• Journal of Nutrition and Health
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• 제24권3호
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• pp.149-156
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• 1991

고지방식이와 총열량섭취 제한식이가 protein kinase C 활성에 미치는 영향을 규명하고자 기타 양양소 또 총열량섭취가 정확이 조절된 식이를 제조하여 투여해본 결과, protein kinase C의 활성은 본 실험에서 사용한 옥수수유의 양의 증가에 따라 cytosolic과 membrane-associated protein kinase C의 활성을 모두 증가시키는 것을 관찰 하였다. 또한 기타 영양소는 같게 투여하고 열량소만 40% 감소시킨 실험군은 대조군에 비해 양쪽의 protein kinase C가 모두 감소하는 경향을 보였다.

• Genomics & Informatics
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• 제6권1호
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• pp.44-49
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• 2008

Protein kinase C (PKC) is a family of kinases involved in the transduction of cellular signals that promote lipid hydrolysis. PKC plays a pivotal role in mediating cellular responses to extracellular stimuli involved in proliferation, differentiation and apoptosis. Comparative analysis of the PKC-${\alpha},{\beta},{\varepsilon}$ isozymes of 200 recently sequenced microbial genomes was carried out using variety of bioinformatics tools. Diversity and evolution of PKC was determined by sequence alignment. The ser/thr protein kinases of Streptomyces coelicolor A3 (2), is the only bacteria to show sequence alignment score greater than 30% with all the three PKC isotypes in the sequence alignment. S.coelicolor is the subject of our interest because it is notable for the production of pharmaceutically useful compounds including anti-tumor agents, immunosupressants and over two-thirds of all natural antibiotics currently available. The comparative analysis of three human isotypes of PKC and Serine/threonine protein kinase of S.coelicolor was carried out and possible mechanism of action of PKC was derived. Our analysis indicates that Serine/ threonine protein kinase from S. coelicolor can be a good candidate for potent anti-tumor agent. The presence of three representative isotypes of the PKC super family in this organism helps us to understand the mechanism of PKC from evolutionary perspective.

• 대한수의학회지
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• 제38권1호
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• pp.9-15
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• 1998

To investigate the involvement of protein kinase C(PKC) isoenzyme in the testes which control spermatogenesis and hormone secretion, we examined cellular distribution of four types of PKC $\alpha$, ${\beta}I$, ${\delta}$ and ${\theta}$ in the horse testes using PKC antisera by western blot analysis and immunohistochemistry. By the western blot analysis, PKC $\alpha$ and ${\beta}I$ were detected at 82KD, while PKC ${\delta}$ and ${\theta}$ were detected at 80KD in the testes of both juvenile and adult horses. In juvenile horse, PKC $\alpha$, ${\delta}$ and ${\theta}$ except ${\beta}I$ were not detected in the cells of the testes, whereas PKC ${\beta}I$ was immunoreacted with only in spermatocytes. In adult, PKC $\alpha$, ${\beta}I$, ${\delta}$ and ${\theta}$isoenzymes were localized in interstitial cells of the testes. In the seminiferous tubules, PKC ${\beta}I$ is localized in spermatocyte, spermatid and spermatozoa, while PKC ${\delta}$ is localized only in spermatids. We suggest that this is a first report to localize PKC in the testes of horse and PKC isoenzymes are upregulated in the cells of horse testes depending on ages. These findings also suggest that certain PKC isoenzyme plays an important role in the signal transduction of spermatogenic cells and interstitial cells in horse testes.

• 한국동물학회지
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• 제35권2호
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• pp.161-172
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• 1992

In the short-term treahent of 12-0-tetradecanoylphorbol-13-acetate (TPA) or platelet-derived growth factor (PDGF), the'Wh and PDGF induced the Protein Kinase C (PKC) activation and migration from the cytoplasm to the peripheral nulcear membrane. And the activated PKC which was directly or indirectly stimulated by TPA or PDGF Phosphorylated many kinds of PKC's targeting proteins and induces various biological responses. Especially, the cytoplasmic PKC was phosphorylated within 1 hr and 10 min by TPA-and PDGF-treahent respectivelv. In the long-term treatment of TPA or PDGF, both of them induced the down-regulation and translocation of PKC in the mvoblasts. The down-regulation of PKC isozyrnes, the pattern of PKC I and ll was similar to the PKC 111 isozpnes in the cytoplasm. But in the nucleolus, the TPA did not induce and down-regulation or the inhibition of the immunoreactivity of PKC III antibody. This investigation indicates that each isozvmes of PKC mal be performed the different effects to the down-regulation of the cytoplasm or nucleolus. And douvn-regulated myoblasts contained low immunoreactivity of PKC antibodies.

• The Journal of Korean Physical Therapy
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• 제20권3호
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• pp.61-68
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• 2008

Purpose: Protein kinase C (PKC) is a member of a family of serine/threonine kinases that are activated by diacylglycerol (DG) and PKC stimulants. PKC play a key role in signal transduction, including muscle contraction, cell migration, apoptosis, cell proliferation and differentiation. However, the mechanism relating mitogen-activated protein kinases (MAPKs) and PKC, especially in the volume-dependent hypertensive state, remains unclear. Methods: In the present study, I investigated the relationship between PKC and MAPKs for isometric contraction, PKC translocation, and enzymatic activity from normotensive sham-operated rats (NSR) and aldosterone-analogue deoxycorticosterone acetate (DOCA) hypertensive rats (ADHR). Results: Systolic blood pressure was significantly increased in ADHR than in NSR. Physiological salt solution (PSS)-induced resting tension and the intracellular $Ca^{2+}$ concentration ([$Ca^{2+}{_i}$]) were different in the ADHR and NSR. The expression of PKC$\alpha$, PKC$\beta$II, PKC$\delta$, PKC$\varepsilon$ and PKC$\xi$ were different between the cytoplasmic and membranous fractions. However, expression of the PKC isoforms did not differ for the ADHR and NSR. The use of 12-deoxyphorbol 13-isobutyrate (DPB, a PKC stimulant) induced isometric contraction in $Ca^{2+}$-free medium, which was diminished in muscle strips from ADHR as compared to NSR. Increased vasoconstriction and phosphorylation induced by the use of 1 ${\mu}$M DPB were inhibited by treatment with 10 ${\mu}$M PD098059 and 10 ${\mu}$M SB203580, inhibitors of extracellular-regulated protein kinase 1/2 (ERK1/2) and p38 MAPK from ADHR, respectively. Conclusion: These results suggest that the development of aldosterone analogue-induced hypertension is associated with an altered blood pressure, resting tension, [$Ca^{2+}{_i}$], and that the $Ca^{2+}$-independent contraction evoked by PKC stimulants is due to the activation of ERK1/2 and p38 MAPK in volume-dependent hypertension. Therefore, it is suggested that PKC activity affects volume-dependent hypertension and the need to develop cardiovascular disease-specialized physical therapy.

• 한국동물학회지
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• 제34권2호
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• pp.131-141
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• 1991

TPA나 PDGF를 처리로 인한 Protein Kinase C의 신호전달은 힌산화에 의해 일어난다. 그렇지만, PKC에 의해 인산화 되어지는 targeting protein은 TAP나 PDGF 처리시에는 분자량이 서로 다른 단백질들이 인산화가 되어졌다. TPA처리한 myoblast에서 분자량 20,000의 단백질이 인산화되었다. PDGF처리한 세포에서는 분자량 40,000의 단백질이 인산화된 반면에 TPA처리로 인산화 되었던 분자량 20,000의 단백질은 탈인산화 되었다. 이러한 결과들은 TPA와 PDGF가 신호전달계의 활성에 있어서 다를 뿐만 아니라 그들은 장시간의 처리동안 PKC의 down regulation에 관계되어 짐을 암시한다. 그러나 PDGF는 TPA의 경우에서 보다 빠른 down regulation을 유도하였다. 면역세포 화학적인 연구에서 PKC의 동위효소인 PKC II는 세포질에, PKC III는 세포질과 인에 각각 분포하고 있었다. Myoblast에 있어서 PCK두가지 형태의 동위효소의 발현은 이들 동위효소들이 signal transduction이나 down regulation의 각기 다른 경로에 개입되어 진다는 것을 암시한다.

• Bulletin of the Korean Chemical Society
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• 제30권9호
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• pp.1981-1984
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• 2009

Subcellular localization of protein kinase often plays an important role in determining its activity and specificity. Protein kinase C (PKC), a family of multi-gene protein kinases has long been known to be translocated to the particular cellular compartments in response to DAG or its analog phorbol esters. We used C-terminal green fluorescent protein (GFP) fusion proteins of PKC isoforms to visualize the subcellular distribution of individual PKC isoforms. Intracellular localization of PKC-GFP proteins was monitored by fluorescence microscopy after transient transfection of PKC-GFP expression vectors in the HeLa cells. In unstimulated HeLa cells, all PKC isoforms were found to be distributed throughout the cytoplasm with a few exceptions. PKC$\theta$ was mostly localized to the Golgi, and PKC$\gamma$, PKC$\delta$ and PKC$\eta$ showed cytoplasmic distribution with Golgi localization. DAG analog TPA induced translocation of PKC-GFP to the plasma membrane. PKC$\alpha$, PKC$\eta$ and PKC$\theta$ were also localized to the Golgi in response to TPA. Only PKC$\delta$ was found to be associated with the nuclear membrane after transient TPA treatment. These results suggest that specific PKC isoforms are translocated to different intracellular sites and exhibit distinct biological effects.

• Archives of Plastic Surgery
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• 제34권1호
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• pp.13-17
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• 2007

Purpose: To understand the pathogenesis of the disease that presents abnormally proliferated vascular endothelial cells, a model of DMH(1,2-dimethylhydrazine)-induced abnormal proliferation of HUVECs(Human Umbilical Vein Endothelial Cells) was made. We indirectly determined that Protein Kinase C(PKC) restricts the cellular proliferation and inhibits the manifestation of growth factor by using several inhibiting substances of the transmitter through our previous studies. Thereupon, we attempted to observe direct enzymatic activities of PKC and its correlation with the abnormal proliferation of vascular endothelial cells. Methods: $10^5$ HUVECs cells were applied to 6 individual well plates in three different groups; A control group cultured without treatment, a group concentrated with $0.75{\times}10^{-8}M$ DMH only, and a group treated with DMH & $5{\times}10^{-9}M$ Calphostin C, inhibitor of PKC. In analyzing the formation of intracellular PKC enzyme, protein separation was performed, and separated protein was quantitatively measured. PKC enzyme reaction was analyzed through Protein Kinase C Assay System (Promega, USA), and the results were analyzed according to Beer's law. Results: Enzymatic activity of PKC presented the highest in all reaction time of a group concentrated only with DMH, and the lowest in the control group. The group treated with DMH and the inhibitor revealed statistically lower enzymatic activity than group only with DMH in all reaction time, although higher than the control group. Conclusion: From the enzymatic aspect, most active and immediate reaction of the PKC was observed in the group concentrated with DMH only. The group treated with DMH & PKC inhibitor showed meaningful decrease. Accordingly, PKC holds a significant role in DMH-induced abnormal proliferation of vascular endothelial cells.

• BMB Reports
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• 제44권9호
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• pp.559-565
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• 2011

Protein kinase C (PKC) is a central enzyme that modulates numerous biological functions. For this reason, specific PKC inhibitors/activators are required to study PKC-related signaling mechanisms. To date, although many PKC inhibitors have been developed, they are limited by poor selectivity and nonspecificity. In this review, we focus on the nonspecific actions of PKC inhibitors on cardiovascular ion channels in addition to their PKC-inhibiting functions. The aim of this paper is to urge caution when using PKC inhibitors to block PKC function. This information may help to better understand PKC-related physiological/biochemical studies.

• 생명과학회지
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• 제20권10호
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• pp.1451-1457
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• 2010

Serotonin (5-hydroxytryptamine (5-HT))는 신경계의 세포-세포 간의 신호전달의 주요한 신경전달물질이다. 세포막에 존재하는 serotonin transporter (SERT)는 연접간격에 존재하는 5-HT를 세포 내로 재흡수 하여 세포외부의 5-HT 농도를 조절하지만 그 기전은 아직 밝혀지지 않았다. 본 연구에서는 yeast two-hybrid system을 사용하여 SERT의 C-말단이 protein kinase C-$\varepsilon$ (PKC-$\varepsilon$)과 특이적으로 결합함을 알았다. PKC-$\varepsilon$는 PKC의 isotype으로 calcium 비의존적이며 phorbol ester/diacylglycerol 민감성 serine/threonine kinase이다. $Na^+/Cl^-$ 의존성 SLC6 gene family의 다른 수송체는 PKC-$\varepsilon$과 결합하지 않았다. Deletion mutant들을 사용하여 SERT는 PKC-$\varepsilon$의 C-말단부위와 결합함을 알았으며, 또한 이 단백질간의 결합을 GST pull-down assay로 확인하였다. PKC-$\varepsilon$는 in vitro에서 SERT의 N-말단의 펩티드를 인산화시켰다. 이러한 결과들은 PKC-$\varepsilon$에 의한 SERT의 인산화가 세포막에 존재하는 SERT의 활성을 조절하는 역할을 할 가능성을 시사한다.