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Pak, Yunbae,Nam, Imsook,Hong, Yonggeun,Hwang, Inhwan,Cho, Moo Je The Korea Science and Technology Center 1999 BMB Reports Vol.32 No.1
To understand the function of phospholipids and their fatty acid composition on the morphological changes in the amp 1-4 mutant of Arabidopsis, the mutant was compared to the wild-type Arabidopsis by TLC, HPTLC, phosphorous assay, HPLC, and GC. In the mutant, phosphatidylethanolamine (PE) was increased 5-fold and phosphatidylglycerol (PG) was decreased 1.2-fold (nmol phosphorous/g tissue). Inositol phospholipids showed a generally increased trend ranging from 1.4-to 3.0-fold (nmol inositol/g tissue). When fatty acid composition of the mutant was compared to the wild-type, linoleic (18:2) and linolenic (18:3) acids of phosphatidylcholine (PC) and PG were decreased but palmitoleic acid (16:1) and oleic acid (18:1) PC was increased 2.5-and 2.1-fold (mol%), respectively. In galactolipids, myristic acid (14:0) of monogalactosyl-diacyglycerol (MGDG) were increased 5.8-fold (mol%). Among the inositol phospholipids, yso-phosphatidylinositol (L-PI) and phosphatidylinositol 4,5-bisphosphate (PIP₂)showed 4-and 1.9-fold (mol%) increase of 16:1, respectively. These results suggest that the increase of PE, the decrease of PG, the increase of inositol phospholipids, and the altered fatty acid composition are related to the phenotypic changes affecting the morphological features, and might cause different physiological changes in the amp 1-4 mutant compared to wild-type Arabidopsis.
홍용근,박윤배,Hong Yonggeun,Pak Yunbae 한국생명과학회 2005 생명과학회지 Vol.15 No.2
본 연구는 혈당강하효과를 갖는 chiro-inositol을 다량 함유하고 있는 식품이나 식용물질을 탐색하여 선발하고, 선택된 식품이나 식용물질에서 chiro-inositol을 분리$ {\cdot}$정제하여 정제된 chiro-inositol로 동물실험을 실시하여 혈당강하효과를 증명하였다. 약 300여종의 식품 및 식용물질을 HPLC로 분석한 결과 식품으로 안전한 대두 부산물인 탈지대두와 두부 순물에서 chiro-inositol의 함량이 각각 6.75 mg/g, 20mg/kg로 조사되어 선택되었고, chiro-inositol의 순도가 $90\%$ 이상(w/w)인 chiro-inositol의 추출물을 이용하여 동물실험을 통한 혈당강하효과를 조사하였다. 그 결과, STZ로 유발된 고혈당 쥐에 경구 투여시, 약 $40\%$의 강한 혈당강하 효과를 나타내었으며 지속시간은 약 12시간이었고, 인슐린과 복합처리 했을 때 상승작용(synergy)을 나타내었으며, 저혈당증으로 전혀 발전되지 않았다. Studies with diabetic mammalian systems showed that chiro-inositol administration decreased blood glucose levels. We investigated which foodstuffs contain large amounts of chiro-inositol by surveying vegetables, edible plants and other staples in an effort to explore the nutritional or therapeutic supplements of chiro-inositol for diabetic patients. In the course of our investigation, we found that soybean and soybean derivatives have high chiro-inositol levels (upto 20 mg/g). The purified chiro-inositol from the soybean was then tested for reducing hyperglycemia by administrating the chiro-inositol in streptozotocin-treated diabetic rats. The results showed that the intragastric administration of 50 mg chiro-inositol/kg BW lowered hyperglycemia by $40\%$ and that the effect was sustained for approximately 12 hr.
Reynolds IV, Thomas H.,Pak, Yunbae,Harris, Thurl E.,Manchester, Jill,Barrett, Eugene J.,Lawrence Jr., John C. American Society for Biochemistry and Molecular Bi 2005 The Journal of biological chemistry Vol.280 No.7
<P>UDP-glucose (UDP-Glc) and glycogen levels in skeletal muscle fibers of defined fiber type were measured using microanalytical methods. Infusing rats with insulin increased glycogen in both Type I and Type II fibers. Insulin was without effect on UDP-Glc in Type I fibers but decreased UDP-Glc by 35-40% in Type IIA/D and Type IIB fibers. The reduction in UDP-Glc suggested that UDP-Glc pyrophosphorylase (PPL) activity might limit glycogen synthesis in response to insulin. To explore this possibility, we generated mice overexpressing a UDP-Glc PPL transgene in skeletal muscle. The transgene increased both UDP-Glc PPL activity and levels of UDP-Glc in skeletal muscles by approximately 3-fold. However, overexpression of UDP-Glc PPL was without effect on either the levels of skeletal muscle glycogen or glucose tolerance in vivo. The transgene was also without effect on either control or insulin-stimulated rates of (14)C-glucose incorporation into glycogen in muscles incubated in vitro. The results indicate that UDP-Glc PPL activity is not limiting for glycogen synthesis.</P>
정규호,Hayeong Kwon,Chanhee Min,Yunbae Pak 생화학분자생물학회 2009 Experimental and molecular medicine Vol.41 No.4
We investigated the effect of phenylephrine (PE)- and isoproterenol (ISO)-induced cardiac hypertrophy on subcellular localization and expression of caveolin-3 and STAT3 in H9c2 cardiomyoblast cells. Caveolin-3 localization to plasma membrane was attenuated and localization of caveolin-3 to caveolae in the plasma membrane was 24.3% reduced by the catecholamineinduced hypertrophy. STAT3 and phospho-STAT3 were up-regulated but verapamil and cyclosporin A synergistically decreased the STAT3 and phospho- STAT3 levels in PE- and ISO-induced hypertrophic cells. Both expression and activation of STAT3 were increased in the nucleus by the hypertrophy. Immunofluorescence analysis revealed that the catecholamineinduced hypertrophy promoted nuclear localization of pY705-STAT3. Of interest, phosphorylation of pS727- STAT3 in mitochondria was significantly reduced by catecholamine-induced hypertrophy. In addition, mitochondrial complexes II and III were greatly downregulated in the hypertrophic cells. Our data suggest that the alterations in nuclear and mitochondrial activation of STAT3 and caveolae localization of caveolin-3 are related to the development of the catecholamine- induced cardiac hypertrophy. We investigated the effect of phenylephrine (PE)- and isoproterenol (ISO)-induced cardiac hypertrophy on subcellular localization and expression of caveolin-3 and STAT3 in H9c2 cardiomyoblast cells. Caveolin-3 localization to plasma membrane was attenuated and localization of caveolin-3 to caveolae in the plasma membrane was 24.3% reduced by the catecholamineinduced hypertrophy. STAT3 and phospho-STAT3 were up-regulated but verapamil and cyclosporin A synergistically decreased the STAT3 and phospho- STAT3 levels in PE- and ISO-induced hypertrophic cells. Both expression and activation of STAT3 were increased in the nucleus by the hypertrophy. Immunofluorescence analysis revealed that the catecholamineinduced hypertrophy promoted nuclear localization of pY705-STAT3. Of interest, phosphorylation of pS727- STAT3 in mitochondria was significantly reduced by catecholamine-induced hypertrophy. In addition, mitochondrial complexes II and III were greatly downregulated in the hypertrophic cells. Our data suggest that the alterations in nuclear and mitochondrial activation of STAT3 and caveolae localization of caveolin-3 are related to the development of the catecholamine- induced cardiac hypertrophy.
Jang, Donghwan,Kwon, Hayeong,Jeong, Kyuho,Lee, Jaewoong,Pak, Yunbae The Company of Biologists Ltd. 2015 Journal of cell science Vol.128 No.11
<P>Here, we explored flotillin-1-mediated regulation of insulin-like growth factor-1 (IGF-1) signaling. Flotillin-1-deficient cells exhibited a reduction in the activation of IGF-1 receptor (IGF-1R), ERK1/2 and Akt pathways, and the transcriptional activation of Elk-1 and the proliferation in response to IGF-1 were reduced in these cells. We found that IGF-1-independent flotillin-1 palmitoylation at Cys34 in the endoplasmic reticulum (ER) was required for the ER exit and the plasma membrane localization of flotillin-1 and IGF-1R. IGF-1-dependent depalmitoylation and repalmitoylation of flotillin-1 sustained tyrosine kinase activation of the plasma-membrane-targeted IGF-1R. Dysfunction and blocking the turnover of flotillin-1 palmitoylation abrogated cancer cell proliferation after IGF-1R signaling activation. Our data show that flotillin-1 palmitoylation is a new mechanism by which the intracellular localization and activation of IGF-1R are controlled.</P>
Kwon, Hayeong,Jeong, Kyuho,Hwang, Eun Mi,Park, Jae-Yong,Pak, Yunbae Blackwell Publishing Ltd 2011 JOURNAL OF CELLULAR AND MOLECULAR MEDICINE Vol.15 No.4
<P><B>Abstract</B></P><P>Herein, we report that insulin-activated extracellular signal-regulated kinase (ERK) is translocated to the nuclear envelope by caveolin-2 (cav-2) and associates with lamin A/C in the inner nuclear membrane in response to insulin. We identified that the Ser<SUP>154</SUP>–Val<SUP>155</SUP>–Ser<SUP>156</SUP> domain on the C-terminal of cav-2 is essential for insulin-induced phosphorylation and nuclear targeting of ERK and cav-2. In human embryonic kidney 293T cells, ERK was not activated and translocated to the nucleus by insulin in comparison to insulin-like growth factor-1 (IGF-1). However, insulin-stimulated activation of ERK was induced by exogenous addition of cav-2. The activated ERK associated and translocated with the cav-2 to the nucleus. In turn, cav-2 promoted phospho-ERK interaction with lamin A/C in the inner nuclear membrane. In contrast, ERK, but not cav-2, was phosphorylated and translocated to the nucleus by IGF-1. The nuclear targeted phospho-ERK failed to localize in the nuclear envelope in response to IGF-1. Together, our data demonstrate that translocation of phospho-ERK to the nuclear envelope is mediated by Ser<SUP>154</SUP>–Val<SUP>155</SUP>–Ser<SUP>156</SUP> domain of cav-2 and this event is an insulin-specific action.</P>
Jeong, Kyuho,Kwon, Hayeong,Lee, Jaewoong,Jang, Donghwan,Pak, Yunbae Oxford University Press 2015 Nucleic acids research Vol.43 No.6
<P>Insulin controls transcription to sustain its physiologic effects for the organism to adapt to environmental changes added to genetic predisposition. Nevertheless, insulin-induced transcriptional regulation by epigenetic factors and in defined nuclear territory remains elusive. Here we show that inner nuclear membrane (INM)-integrated caveolin-2 (Cav-2) regulates insulin-response epigenetic activation of <I>Egr-1</I> and <I>JunB</I> genes at the nuclear periphery. INM-targeted pY19-Cav-2 in response to insulin associates specifically with the A-type lamin, disengages the repressed <I>Egr-1</I> and <I>JunB</I> promoters from lamin A/C through disassembly of H3K9me3, and facilitates assembly of H3K9ac, H3K18ac and H3K27ac by recruitment of GCN5 and p300 and the subsequent enrichment of RNA polymerase II (Pol II) on the promoters at the nuclear periphery. Our findings show that Cav-2 is an epigenetic regulator of histone H3 modifications, and provide novel mechanisms of insulin-response epigenetic activation at the nuclear periphery.</P>