3.p53-mediated HIV-1 Tat Suppression is Likely to be Assaciated with duble-stranded RNA-dependent Protein Kinase, PKR.
Jung Whan KIM ; Hee Sun BYUN ; Yong Soo BAE
Journal of the Korean Society of Virology 1999;29(4):235-245
No abstract available.
eIF-2 Kinase*
;
HIV-1*
;
Phosphorylation
4.Resveratrol suppresses breast cancer cell invasion by inactivating a RhoA/YAP signaling axis.
Yu Na KIM ; So Ra CHOE ; Kyung Hwa CHO ; Do Yeun CHO ; Jaeku KANG ; Chang Gyo PARK ; Hoi Young LEE
Experimental & Molecular Medicine 2017;49(2):e296-
Hippo/YAP signaling is implicated in tumorigenesis and progression of various cancers. By inhibiting a plethora signaling cascades, resveratrol has strong anti-tumorigenic and anti-metastatic activity. In the present study, we demonstrate that resveratrol decreases the expression of YAP target genes. In addition, our data showed that resveratrol attenuates breast cancer cell invasion through the activation of Lats1 and consequent inactivation of YAP. Strikingly, we also demonstrate that resveratrol inactivates RhoA, leading to the activation of Lats1 and induction of YAP phosphorylation. Further, resveratrol in combination with other agents that inactivate RhoA or YAP showed more marked suppression of breast cancer cell invasion compared with single treatment. Collectively, these findings indicate the beneficial effects of resveratrol on breast cancer patients by suppressing the RhoA/Lats1/YAP signaling axis and subsequently inhibiting breast cancer cell invasion.
Breast Neoplasms*
;
Breast*
;
Carcinogenesis
;
Humans
;
Phosphorylation
5.Quercetin-3-O-β-D-Glucuronide Suppresses Lipopolysaccharide-Induced JNK and ERK Phosphorylation in LPS-Challenged RAW264.7 Cells.
Jin Young PARK ; Man Sup LIM ; Song In KIM ; Hee Jae LEE ; Sung Soo KIM ; Yong Soo KWON ; Wanjoo CHUN
Biomolecules & Therapeutics 2016;24(6):610-615
Quercetin, a flavonol, has been reported to exhibit a wide range of biological properties including anti-oxidant and anti-inflammatory activities. However, pharmacological properties of quercetin-3-O-β-D-glucuronide (QG), a glycoside derivative of quercetin, have not been extensively examined. The objective of this study is to elucidate the anti-inflammatory property and underlying mechanism of QG in lipopolysaccharide (LPS)-challenged RAW264.7 macrophage cells in comparison with quercetin. QG significantly suppressed LPS-induced extracellular secretion of pro-inflammatory mediators such as nitric oxide (NO) and PGE2, and pro-inflammatory protein expressions of iNOS and COX-2. To elucidate the underlying mechanism of the anti-inflammatory property of QG, involvement of MAPK signaling pathways was examined. QG significantly attenuated LPS-induced activation of JNK and ERK in concentration-dependent manners with a negligible effect on p38. In conclusion, the present study demonstrates QG exerts anti-inflammatory activity through the suppression of JNK and ERK signaling pathways in LPS-challenged RAW264.7 macrophage cells.
Dinoprostone
;
Macrophages
;
Nitric Oxide
;
Phosphorylation*
;
Quercetin
6.Advances in the structure and physiological function of protein kinase CK2.
Chenchen WAN ; Yuanli CHEN ; Tingting FAN
Chinese Journal of Biotechnology 2021;37(12):4201-4214
Protein kinase CK2 is a common, evolutionarily conserved and ubiquitous protein kinase. In recent years, increasing evidences have shown that CK2 has a variety of phosphorylated protein substrates, which play important roles in growth, development and various diseases. Therefore, CK2 may participate in these physiological processes by regulating the phosphorylation of these substrates. This article briefly reviewed the structural characteristics of protein kinase CK2 and its physiological functions in growth, development, immunity, formation of tumor and other diseases, in order to provide knowledge basis for further research on the regulatory mechanism of CK2 and potential applications of its inhibitors.
Casein Kinase II/metabolism*
;
Phosphorylation
;
Proteins
7.Advances and application of enrichment technology in SH2 superbinder-based tyrosine phosphoproteomics.
Liying MEN ; Feng XU ; Ping XU
Chinese Journal of Biotechnology 2021;37(7):2334-2341
Tyrosine phosphorylation is one of the important protein phosphorylations in eukaryotes responsible for a variety of biological processes including cell signaling transduction, cell migration, and apoptosis. In the study of phosphoproteomics, due to the low stoichiometry of tyrosine phosphorylation (pTyr) proteins and sometimes limited initial sample, traditional phosphoproteomics enrichment technology is inefficient for the enrichment of pTyr peptides. Here, we review the substantial progress in tyrosine phosphoproteomics by preparation of limited amount sample and the newly introduced SH2 superbinder.
Cell Movement
;
Peptides
;
Phosphorylation
;
Technology
;
Tyrosine/metabolism*
8.A Case of Delayed Peripheral Polyneuropathy Induced by Organophosphorus Intoxication.
Won Young JUNG ; Myung Sik LEE ; Il Saing CHOI ; Je Geun CHI
Journal of the Korean Neurological Association 1988;6(2):261-267
Delayed peripheral polyneuropathy caused by organophosphorus intoxication is not uncommon. This is a case report of 32 years old female with peripheral polyneuropathy which is appeared two weeks after organophosphorus poisoning. It is characterized by calves pain followed by minmal sensory change and predominant motor weakness affecting the distal part of the limbs. The electrophysiologic and pathologic studies support the clinical diagnosis. The exact pathogenesis is still debated, but phosphorylation of neurotoxic esterase (NTE), followed by "aging" process was suspected to play a role in the development of axonal degeneration.
Adult
;
Axons
;
Diagnosis
;
Extremities
;
Female
;
Humans
;
Organophosphate Poisoning
;
Phosphorylation
;
Polyneuropathies*
9.Osteoactivin inhibition of osteoclastogenesis is mediated through CD44-ERK signaling.
Gregory R SONDAG ; Thomas S MBIMBA ; Fouad M MOUSSA ; Kimberly NOVAK ; Bing YU ; Fatima A JABER ; Samir M ABDELMAGID ; Werner J GELDENHUYS ; Fayez F SAFADI
Experimental & Molecular Medicine 2016;48(9):e257-
Osteoactivin is a heavily glycosylated protein shown to have a role in bone remodeling. Previous studies from our lab have shown that mutation in Osteoactivin enhances osteoclast differentiation but inhibits their function. To date, a classical receptor and a signaling pathway for Osteoactivin-mediated osteoclast inhibition has not yet been characterized. In this study, we examined the role of Osteoactivin treatment on osteoclastogenesis using bone marrow-derived osteoclast progenitor cells and identify a signaling pathway relating to Osteoactivin function. We reveal that recombinant Osteoactivin treatment inhibited osteoclast differentiation in a dose-dependent manner shown by qPCR, TRAP staining, activity and count. Using several approaches, we show that Osteoactivin binds CD44 in osteoclasts. Furthermore, recombinant Osteoactivin treatment inhibited ERK phosphorylation in a CD44-dependent manner. Finally, we examined the role of Osteoactivin on receptor activator of nuclear factor-κ B ligand (RANKL)-induced osteolysis in vivo. Our data indicate that recombinant Osteoactivin inhibits RANKL-induced osteolysis in vivo and this effect is CD44-dependent. Overall, our data indicate that Osteoactivin is a negative regulator of osteoclastogenesis in vitro and in vivo and that this process is regulated through CD44 and ERK activation.
Bone Remodeling
;
In Vitro Techniques
;
Osteoclasts
;
Osteolysis
;
Phosphorylation
;
Stem Cells
10.Regulation of MAPK Activity by Seizure-induced MKP-1 in Rat Hippocampus.
Bum Hee YU ; Ung Gu KANG ; Yong Min AHN ; Sun Ju CHUNG ; Song Hee JEON ; Joo Bae PARK ; Yong Sik KIM
Journal of Korean Neuropsychiatric Association 1999;38(4):873-880
OBJECTIVES: Both electroconvulsive shock(ECS) and kainic acid-induced seizures activate mitogenactivated protein kinases(MAPKs)in rat hippocampus. They can also induce the expression of MAPK phosphatase-1(MKP-1)in rat hippocampus. MKP-1 is known as a specific MAPK deactivator. This study aimed to elucidate the role of MKP-1 in the deactivation of MAPKs in rat hippocampus. METHODS: In order to induce MKP-1 in the hippocampus, ECS was given to the rats. At the time points when MKP-1 was sufficiently induced, the second ECS was given to them and the subsequent phosphorylation or activation of MAPKs were measured in the hippocampus. A second group of rats were injected with kainic acid and the relationship between MKP-1 expression and MAPK phosphorylation was examined in their hippocampi. RESULTS: The expression of MKP-1 did not influence the phosphorylation or activation of MAPKs following ECS in rat hippocampus. Kainic acid-induced expression of MKP-1 did not significantly reduce the phosphorylation of MAPKs. CONCLUSION: MKP-1 did not play a significant role in the deactivation of MAPKs which were activated by ECS or kainic acid in rat hippocampus.
Animals
;
Electroshock
;
Hippocampus*
;
Kainic Acid
;
Phosphorylation
;
Rats*
;
Seizures