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WonSikEum,MingZhenLi,GyeSukSin,SooYoungChoi,Jae-BongPark,JaeYongLee,HyeokYilKwon 생화학분자생물학회 2003 Experimental and molecular medicine Vol.35 No.5
Dexamethasone converts pluripotent pancreatic AR42J cels into exocrine cells expressing diges-tive enzymes. In order to adress molecular me-chanism of this diferentiation, we have investi-gated the role of mitogen-activated protein (MAP) kinase pathway and gene expresions of p21waf1/cip1 and nuclear oncogenes (c-fos and c-myc) during AR42J cell diferentiation. Dexamethasone marked-ly increased the intracellular and secreted amylase contents as wel as its mRNA level. However, cell growth and DNA content were significantly de-creased. With these phenotypic changes, AR42J cells induced transient mRNA expression of p21waf1/cip1gene, which reached maximal level by 6 h and then declined gradualy toward basal state. In contrast to p21waf1/cip1, c-fos gene expres-sion was transiently inhibited by 6 h and then recovered to basal level by 24 h. Increased c-myc expression detected after 3 h, peaked by 12 h, and remained elevated during the rest of observation. Dexamethasone inhibited epidermal growth factor- induced phosphorylation of extracelular signal regulated kinase. Inhibition of MAP kinase pathway by PD98059 resulted in further elevation of the de-xamethasone-induced amylase mRNA and p21waf1/cip1 gene expression. These results sugest that p21waf1/cip1 and nuclear oncogenes are involved in dexamethasone-induced diferentiation and inhi-bition of MAP kinase pathway accelerates the con-version of undiferentiated AR42J cels into am-ylase-secreting exocrine cels.
Production and Characterization of Monoclonal Antibodies against Human Ceruloplasmin
( Won Sik Eum ),( Hee Soon Choi ),( Dae Won Kim ),( Sang Ho Jang ),( Soo Hyun Choi ),( So Young Kim ),( Jin Seu Park ),( Jung Hoon Kang ),( Sung Woo Cho ),( Oh Shin Kwon ),( In Koo Hwang ),( Ki Yeon Y 생화학분자생물학회 2005 BMB Reports Vol.38 No.1
Ceruloplasmin (CP) is the major plasma antioxidant and copper transport protein. Monoclonal antibodies (mAbs) against human CP were produced and characterized. A total of five hybridoma cell lines were established (CP2, CP10, CP20, CP25, CP30). From the epitope mapping analysis, two subgroups of mAbs recognize different peptide fragments were identified. When the purified CP was incubated with the mAbs, the ferroxidase activity of CP was inhibited up to a maximum 57%. Immunoblotting with various tissue homogenates indicated that all the mAbs specifically recognize a single protein band of 130 kDa. They also appear to be extensively cross-reactive among different mammalian including human and avian sources. These results demonstrated that only one type of immunologically similar CP is present in all of the mammalian tissues including human. The CP mAbs could be of great benefit to design the diagnostic kit for CP-related diseases such as Wilson`s disease.
Human glutamate dehydrogenase is immunologically distinct from other mammalian orthologues
SangHoJang,AYeonKim,JaeHoonBahn,WonSikEum,김대원,JinseuPark,KilSooLee,Tae-CheonKang,원무호,JungHoonKang,Oh-ShinKwon,Hae-YoungYoon,Eun-YoungLee,Sung-WooCho,SooYoungChoi 생화학분자생물학회 2003 Experimental and molecular medicine Vol.35 No.4
Five monoclonal antibodies (mAbs) that recognizehuman glutamate dehydrogenase (GDH) have beenselected and designated as monoclonal antibodieshGDH60-6, hGDH60-8, hGDH63-10, hGDH63-11, andhGDH91-14. A total of five mAbs recognizing differentepitopes of the enzyme were obtained, two ofwhich inhibited human GDH activity. When totalproteins of human homogenate separated by SDSPAGE,were probed with mAbs, a single reactiveprotein band of 55 kDa, which co-migrated withpurified recombinant human GDH was detected. When the purified GDH was incubated with eachof the mAbs, its enzyme activity was inhibited byup to 58%. Epitope mapping analysis identified,two subgroups of mAbs recognizing different peptidefragments. Using the individual anti-GDH antibodiesas probes, the cross reactivities of brainGDH obtained from human and other animal braintissues were investigated. For the human and animaltissues tested, immunoreactive bands onWestern blots appeared to have the same molecularmass of 55 kDa when hGHD60-6, hGHD60-8,or hGHD91-14 mAbs were used as probes. However,the anti-human GDH mAbs immunoreactiveto bands on Western blots reacted differently onthe immunoblots of the other animal brains tested,i.e., the two monoclonal antibodies hGDH63-10and hGDH63-11 only produced positive results forhuman. These results suggest that human brainGDH is immunologically distinct from those ofother mammalian brains. Thorough characterizationof these anti-human GDH mAbs could providepotentially valuable tool as immunodiagnostic reagentsfor the detection, identification and characterizationof the various neurological diseases relatedto the GDH enzyme. Five monoclonal antibodies (mAbs) that recognize human glutamate dehydrogenase (GDH) have been selected and designated as monoclonal antibodies hGDH60-6, hGDH60-8, hGDH63-10, hGDH63-1, and hGDH91-14. A total of five mAbs recognizing differ-which inhibited human GDH activity. When total proteins of human homogenate separated by SDS- PAGE, were probed with mAbs, a single reactive protein band of 5 kDa, which co-migrated with purified recombinant human GDH was detected. When the purified GDH was incubated with each of the mAbs, its enzyme activity was inhibited by up to 58%. Epitope maping analysis identified, two subgroups of mAbs recognizing diferent pep-tide fragments. Using the individual anti-GDH anti-bodies as probes, the cross reactivities of brain tisues were investigated. For the human and ani-mal tissues tested, imunoreactive bands on Western blots appeared to have the same molec-ular mas of 55 kDa when hGHD60-6, hGHD60-8, or hGHD91-14 mAbs were used as probes. How-ever, the anti-human GDH mAbs imunoreactive to bands on Western blots reacted diferently on the imunoblots of the other animal brains tested, i.e., the two monoclonal antibodies hGDH63-10 and hGDH63-1 only produced positive results for human. These results suggest that human brain other mamalian brains. Thorough characterization of these anti-human GDH mAbs could provide potentially valuable tol as immunodiagnostic rea-gents for the detection, identification and charac-terization of the various neurological diseases re-lated to the GDH enzyme.
PEP-1-p18 prevents neuronal cell death by inhibiting oxidative stress and Bax expression
DukSooKim,EunJeongSohn,DaeWonKim,YoungNamKim,SeonAeEom,GaHyeonYoon,SungWooCho,SangHyunLee,HyunSookHwang,YoonShinCho,JinSeuPark,WonSikEum,SooYoungChoi 생화학분자생물학회 2012 BMB Reports Vol.45 No.9
P18, a member of the INK4 family of cyclin-dependent kinase inhibitors, is a tumor suppressor protein and plays a key cell survival role in a variety of human cancers. Under pathophysiological conditions, the INK4 group proteins participate in novel biological functions associated with neuronal diseases and oxidative stress. Parkinson`s disease (PD) is characterized by loss of dopaminergic neurons, and oxidative stress is important in its pathogenesis. Therefore, we examined the effects of PEP-1-p18 on oxidative stress-induced SH-SY5Y cells and in a PD mouse model. The transduced PEP-1-p18 markedly inhibited 1-methyl-4-phenyl pyridinium-induced SH-SY5Y cell death by inhibiting Bax expression levels and DNA fragmentation. Additionally, PEP-1-p18 prevented dopaminergic neuronal cell death in the substantia nigra of a 1-methyl-4-phenyl-1,2,3,6,-tetrahydropyridine-induced PD mouse model. These results indicate that PEP-1-p18 may be a useful therapeutic agent against various diseases and is a potential tool for treating PD. [BMB Reports 2012; 45(9): 532-537]