343-34-7) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; Casp3 protein, mouse (EC 3.4.22.-) ; Caspase 3 (EC 3.4.22.-) ; Caspases (EC 3.4.22.-) ; Cysteine Endopeptidases (EC 3.4.22.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Acetylcysteine (WYQ7N0BPYC)
Language	English
Publishing date	2002-11-21
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632883-0
ISSN	1872-6941 ; 0169-328X
ISSN (online)	1872-6941
ISSN	0169-328X
DOI	10.1016/s0169-328x(02)00460-6
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Zs.A 2181: Show issues

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Article ; Online: BCR-ABL promotes neutrophil differentiation in the chronic phase of chronic myeloid leukemia by downregulating c-Jun expression.

Kobayashi, S / Kimura, F / Ikeda, T / Osawa, Y / Torikai, H / Kobayashi, A / Sato, K / Motoyoshi, K

Leukemia

2009 Volume 23, Issue 9, Page(s) 1622–1627

Abstract: ... tyrosine kinase BCR-ABL, remains obscure. In this study, microarray analysis revealed that c-Jun, a monopoiesis ... promoting transcription factor, was downregulated in CML neutrophils. BCR-ABL directly inhibited c-Jun ... expression, as c-Jun downregulation in primary CML neutrophils and in the CML blast cell lines, KCL22 and ...

Abstract	The mechanism that is responsible for mature neutrophil overproduction in the chronic phase (CP) of chronic myeloid leukemia (CML), a neoplastic disease of hematopoietic stem cells carrying a constitutively active tyrosine kinase BCR-ABL, remains obscure. In this study, microarray analysis revealed that c-Jun, a monopoiesis-promoting transcription factor, was downregulated in CML neutrophils. BCR-ABL directly inhibited c-Jun expression, as c-Jun downregulation in primary CML neutrophils and in the CML blast cell lines, KCL22 and K562, was reversed by the tyrosine kinase inhibitor imatinib. We established a myeloid differentiation model in KCL22 cells using zinc-inducible CCAAT/enhancer-binding protein (C/EBP)alpha (KCL22/alpha). Myeloid differentiation was observed in C/EBP-induced KCL22/alpha cells. Imatinib-induced c-Jun upregulation promoted the monocytic differentiation of KCL22/alpha cells. c-Jun knockdown in KCL22/alpha cells by a short interfering RNA redirected their differentiation from the monocytic to the neutrophilic lineage, even after imatinib treatment. A blockade of PI3K-Akt signaling with an Akt inhibitor upregulated c-Jun and induced the monocytic differentiation of KCL22, K562, and C/EBP-induced KCL22/alpha cells. Thus, BCR-ABL downregulates c-Jun expression by activating the PI3K-Akt pathway during CML-CP, thereby allowing C/EBPs to promote neutrophil differentiation.
MeSH term(s)	Benzamides ; CCAAT-Enhancer-Binding Protein-alpha/genetics ; CCAAT-Enhancer-Binding Protein-alpha/physiology ; Cell Differentiation ; Down-Regulation ; Fusion Proteins, bcr-abl/physiology ; Gene Expression Profiling ; Humans ; Imatinib Mesylate ; Leukemia, Myeloid, Chronic-Phase/pathology ; Neutrophils/cytology ; Neutrophils/metabolism ; Phosphatidylinositol 3-Kinases/physiology ; Piperazines/pharmacology ; Proto-Oncogene Proteins c-akt/physiology ; Proto-Oncogene Proteins c-jun/antagonists & inhibitors ; Pyrimidines/pharmacology
Chemical Substances	Benzamides ; CCAAT-Enhancer-Binding Protein-alpha ; Piperazines ; Proto-Oncogene Proteins c-jun ; Pyrimidines ; Imatinib Mesylate (8A1O1M485B) ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Fusion Proteins, bcr-abl (EC 2.7.10.2) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2009-09
Publishing country	England
Document type	Journal Article
ZDB-ID	807030-1
ISSN	1476-5551 ; 0887-6924
ISSN (online)	1476-5551
ISSN	0887-6924
DOI	10.1038/leu.2009.74
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Zs.A 2295: Show issues

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Article: Clinicopathological impacts of activated transcription factor c-Jun in peritubular capillary endothelial cells in chronic antibodymediated rejection after kidney transplantation.

Kobayashi, Akimitsu / Takahashi, Takamune / Horita, Shigeru / Yamamoto, Izumi / Yamamoto, Hiroyasu / Tanabe, Kazunari / Yamaguchi, Yutaka / Hosoya, Tatsuo

Clinical nephrology

2011 Volume 77, Issue 1, Page(s) 32–39

Abstract: Aim: The transcription factor c-Jun is a major component of the activator protein-1 complex ... involved in renal physiological events, such as inflammation and fibrosis. We recently demonstrated c-Jun ... rejection after kidney transplantation. However, the clinicopathological role of PC endothelial c-Jun ...

Abstract	Aim: The transcription factor c-Jun is a major component of the activator protein-1 complex involved in renal physiological events, such as inflammation and fibrosis. We recently demonstrated c-Jun activation in peritubular capillary (PC) endothelial cells and infiltrating cells in acute antibody-mediated rejection after kidney transplantation. However, the clinicopathological role of PC endothelial c-Jun activation has remained undetermined. Material and method: We investigated endothelial c-Jun activation in PC using phosphorylated c-Jun (p-c-Jun) immunohistochemical staining in 21 cases of chronic active antibody-mediated rejection (CAMR), 14 cases of interstitial fibrosis and tubular atrophy (IF/TA) lacking specific etiology, and 8 normal control subjects (NC). Results: In CAMR cases, swollen PC endothelial cells showed strong p-c-Jun staining. More p-c-Jun-positive endothelial cells in PC were observed in CAMR than in IF/TA and NC subjects (p < 0.01). These findings were significantly correlated with reduced PC (rs = -0.78, p = 0.0005), the "ci + ct" score of the Banff classification (rs = 0.81, p = 0.0003) and serum creatinine level (rs = 0.48, p = 0.03). Conclusion: Endothelial c-Jun activation in PC may contribute to PC loss, interstitial fibrosis and late allograft deterioration in CAMR. These data suggest that c-Jun is an appropriate therapeutic target of CAMR.
MeSH term(s)	Adult ; Capillaries/pathology ; Capillaries/ultrastructure ; Chronic Disease ; Disease Progression ; Endothelial Cells/immunology ; Endothelial Cells/metabolism ; Endothelial Cells/pathology ; Graft Rejection/immunology ; Graft Rejection/metabolism ; Graft Rejection/pathology ; Humans ; Kidney/immunology ; Kidney/metabolism ; Kidney/pathology ; Kidney Transplantation/immunology ; Microscopy, Electron ; Middle Aged ; Primary Graft Dysfunction/immunology ; Primary Graft Dysfunction/metabolism ; Primary Graft Dysfunction/pathology ; Proto-Oncogene Proteins c-jun/immunology ; Proto-Oncogene Proteins c-jun/metabolism ; Transplantation, Homologous
Chemical Substances	Proto-Oncogene Proteins c-jun
Language	English
Publishing date	2011-12-15
Publishing country	Germany
Document type	Journal Article
ZDB-ID	185101-9
ISSN	0301-0430
ISSN	0301-0430
DOI	10.5414/cn107246
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Article ; Online: Phosphorylation of protein phosphatase 2Czeta by c-Jun NH2-terminal kinase at Ser92 attenuates its phosphatase activity.

Awano, Kenjiro / Amano, Kazutaka / Nagaura, Yuko / Kanno, Shin-ichiro / Echigo, Seishi / Tamura, Shinri / Kobayashi, Takayasu

Biochemistry

2008 Volume 47, Issue 27, Page(s) 7248–7255

Abstract: ... germ cells, is phosphorylated by c-Jun NH 2-terminal kinase (JNK) but not by p38 in vitro. Mass spectrometry ...

Abstract	The protein phosphatase 2C (PP2C) family represents one of the four major protein Ser/Thr phosphatase activities in mammalian cells and contains at least 13 distinct gene products. Although PP2C family members regulate a variety of cellular functions, mechanisms of regulation of their activities are largely unknown. Here, we show that PP2Czeta, a PP2C family member that is enriched in testicular germ cells, is phosphorylated by c-Jun NH 2-terminal kinase (JNK) but not by p38 in vitro. Mass spectrometry and mutational analyses demonstrated that phosphorylation occurs at Ser (92), Thr (202), and Thr (205) of PP2Czeta. Phosphorylation of these Ser and Thr residues of PP2Czeta ectopically expressed in 293 cells was enhanced by osmotic stress and was attenuated by a JNK inhibitor but not by p38 or MEK inhibitors. Phosphorylation of PP2Czeta by TAK1-activated JNK repressed its phosphatase activity in cells, and alanine mutation at Ser (92) but not at Thr (202) or Thr (205) suppressed this inhibition. Taken together, these results suggest that specific phosphorylation of PP2Czeta at Ser (92) by stress-activated JNK attenuates its phosphatase activity in cells.
MeSH term(s)	Amino Acid Sequence ; Animals ; Cell Line ; Humans ; JNK Mitogen-Activated Protein Kinases/metabolism ; Mice ; Molecular Sequence Data ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Phosphoprotein Phosphatases/chemistry ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Protein Phosphatase 2C
Chemical Substances	Phosphoserine (17885-08-4) ; JNK Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; PPM1A protein, human (EC 3.1.3.16) ; PPM1B protein, human (EC 3.1.3.16) ; PPM1G protein, human (EC 3.1.3.16) ; Phosphoprotein Phosphatases (EC 3.1.3.16) ; Protein Phosphatase 2C (EC 3.1.3.16)
Language	English
Publishing date	2008-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi800067p
Database	MEDical Literature Analysis and Retrieval System OnLINE

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