関: Bcl-X protein

WordNet

the 2nd letter of the Roman alphabet (同)b
the blood group whose red cells carry the B antigen (同)type_B, group B
any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"

PrepTutorEJDIC

蛋白(たんばく)質
extra large
x-axis

UpToDate Contents

全文を閲覧するには購読必要です。 To read the full text you will need to subscribe.

1. 成人における一次救命処置 basic life support bls in adults
2. 幼児および小児における一次救命処置 basic life support in infants and children
3. 突然の心停止の転帰 outcome of sudden cardiac arrest
4. 成人における二次救命処置（ACLS） advanced cardiac life support acls in adults
5. バーキットリンパ腫の疫学、臨床症状、病理学的特徴、および診断 epidemiology clinical manifestations pathologic features and diagnosis of burkitt lymphoma

English Journal

Capillarisin inhibits constitutive and inducible STAT3 activation through induction of SHP-1 and SHP-2 tyrosine phosphatases.

Lee JH1, Chiang SY1, Nam D1, Chung WS1, Lee J1, Na YS2, Sethi G3, Ahn KS4.Author information 1College of Korean Medicine, Kyung Hee University, 1 Hoegidong Dongdaemun-Gu, Seoul 130-701, Republic of Korea.2Asan Institute for Life Science, Asan Medical Center, Seoul 138-736, Republic of Korea.3Department of Pharmacology, Yong Loo Lin School of Medicine, Cancer Science Institute of Singapore, National University of Singapore, Singapore 117597, Singapore.4College of Korean Medicine, Kyung Hee University, 1 Hoegidong Dongdaemun-Gu, Seoul 130-701, Republic of Korea. Electronic address: ksahn@khu.ac.kr.AbstractSignal transducers and activators of transcription (STAT)-3 is a latent cytosolic transcription factor that has been closely associated with survival, proliferation, chemoresistance, and metastasis of tumor cells. Whether the anti-proliferative, pro-apoptotic, and anti-metastatic effects of capillarisin (CPS), derived from Artemisia capillaris (Compositae), are linked to its capability to inhibit STAT3 activation was investigated. We found that CPS specifically inhibited both constitutive and inducible STAT3 activation at tyrosine residue 705 but not at serine residue 727 in human multiple myeloma cells. Besides the inhibition of STAT3 phosphorylation, CPS also abrogated STAT3 constitutive activity and nuclear translocation. The suppression of STAT3 was mediated through the inhibition of activation of upstream JAK1, JAK2, and c-Src kinases. Treatment with the protein tyrosine phosphatase (PTP) inhibitor pervanadate treatment reversed the CPS-induced down-regulation of JAK1/2 and STAT3, thereby suggesting the involvement of a PTP. Indeed, knockdown of the SHP-1 and SHP-2 genes by small interfering RNA suppressed the ability of CPS to inhibit JAK1 and STAT3 activation, suggesting the critical role of both SHP-1 and SHP-2 in its possible mechanism of action. CPS downregulated the expression of STAT3-regulated antiapoptotic and proliferative gene products; and this correlated with suppression of cell viability, the accumulation of cells in sub-G1 phase of cell cycle and induction of apoptosis. Moreover, CPS potentiated bortezomib-induced apoptotic effects in MM cells, and this correlated with down-regulation of various gene products that mediate cell proliferation (Cyclin D1 and COX-2), cell survival (Bcl-2, Bcl-xl, IAP1, IAP2, and Survivin), invasion (MMP-9), and angiogenesis (VEGF). Thus, overall, our results suggest that CPS is a novel blocker of STAT3 activation and thus may have a potential in negative regulation of growth, metastasis, and chemoresistance of tumor cells.
Cancer letters.Cancer Lett.2014 Apr 1;345(1):140-8. doi: 10.1016/j.canlet.2013.12.008. Epub 2013 Dec 11.
Signal transducers and activators of transcription (STAT)-3 is a latent cytosolic transcription factor that has been closely associated with survival, proliferation, chemoresistance, and metastasis of tumor cells. Whether the anti-proliferative, pro-apoptotic, and anti-metastatic effects of capillar
PMID 24333736

High-mobility group box 1 (HMGB1) protein regulates tumor-associated cell migration through the interaction with BTB domain.

Ko YB1, Kim BR2, Nam SL1, Yang JB1, Park SY2, Rho SB3.Author information 1Department of Obstetrics and Gynecology, Chungnam National University Hospital, 282, Munhwa-ro, Jung-gu, Daejeon 301-721, Republic of Korea.2Research Institute, National Cancer Center, 323, Ilsan-ro, Ilsandong-gu, Goyang-si, Gyeonggi-do 410-769, Republic of Korea.3Research Institute, National Cancer Center, 323, Ilsan-ro, Ilsandong-gu, Goyang-si, Gyeonggi-do 410-769, Republic of Korea. Electronic address: sbrho@ncc.re.kr.AbstractHigh-mobility group box 1 (HMGB1) was shown to be strongly implicated in high incidences of metastasis and the poor clinical pathologic conditions found in various human tumors. In this study, we explored the possible mechanism of HMGB1 in tumor metastases in vitro, using a human carcinoma cell system. BTB, as a negative regulator of cell cycle progression, was identified as a HMGB1 interacting partner. The ectopic expression of HMGB1 activates cell growth by suppressing BTB-induced cell death, decreasing Bax and p53 expression, while enhancing Bcl-xL, Bcl-2, cyclin D1, and NF-κB expression. HMGB1 activates the FAK/PI3K/mTOR signaling cascade, and BTB prominently inhibits HMGB1-induced oncogenesis. The effect of HMGB1 on FAK/mTOR signaling was also confirmed through the silencing of HMGB1 expression. These insights provide evidence that HMGB1 enhances cell proliferation and suppresses apoptosis. Collectively, our results show an underlying mechanism for an HMGB1-associated promotion of carcinoma cells.
Cellular signalling.Cell Signal.2014 Apr;26(4):777-83. doi: 10.1016/j.cellsig.2013.12.018. Epub 2014 Jan 8.
High-mobility group box 1 (HMGB1) was shown to be strongly implicated in high incidences of metastasis and the poor clinical pathologic conditions found in various human tumors. In this study, we explored the possible mechanism of HMGB1 in tumor metastases in vitro, using a human carcinoma cell syst
PMID 24412753

Apoptotic cell death and altered calcium homeostasis caused by frataxin depletion in dorsal root ganglia neurons can be prevented by BH4 domain of Bcl-xL protein.

Mincheva-Tasheva S1, Obis E, Tamarit J, Ros J.Author information 1Grup de Bioquímica de L'Estrès Oxidatiu, Departament de Ciències Mèdiques Bàsiques, IRB Lleida, Universitat de Lleida, Lleida, Spain.AbstractFriedreich ataxia (FRDA) is a neurodegenerative disease characterized by a decreased expression of the mitochondrial protein frataxin. Major neurological symptoms of the disease are due to degeneration of dorsal root ganglion (DRG) sensory neurons. In this study we have explored the neurodegenerative events occurring by frataxin depletion on primary cultures of neurons obtained from rat DRGs. Reduction of 80% of frataxin levels in these cells was achieved by transduction with lentivirus containing shRNA silencing sequences. Frataxin depletion caused mitochondrial membrane potential decrease, neurite degeneration and apoptotic cell death. A marked increase of free intracellular Ca(2+) levels and alteration in Ca(2+)-mediated signaling pathways was also observed, thus suggesting that altered calcium homeostasis can play a pivotal role in neurodegeneration caused by frataxin deficiency. These deleterious effects were reverted by the addition of a cell-penetrant TAT peptide coupled to the BH4, the anti-apoptotic domain of Bcl-xL. Treatment of cultured frataxin-depleted neurons with TAT-BH4 was able to restore the free intracellular Ca(2+) levels and protect the neurons from degeneration. These observations open the possibility of new therapies of FRDA based on modulating the Ca(2+) signaling and prevent apoptotic process to protect DRG neurons from neurodegeneration.
Human molecular genetics.Hum Mol Genet.2014 Apr 1;23(7):1829-41. doi: 10.1093/hmg/ddt576. Epub 2013 Nov 15.
Friedreich ataxia (FRDA) is a neurodegenerative disease characterized by a decreased expression of the mitochondrial protein frataxin. Major neurological symptoms of the disease are due to degeneration of dorsal root ganglion (DRG) sensory neurons. In this study we have explored the neurodegenerativ
PMID 24242291

Japanese Journal

Ursolic Acid Induces Apoptosis Through Mitochondrial Intrinsic Pathway and Suppression of ERK1/2 MAPK in HeLa Cells

Li Yanhong,Lu Xueying,Qi Hongxue,Li Xiaobo,Xiao Xiangwen,Gao Jianfeng
Journal of Pharmacological Sciences 125(2), 202-210, 2014
… Here, we reported that UA induced apoptosis through the mitochondrial intrinsic pathway in HeLa cells, as shown by release of cytosol cytochrome c, activation of caspase-9 and -3, reduction of Bcl-2 and Bcl-xL, and increase of Bax and Bak. …
NAID 130004438631

Combination of guanine arabinoside and Bcl-2 inhibitor YC137 overcome the cytarabine resistance in HL-60 leukemia cell line.

Nishi Rie,Yamauchi Takahiro,Negoro Eiju,Takemura Haruyuki,Ueda Takanori
Cancer Science 104, 502-507, 2013-04
… Here, we established a new ara-C-resistant acute myeloid leukemia cell line (HL-60/ara-C60) with dual resistance characteristics of the anti-antimetabolic character of decreased ara-CTP production and an increase in the antiapoptotic factors Bcl-2 and Bcl-XL. … HL-60/ara-C60 cells exhibited low capacity for dCK protein expression, which resulted in decreased ara-CTP production. …
NAID 120005254373

Protease activity of procaspase-8 is essential for cell survival by inhibiting both apoptotic and nonapoptotic cell death dependent on receptor-interacting protein kinase 1 (RIP1) and RIP3.

Kikuchi Mina,Kuroki Shunsuke,Kayama Mitsuhiro,Sakaguchi Shota,Lee Kyung-Kwon,Yonehara Shin
The Journal of biological chemistry 287(49), 41165-41173, 2012-11-30
… The cell death was inhibited completely by treatment with ROS scavengers, but only partly by treatment with caspase inhibitors, expression of Bcl-xL, and knockdown of caspase-3 or Atg-7 which completely inhibits apoptosis or autophagosome formation, respectively, indicating that apoptosis and autophagy-associated cell death are induced simultaneously by the knockdown of caspase-8 expression. …
NAID 120005385882