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Kwon, Hyeok Yil,Lim, Bong Hee,Park, Hyung Seo,Lee, Yun Lyul,Lee, Eun Hee,Choi,Soo Young,Park, Hyoung Jin The Korea Science and Technology Center 1998 BMB Reports Vol.31 No.3
An inositol monophosphatase (IMPase) was purified to homogeneity from rat duodenal mucosa for the first time and its enzymatic properties were investigated. Rat duodenal mucosa peculiarly exhibited the highest IMPase activity among various rat tissues examined. By means of ammonium sulfate precipitation, followed by Q-Sepharose, polylysine agarose, reactive-red agarose column chromatography, Uno-Q FPLC, and Bio-Silect FPLC, duodenal IMPase was purified 223-fold to a specific activity of 13.6U/mg protein. The molecular mass of the native enzyme was estimated to be 48,000 Da on gel filtration. The subunit molecular mass was determined by SDS-PAGE to be 24,000 Da. These results indicate that duodenal IMPase is a dimeric protein made up of identical subunits. Rat duodenal IMPase has distinct properties from brain IMPase. It has a broad spectrum of substrate specificity and is insensitive to Li+. Duodenal IMPase does not absolutely require Mg²+ for its catalytic activity. Furthermore, duodenal IMPase is less stable to heat than brain enzyme. It is suggested that the rat duodenal mucosa needs a large amount of IMPase whose properties are quite different from that of the brain enzyme.
Production and Characterization of Specific Antibodies to Bombesin
Kwon. Hyeok-Yil,Lee. Yun-Lyul,Park. Hyoung-Jin 대한생리학회 1994 대한생리학회지 Vol.28 No.1
In order to produce a specific bombesin antiserum far very sensitive radioimmunoassay, synthetic [lys<sup>3</sup>]-bombesin conjugated to bovine serum albumin was subcutaneously injected into guinea pigs. The conjugation was performed using either carbodiimide or gIutaraldehyde as a coupling agent. The antisera were characterized by analysis of Scatchard and Sips plots. The antiserum LBE 2G/2 raised by repeat injection of the immunogen conjugated with carbodiimide showed the titer of 1 : 188,000, very low cross-reactivity to bombesin-like peptides except bombesin, with high affinity constant (1.64 X 10<sup>11</sup> M<sup>-1</sup>) and high heterogeneity index (0.91). The antiserum LBG 1G/2 produced by repeat injection of the immunogen conjugated with glutaraldehyde possessed the titer of 1 : 43,000, high cross-reactivity to some bombesin-like peptides, high affinity constant (1.19 X 10<sup>11</sup> M<sup>-1</sup>) and high heterogeneity index (0.79). These results indicate that the antiserum LBE 2G/2 is specific only to bombesin and that the antiserum LBG IG/2 binds to some bombesin-like peptides such as alytesin, gastrin releasing peptide and neuromedin C. The antiserum LBE 2G/2 is sufficient for the very sensitive radioimmunoassay of bombesin.
Kwon, Hyeok-Yil,Lim, Bong-Hee,Park, Hyung-Seo,Lee, Yun-Lyul,Lee, Eun-Hee,Choi, Soo-Young,Park, Hyoung-Jin Korean Society for Biochemistry and Molecular Biol 1998 Journal of biochemistry and molecular biology Vol.31 No.3
An inositol monophosphatase (IMPase) was purified to homogeneity from rat duodenal mucosa for the first time and its enzymatic properties were investigated. Rat duodenal mucosa peculiarly exhibited the highest IMPase activity among various rat tissues examined. By means of ammonium sulfate precipitation, followed by Q-Sepharose, polylysine agarose, reactive-red agarose column chromatography, Uno-Q FPLC, and Bio-Silect FPLC, duodenal IMPase was purified 223-fold to a specific activity of 13.6 U/mg protein. The molecular mass of the native enzyme was estimated to be 48,000 Da on gel filtration. The subunit molecular mass was determined by SDS-PAGE to be 24,000 Da. These results indicate that duodenal IMPase is a dime ric protein made up of identical subunits. Rat duodenal IMPase has distinct properties from brain IMPase. It has a broad spectrum of substrate specificity and is insensitive to $Li^+$. Duodenal IMPase does not absolutely require $Mg^{2+}$ for its catalytic activity. Furthermore, duodenal IMPase is less stable to heat than brain enzyme. It is suggested that the rat duodenal mucosa needs a large amount of IMPase whose properties are quite different from that of the brain enzyme.
Hyeok Yil Kwon,Yun Beom Sim 한국실험동물학회 2006 Laboratory Animal Research Vol.22 No.2
Both acetylcholine and secretin are major physiological stimulators of pancreatic exocrine secretion in humans and animals. However, it has been shown that pre-exposure of carbamylcholine, a muscarinic agonist, markedly inhibits secretin-stimulated pancreatic secretion in rat pancreatic acinar cells. In this study, we have investigated the effects of carbamylcholine on the pancreatic secretin receptor to elucidate the cellular mechanism underlying carbamylcholine-induced desensitization of pancreatic exocrine secretion. Pre-treatment with carbamylcholine inhibited the specific binding of isotope-labeled secretin (<SUP>125</SUP>I-secretin) to its receptors on acinar cells in a dose-dependent manner, and this inhibitory effect was completely reversed by atropine. Using the Scatchard analysis for competitive binding data, the number of high affinity secretin receptors was found to be reduced 45% after pre-treatment of 1 mM carbamylcholine in culture media. However, the affinity of high affinity secretin receptors and the binding parameters of low affinity secretin receptors were not changed. Pre-treatment with protein kinase C inhibitor (chelerythrine) and guanylate cyclase inhibitor (LY83583) significantly inhibited the carbamylcholine effect on the binding of <SUP>125</SUP>I-secretin to its receptors; whereas calcium ionophore (A23187) and mitogen-activated protein kinase pathway inhibitor (PD98059) did not alter this inhibitory effect of carbamylcholine. These findings suggested that carbamylcholine-induced down-regulation of the high affinity secretin receptor is mediated by initial interaction of carbamylcholine with a muscarinic receptor followed by post-receptor processes, which appear to be coupled to protein kinase C and intracellular cGMP production in rat pancreatic acinar cells.
Hyeok Yil Kwon,Hyung Seo Park,Moo Ho Won,Yun Lyul Lee,Hyoung Jin Park 대한생리학회-대한약리학회 1998 The Korean Journal of Physiology & Pharmacology Vol.2 No.5
<P> Previously, we have isolated authentic bombesin and another bombesin like peptide named bombesin like immunoreactivity (BLI)-K2 from the skin of Korean fire-bellied toad, <I>Bombina orientalis. </I>In the present study, we have newly purified three heterogeneous forms of BLI named BLI-K3, BLI-K4, and BLI-K5 from side fractions obtained in previous isolation of bombesin like peptide. The BLIs were separated into five peaks on a column of C<SUB>18 </SUB>preparative HPLC. Among them, three minor peaks containing BLI-K3, K4, and K5 were purified by means of sequential chromatography on the columns of SP cation exchange HPLC and C<SUB>18 </SUB>reverse phase HPLC. The purified BLI-K3 and K4 showed high binding affinity to an anti-bombesin serum (LBE 2G-2) with binding potency of 72 and 95%, respectively, relative to that of bombesin. However, they did not possess any distinctive biological activity of bombesin like peptide. On the contrary, the biological activity of BLI-K5 was similar to that of bombesin but its binding affinity to an anti-bombesin serum was low. The results indicate that three heterogeneous forms of BLI were coexpressed with bombesin and BLI-K2 in the skin of <I>B. orientalis. </I>All forms of the purified BLI in the present study were immunologically active but only BLI-K5 possessed the distinctive biological activity of bombesin like peptide.
Effects of lipopolysaccharide and CpG-DNA on burn-induced skin injury
( Byoung Kwon Park ),( Dong Bum Kim ),( Sun Hee Cho ),( Jae Nam Seo ),( Jae Bong Park ),( Yong Sun Kim ),( Ihn Geun Choi ),( Hyeok Yil Kwon ),( Young Hee Lee ),( Hyung Joo Kwon ) 생화학분자생물학회(구 한국생화학분자생물학회) 2011 BMB Reports Vol.44 No.4
Destruction of the skin barrier by thermal injury induces microbial invasion, which can lead to the development of systemic infection and septic shock. Microbial pathogens possess pathogen-associated molecular patterns (PAMPs), which are recognized by conserved receptors. To understand the role of PAMPs in thermal injury-induced mice, LPS or CpG-DNA were topically applied to dorsal skin after thermal injury. We observed an increase in the number of inflammatory cell infiltrates as well as thickening in the dermis upon treatment with LPS or CpG-DNA. We also found that expression of IL-1β, MIP-2, and RANTES induced by thermal injury was enhanced by LPS or CpG-DNA. In addition, the proportions of CD4+ and CD8+ T cells in the spleen and lymph nodes were altered by LPS or CpG-DNA. These results provide important information concerning PAMPs-induced inflammation upon thermal injury and provide a basis for studying the role of PAMPs in thermal injury-induced complications. [BMB reports 2011; 44(4): 273-278]
한국산 무당개구리 피부에 존재하는 Bombesin 유사면역 반응물질의 순수정제 및 생물학적 활성
권혁일(Kwon, Hyeok-Yil),김일(Kim, Yil),박형진(Park, Hyoung-Jin) 대한생리학회 1990 대한생리학회지 Vol.24 No.2
The present investigation was performed to purify bombesin-like immunoreactivity (BBS-LI) from the skin of frogs, B. orientalis inhabiting Korea. For extraction of BBS-LI, the fresh skin of 360 g from frogs was immersed in 1,800 ml of 100% methanol and then kept at 4℃ for 5 days. BBS-LI was partially purified by liquid chromatography using an alkaline alumina column followed by a Sephadex G-10 column. BBS-LI was further purified by using sequential HPLC of reversed phase C18 preparation, gel permeation, SP-ion exchange and reversed phase C18 analysis. BBS-LI in fractions of each step was monitored by radioimmunoassay for which bombesin antiserum with a titer of 1 : 188,800 was raised in a guinea pig. Eventually, two different BBS-LI were successfully purified and each BBS-LI showed the following character. 1) BBS-LI was well separated into two peaks in SP-ion exchange HPLC. One (BBS-LI-K1) bound to the column while the other (BBS-LI-K2) did not. 2) BBS-LI-K1, 73.8% of total BBS-LI, was not differentiated from synthetic bombesin in reversed phase C18 analytical and gel permeation HPLC. 3) BBS-LI-K2, 26.2% of total BBS-LI, eluted later than synthetic bombesin in reversed phase C18 analytical HPLC, but it eluted with a retention time identical to that of synthetic bombesin in gel permeation HPLC. 4) The two forms of BBS-LI and synthetic bombesin identically stimulated gastrin release and pancreatic exocrine secretion including volume, protein output and amylase output in anesthetized rats. It is concluded from the above results that the skin of B. orientalis contains two different forms of BBS-LI which are very identical to bombesin immunologically and biologically. In comparison with synthetic bombesin containing 14 amino acid residues, the major form shows quite similar pattern in all HPLC used in the present study, but the minor form exhibits quite different pattern in SP-ion exchange and reversed phase C18 analytical HPLG.