• Title/Summary/Keyword: protein kinase C

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Protein Kinase Modulates the $GABA_c$ Currents in Cone-horizontal Cell Axon-terminals Isolated from Catfish Retina

  • Paik, Sun-Sook;Lee, Sung-Jong;Jung, Chang-Sub;Bai, Sun-Ho
    • Proceedings of the Korean Biophysical Society Conference
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    • 1999.06a
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    • pp.54-54
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    • 1999
  • Protein kinase modulation of gamma-aminobutyric acid C (GABA$_{c}$) currents in freshly dissociated catfish retinal cone-horizontal cell axon-terminals was studied under voltage clamp with the use of the whole cell patch-clamp technique. Responses to pulses of GABA were monitored in intracellular application of adenosin 3',5'-cycle monophophate (cAMP)-dependent protein kinase (PKA) and protein kinase C (PKC) activators, and their inhibitors or inactive analogues.(omitted)d)

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Brazilin Inhibits Activities of Protein Kinase C and Insulin Receptor Serine Kinase in Rat Liver

  • Kim, Seong-Gon;Kim, You-Me;Khil, Lee-Yong;Jeon, Sun-Duck;So, Dhong-Su;Moon, Chang-Hyun;Moon, Chang-Kiu
    • Archives of Pharmacal Research
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    • v.21 no.2
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    • pp.140-146
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    • 1998
  • Hypoglycemic action of brazilin was found to be based on the improvement of peripheral glucose utility, and this action might be correlated with the insulin action pathway. In the present study we investigated the effect of brazilin on the insulin receptor autophosphorylation, protein kinase C (PKC), protein phosphatase and insulin receptor serine kinase in order to confirm whether the hypoglycemic mechanism is concerned with insulin action pathway. Brazilin was found to inhibit PKC and insulin receptor serine kinase, which are involved in the regulation of insulin signal pathway. But any significant effect was not shown on insulin receptor tyrosine kinase activity, autophosphorylation and phosphatase activity. These findings suggest that brazilin might enhance insulin receptor function by decreasing serine phosphorylation, which might mediate hypoglycemic effect of brazilin.

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Effects of Staurosporine and Genistein on Superoxide and HOCl Production in C5a- or PMA-activated Neutrophils (Staurosporine과 Genistein이 C5a 또는 PMA에 의하여 활성화된 호중구에서의 Superoxide와 HOCl 생성에 나타내는 영향)

  • Yun Young-Chul;Kang Hee-Jeong;Shin Yong-Kyoo;Lee Chung-Soo
    • The Korean Journal of Pharmacology
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    • v.31 no.1 s.57
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    • pp.115-122
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    • 1995
  • Effects of staurosporine, genistein and pertussis toxin on superoxide and HOCl production in C5a- or PMA-activated neutrophils were investigated. A C5a-induced superoxide and $H_2O_2$ production was inhibited by staurosporine, genistein and pertussis toxin. The stimulatory effect of PMA was inhibited by staurosporine but was not affected by pertussis toxin, whereas it was further promoted by genistein. Staurosporine and genistein inhibited superoxide production by sodium fluoride, but pertussis toxin did not affect it. PMA-induced $H_2O_2$ production was inhibited by staurosporine but was not affected by pertussis toxin. Genistein did not show a stimulatory effect on PMA-induced $H_2O_2$ production. Staurosporine and pertussis toxin inhibited HOCl production by C5a- or PMA, whereas genistein stimulated it. C5a-or PMA-induced myeloperoxidase release was inhibited by genistein, in this response the effect of pertussis toxin was not detected. Staurosporine did not affect the stimulatory effect of PMA on the release. Myeloperoxidase activity was markedly increased by genistein but was not affected by staurosporine and pertussis toxin. These results indicate that the respiratory burst of neutrophils may be regulated by protein kinase C and protein tyrosine kinase. Superoxide production induced by the direct activation of protein kinase C might be affected by protein tyrosine kinase oppositely. Genistein probably pro-motes HOCl production by activating myeloperoxidase.

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Potential Role of Protein Kinase C on the Differentiation of Erythroid Progenitor Cells

  • Lee, Sang-Jun;Cho, In-Koo;Huh, In-Hoe;Yoon, Ki-Yom;Ann, Hyung-Soo
    • Archives of Pharmacal Research
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    • v.18 no.2
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    • pp.90-99
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    • 1995
  • The effect of protein kinase C inhibitors, sturosporine and 1-(5-isoquinolinyl sulfonyl)-2-methyl piperazine(H7) on in vitro differentiation of erythroid progenitor cells which were isolated from spleens of mice infected with the anemia-inducing strain of Friend virus were examined. Erythropoietin-mediated differentitation of erythroid progenitor cells, as determined by the incorporation of $^{59}Fe$ into protoporphyrin, was inhibited by staurosporine and H7 in a concentration -dependent manner. Scatchard analysis of the $^3H-phorbol-12$, 13-dibutyrate binding to erythroid progenitor cells revealed that at the high affinity sites the dissociation constant was 22nM and the maximum number of $^3H-phorbol-12$, 13-dibutyrate binding to erythroid progenitor cells revealed that at the high affinity sites the dissociation constant was 22nM and the maximum number of $^3H-phorbol-12$, 13-dibutyrate binding sites per cell was approximately $3.7\times10^5$. Cytosonic protein kinase C was isolated from erthroid progenitor cells and then purified by sequential column chromatogrphy. Two isoforms of protein kinase C were found. Photoaffinity labeling of the purified protein kinase C samples with $^3H-phorbol-12$12-myristate 13-acetate followed by analysis of SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and autofluorography showed radiolabeled 82-KDa pepticles. Rediolabeling of the 82-KDa peptides with $^3H-phorbol-12$myristate 13-acete was almost completely blocked by excess unlabeled phorbol 12-myristate 13-acetate was almost 12-muristate 13-acetate-promoted phosphorylation with the puyrified protein kinase C samples showed that the phosphorylation of 82-KDa peptides was increased as the concentration of phorbol 12-myristate 13-acetate was increased from $10^{-8}M{\;}to{\;}10^{-4}$M. In light of the findings that erythroid progenitor cells possessed an abundance of protein kinase C and that stauroporine and H7 inhibited erythroid differentiation, it seemed likely that protein kinase C would play a role in the erythroid progenitor cell development.

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Nucleotide and Deduced Amino Acid Sequences of Rat Myosin Binding Protein H (MyBP-H)

  • Jung, Jae-Hoon;Oh, Ji-Hyun;Lee, Kyung-Lim
    • Archives of Pharmacal Research
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    • v.21 no.6
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    • pp.712-717
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    • 1998
  • The complete nucleotide sequence of the cDNA clone encoding rat skeletal muscle myosin- binding protein H (MyBP-H) was determined and amino acid sequence was deduced from the nucleotide sequence (GenBank accession number AF077338). The full-length cDNA of 1782 base pairs(bp) contains a single open reading frame of 1454 bp encoding a rat MyBP-H protein of the predicted molecular mass 52.7kDa and includes the common consensus 1CA__TG' protein binding motif. The cDNA sequence of rat MyBP-H show 92%, 84% and 41% homology with those of mouse, human and chicken, respectively. The protein contains tandem internal motifs array (-FN III-Ig C2-FN III- Ig C2-) in the C-terminal region which resembles to the immunoglobulin superfamily C2 and fibronectin type III motifs. The amino acid sequence of the C-terminal Ig C2 was highly conserved among MyBPs family and other thick filament binding proteins, suggesting that the C-terminal Ig C2 might play an important role in its function. All proteins belonging to MyBP-H member contains `RKPS` sequence which is assumed to be cAMP- and cGMP-dependent protein kinase A phosphorylation site. Computer analysis of the primary sequence of rat MyBP-H predicted 11 protein kinase C (PKC)phosphorylation site, 7 casein kinase II (CK2) phosphorylation site and 4N-myristoylation site.

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Sequence Analysis and Potential Action of Eukaryotic Type Protein Kinase from Streptomyces coelicolor A3(2)

  • Roy, Daisy R.;Chandra, Sathees B.C.
    • Genomics & Informatics
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    • v.6 no.1
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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.

Inhibitory Activity against Protein Kinase C of Some Medicinal Plants (수종 생약의 Protein kinase C 저해활성)

  • Lee, Hyun-Sun;Ahn, Soon-Cheol;Kim, Bo-Hyun;Park, Moon-Su;Oh, Won-Keun;Yoon, Byung-Dae;Ahn, Jong-Seog;Mheen, Tae-Ick
    • Korean Journal of Pharmacognosy
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    • v.23 no.3
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    • pp.142-145
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    • 1992
  • MeOH extract of twenty medicinal herbs were screened for their effects against protein kinase C (PKC) using bleb-forming assay and PKC enzyme assay. Smilax china and Sanguisorba officinalis showed potent anti-PKC activity. Campsis grandiflora and Galla Halepensis showed moderate inhibitory effect on PKC.

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Molecular Mechanisms of Neutrophil Activation in Acute Lung Injury (급성 폐손상에서 호중구 활성화의 분자학적 기전)

  • Yum, Ho-Kee
    • Tuberculosis and Respiratory Diseases
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    • v.53 no.6
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    • pp.595-611
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    • 2002
  • Akt/PKB protein kinase B, ALI acute lung injury, ARDS acute respiratory distress syndrome, CREB C-AMP response element binding protein, ERK extracelluar signal-related kinase, fMLP fMet-Leu-Phe, G-CSF granulocyte colony-stimulating factor, IL interleukin, ILK integrin-linked kinase, JNK Jun N-terminal kinase, LPS lipopolysaccharide, MAP mitogen-activated protein, MEK MAP/ERK kinase, MIP-2 macrophage inflammatory protein-2, MMP matrix metalloproteinase, MPO myeloperoxidase, NADPH nicotinamide adenine dinucleotide phosphate, NE neutrophil elastase, NF-kB nuclear factor-kappa B, NOS nitric oxide synthase, p38 MAPK p38 mitogen activated protein kinase, PAF platelet activating factor, PAKs P21-activated kinases, PMN polymorphonuclear leukocytes, PI3-K phosphatidylinositol 3-kinase, PyK proline-rich tyrosine kinase, ROS reactive oxygen species, TNF-${\alpha}$ tumor necrosis factor-a.

Induction of Maturation Promoting Factor in Runo Oocvtes by Protein Kinase C Activation in uitro. (개구리 난자에서 Protein Kinase C의 활성화에 의한 Maturation Promoting Factor의 생성유도)

  • 유영란;임욱빈
    • The Korean Journal of Zoology
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    • v.35 no.3
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    • pp.277-286
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    • 1992
  • 개구리의 난자로 부터 maturation promoting factor(MPF)를 추출, 부분 분리하여 이들의 활성을 조사하고 이 물질의 생성과 protein kinase C(반KC)와의 관계를 조사하SB다. 성숙된 난자를 분쇄한 후 초원심분리과정을 거쳐 MPF의 crude extract(CE)를 얻은 다음 ultrafiltration (UF)과 고속액체크로마토그라피를 거쳐서 3종류의 분획 (peak 1, 11, and 111)을 얻었다. 이들 분획을 in nitro assay와 autoradiDgraphy를 사용하여 확인한 결과 분획 11에서 MPF 활성이 있는 것을 알았다. 분리 단계에 따라 MPF의 정제도를 Hl histone kinase assay로 조사한 결깍 UF를 거친 것은 CE보다 약 3배로, 분획 11에서는 약 117배로 증가한 것을 확인하였다. 또한 MPF분획의 인산화를 autoradiography로 조사한 결과 45 KD 단백질을 포함한 수종의 난자 단백질이 강하게 인산화되었음을 알 수 있었다. PKC의 활성화가 난자내 MPF의 생성을 유도하는가를 보기 위하여 PKC의 활성제인 12-0-tetradecanoyl phorbol 13 acetate(TPA)를 처리한 난자의 세포질 추출물을 미세주입 법으로 조사한 결과 TPA 처리 후 6시간부터 난자내 MPF의 활성이 나타나는 것을 알 수 있었다. 이러한 결과들은 PKC의 활성화가 MPF의 생성을 유도하고, MPF의 활성화와 함께 일부 단백질들의 인산화를 통하여 궁극적으로 난자 성숙을 촉진했음을 시사한다.

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