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Pkc delta 2 c region

Richard Gordon, Neeraj Singh, Vivek Lawana, Anamitra Ghosh, Dilshan S Harischandra, Huajun Jin, Colleen Hogan, Souvarish Sarkar, Dharmin Rokad, Nikhil Panicker, Vellareddy Anantharam, Anumantha G Kanthasamy, Arthi Kanthasamy
Chronic microglial activation has been linked to the progressive degeneration of the nigrostriatal dopaminergic neurons evidenced in Parkinson's disease (PD) pathogenesis. The exact etiology of PD remains poorly understood. Although both oxidative stress and neuroinflammation are identified as co-contributors in PD pathogenesis, signaling mechanisms underlying neurodegenerative processes have yet to be defined. Indeed, we recently identified that protein kinase C delta (PKCδ) activation is critical for induction of dopaminergic neuronal loss in response to neurotoxic stressors...
September 2016: Neurobiology of Disease
Rehan Zafar Paracha, Amjad Ali, Jamil Ahmad, Riaz Hussain, Umar Niazi, Syed Aun Muhammad
A number of diseases including sepsis, rheumatoid arthritis, diabetes, cardiovascular diseases and hyperinflammatory immune disorders have been associated with Toll like receptor (TLR) 2 and TLR4. Endogenous adaptor protein known as MyD88 adapter-like protein (MAL) bind exclusively to the cytosolic portions of TLR2 and TLR4 to initiate downstream signalling. Brutons tyrosine kinase (BTK) and protein kinase C delta (PKCδ) have been implicated to phosphorylate MAL and activate it to initiate downstream signalling...
August 2014: Computational Biology and Chemistry
Rika Kuriwaka-Kido, Shinsuke Kido, Yuka Miyatani, Yuji Ito, Takeshi Kondo, Takashi Omatsu, Bingzi Dong, Itsuro Endo, Ken-Ichi Miyamoto, Toshio Matsumoto
Glucocorticoid (GC) excess causes a rapid loss of bone with a reduction in bone formation. Intermittent PTH (1-34) administration stimulates bone formation and counteracts the inhibition of bone formation by GC excess. We have previously demonstrated that mechanical strain enhances interleukin (IL)-11 gene transcription by a rapid induction of ΔFosB expression and protein kinase C (PKC)-δ-mediated phosphorylation of phosphorylated mothers against decapentaplegic (Smad)-1. Because IL-11 suppresses the expression of dickkopf-1 and -2 and stimulates Wnt signaling, IL-11 appears to mediate at least a part of the effect of mechanical strain on osteoblast differentiation and bone formation...
March 2013: Endocrinology
Huajun Jin, Arthi Kanthasamy, Vellareddy Anantharam, Ajay Rana, Anumantha G Kanthasamy
We previously demonstrated that protein kinase Cδ (PKCδ; PKC delta) is an oxidative stress-sensitive kinase that plays a causal role in apoptotic cell death in neuronal cells. Although PKCδ activation has been extensively studied, relatively little is known about the molecular mechanisms controlling PKCδ expression. To characterize the regulation of PKCδ expression, we cloned an ∼2-kbp 5'-promoter segment of the mouse Prkcd gene. Deletion analysis indicated that the noncoding exon 1 region contained multiple Sp sites, including four GC boxes and one CACCC box, which directed the highest levels of transcription in neuronal cells...
June 3, 2011: Journal of Biological Chemistry
Seung Eun Lee, Seong Il Jeong, Gun-Dong Kim, Hana Yang, Cheung-Seog Park, Young-Ho Jin, Yong Seek Park
Crotonaldehyde, a highly reactive α, β-unsaturated aldehyde, is a ubiquitous environmental pollutant and a product of endogenous lipid peroxidation. It is also a major component of cigarette smoke and is present in many foods and beverages, and has also been linked to development of various diseases. Activation of endothelial cells by stimuli such as cigarette smoke is an important risk factor for cardiovascular diseases, including atherosclerosis. Heme oxygenase-1 (HO-1) is a protective antioxidant enzyme with a critical role in resistance to oxidative stress and other cellular functions...
March 25, 2011: Toxicology Letters
Venkataraman Sriraman, Swati R Modi, Yvonne Bodenburg, Larry A Denner, Randall J Urban
PKC signaling is critical for follicular development and the induction of ovulatory genes including Pgr, Prkg2, and Cyp11a1 (SCC). We investigated PKC signaling mechanisms in the JC-410 porcine granulosa cell line stably expressing an SCC-luciferase reporter gene containing 2kb of the porcine SCC promoter. Addition of phorbol 12-myristate 13-acetate (PMA), which activates protein kinase C, induced the promoter approximately 6-fold over the basal levels in 4h. This effect was predominantly mediated by the PKC beta and delta isoforms...
November 6, 2008: Molecular and Cellular Endocrinology
Noriko Sakai, Hiromi Terami, Shinobu Suzuki, Megumi Haga, Ken Nomoto, Nobuko Tsuchida, Ken-ichirou Morohashi, Naoaki Saito, Maki Asada, Megumi Hashimoto, Daisuke Harada, Hiroshi Asahara, Tetsuya Ishikawa, Fumiki Shimada, Kazuhiro Sakurada
Nuclear receptor subfamily 5, group A, member 1 (NR5A1 previously known as SF-1/AD4BP) is a transcription factor involved in the development of adrenal/gonadal tissues and steroidogenic lineage cell differentiation in adult somatic stem cells. To understand the cellular signaling network that regulates NR5A1 gene expression, loss of function screening with an siRNA kinome library, and gain of function screening with an addressable full-length cDNA library representing one quarter of the human genome was carried out...
September 2008: Journal of Endocrinology
Zhiyong Zhao, Ying-King Wu, E Albert Reece
To address the role of PKC isoforms in hyperglycemia-induced apoptosis and malformations in the embryos of diabetic pregnancies, expression of PKCalpha, beta1, beta 2, gamma, delta, epsilon, and zeta was examined in the neural tube of rat embryos and showed to overlap with the regions of increased apoptosis. Levels of activated (phosphorylated) PKCalpha , beta2, and delta were increased in the embryos of diabetic dams whereas those of PKCepsilon and zeta were decreased when compared with those in control groups...
April 2008: Reproductive Sciences
Eun-Young Choi, SungGa Lee, Hyun-Mee Oh, Young-Dae Kim, Eun-Ju Choi, Sang-Hyun Kim, Sang-Wook Kim, Suck-Chei Choi, Chang-Duk Jun
We have shown that the bacterial iron chelator, deferoxamine (DFO), triggers inflammatory signals, including the production of CXC chemokine IL-8, in human intestinal epithelial cells (IECs) by activating ERK1/2 and p38 kinase pathways. In the present study, we show that PKCdelta, one of the novel protein kinase C (PKC) isoforms, involves in signal transduction pathways leading to DFO-induced IL-8 production. Pretreatment of human intestinal epithelial HT-29 cells with rottlerin showed remarkable inhibition of DFO-induced IL-8 production...
January 9, 2007: Life Sciences
Hsi-Lung Hsieh, Hui-Hsin Wang, Cheng-Ying Wu, Mei-Jie Jou, Mao-Hsiung Yen, Peter Parker, Chuen-Mao Yang
Bradykinin (BK) is an inflammatory mediator, elevated levels in the region of several brain injury and inflammatory diseases. It has been shown to induce cyclooxygenase-2 (COX-2) expression implicating in inflammatory responses in various cell types. However, the signaling mechanisms underlying BK-induced COX-2 expression in astrocytes remain unclear. First, RT-PCR and Western blotting analysis showed that BK induced the expression of COX-2 mRNA and protein, which was inhibited by B(2) BK receptor antagonist Hoe140, suggesting the involvement of B(2) BK receptors...
February 2007: Cellular Signalling
A M D'Costa, M F Denning
Keratinocyte apoptosis induced by UV radiation is a major protective mechanism from skin photocarcinogenesis. The induction of apoptosis by UV radiation, as well as a variety of genotoxic stimuli, involves the activation of PKC-delta by caspase-3-mediated cleavage in its hinge region, thus generating a constitutively active catalytic fragment. To determine the role of PKC-delta cleavage in UV apoptosis signaling, we introduced a caspase-resistant PKC-delta mutant (D330A) into human keratinocytes by retrovirus transduction...
March 2005: Cell Death and Differentiation
S Husain, D Young, C J Wingard
Constriction of the penile vasculature prevents erection and is largely mediated by physiological agonists. We hypothesized that protein kinase C (PKC) may act as a regulator of penile vascular tone. Studies were designed to identify PKC isoforms present and to investigate their roles in phenylephrine-induced muscle contraction in the isolated rat corpora cavernosa. We demonstrated the presence of PKCalpha, beta, gamma, epsilon, delta, eta, and iota in rat corpora cavernosa and a subcellular distribution, which favored a membrane association for PKCalpha, beta, delta, and iota...
August 2004: International Journal of Impotence Research
Taketoshi Kajimoto, Yasuhito Shirai, Norio Sakai, Toshiyoshi Yamamoto, Hidenori Matsuzaki, Ushio Kikkawa, Naoaki Saito
Protein kinase C (PKC), a Ca(2+)/phospholipid-dependent protein kinase, is known as a key enzyme in various cellular responses, including apoptosis. However, the functional role of PKC in apoptosis has not been clarified. In this study, we focused on the involvement of PKCdelta in ceramide-induced apoptosis in HeLa cells and examined the importance of spatiotemporal activation of the specific PKC subtype in apoptotic events. Ceramide-induced apoptosis was inhibited by the PKCdelta-specific inhibitor rottlerin and also was blocked by knockdown of endogenous PKCdelta expression using small interfering RNA...
March 26, 2004: Journal of Biological Chemistry
Corinne Quittau-Prévostel, Nathalie Delaunay, Alejandra Collazos, Alice Vallentin, Dominique Joubert
Protein kinase C (PKC) has been implicated in the control of intercellular adhesion. Our previous observation demonstrating that activated PKC alpha (PKCalpha is selectively targeted to cell-cell contacts of pituitary GH3B6 cells supports these findings. The relevance of this observation is further strengthened by the present data establishing that this targeting selectivity also occurs in the pituitary gland. Moreover, a new mechanism involved in the control of PKC targeting is unravelled. We demonstrate that a three amino acid motif located in the V3 region of alpha and epsilon (epsilon (GDE/GEE respectively) is essential for the targeting selectivity of these isoforms because: (1) this motif is absent in delta (delta) and mutated in the natural D294GPKCalpha mutant, which do not exhibit such selectivity, and (2) a GEE to GGE mutation abolishes the selectivity of targeting to cell-cell contacts for epsilon, as it does for the D294G PKCalpha mutant...
January 1, 2004: Journal of Cell Science
Qingding Wang, Xiaofu Wang, B Mark Evers
Activation of protein kinase C (PKC) prevents apoptosis in certain cells; however, the mechanisms are largely unknown. Inhibitors of apoptosis (IAP) family members, including NAIP, cIAP-1, cIAP-2, XIAP/hILP, survivin, and BRUCE, block apoptosis by binding and potently inhibiting caspases. Activation of NF-kappa B contributes to cIAP-2 induction; however, the cellular mechanisms regulating cIAP-2 expression have not been entirely defined. In this study, we examined the role of the PKC and NF-kappa B pathways in the regulation of cIAP-2 in human colon cancers...
December 19, 2003: Journal of Biological Chemistry
Antonella Muscella, Simona Greco, Maria Giovanna Elia, Carlo Storelli, Santo Marsigliante
We examined the signalling pathways responsible for the Ang II induction of growth in MCF-7 human breast cancer cells. Ang II in MCF-7 cells induced: (a) the translocation from the cytosol to membrane and nucleus of atypical protein kinase C-zeta (PKC-zeta) but not of PKC-alpha, -delta, - epsilon and -eta; (b) the expression of c-fos mRNA and protein; (c) the phosphorylation of the extracellular signal-regulated protein kinases 1 and 2 (ERK1/2). All these effects were due to the activation of the Ang II type I receptor (AT1) since they were blocked by the AT1 antagonist losartan...
October 2003: Journal of Cellular Physiology
Jae-Won Soh, I Bernard Weinstein
Although protein kinase C (PKC) has been implicated in cell cycle progression, cell proliferation, and tumor promotion, the precise roles of specific isoforms in these processes is not clear. Therefore, we constructed and analyzed a series of expression vectors that encode hemagglutinin-tagged wild type (WT), constitutively active mutants (Delta NPS and CAT), and dominant negative mutants of PKCs alpha, beta 1, beta 2, gamma, delta, epsilon, eta, zeta, and iota. Cyclin D1 promoter reporter assays done in serum-starved NIH3T3 cells indicated that the constitutively active mutants of PKC-alpha and PKC-epsilon were the most potent activators of this reporter, whereas the constitutively active mutant of PKC-delta inhibited its activity...
September 5, 2003: Journal of Biological Chemistry
Takashi Minami, Md Ruhul Abid, Jie Zhang, George King, Tatsuhiko Kodama, William C Aird
We recently demonstrated that thrombin induces the expression of vascular adhesion molecule-1 (VCAM-1) in endothelial cells by an NF-kappaB- and GATA-dependent mechanism. In the present study, we describe the signaling pathways that mediate this response. Thrombin stimulation of the VCAM-1 gene and promoter in human umbilical vein endothelial cells was inhibited by preincubation with the phosphatidylinositol 3-kinase inhibitor, LY294002, the protein kinase C (PKC)-delta inhibitor, rottlerin, a PKC-zeta peptide inhibitor, or by overexpression of dominant negative (DN)-PKC-zeta...
February 28, 2003: Journal of Biological Chemistry
Harvey S Hahn, Martin G Yussman, Tsuyoshi Toyokawa, Yehia Marreez, Thomas J Barrett, K Chad Hilty, Hanna Osinska, Jeffrey Robbins, Gerald W Dorn
To delineate the in vivo cardiac functions requiring normal delta protein kinase C (PKC) activity, we pursued loss-of-function through transgenic expression of a deltaPKC-specific translocation inhibitor protein fragment, deltaV1, in mouse hearts. Initial results using the mouse alpha-myosin heavy chain (alphaMHC) promoter resulted in a lethal heart failure phenotype. Viable deltaV1 mice were therefore obtained using novel attenuated mutant alphaMHC promoters lacking one or the other thyroid response element (TRE-1 and -2)...
October 18, 2002: Circulation Research
Paolo Pinton, Takashi Tsuboi, Edward K Ainscow, Tullio Pozzan, Rosario Rizzuto, Guy A Rutter
The mechanisms by which glucose may affect protein kinase C (PKC) activity in the pancreatic islet beta-cell are presently unclear. By developing adenovirally expressed chimeras encoding fusion proteins between green fluorescent protein and conventional (betaII), novel (delta), or atypical (zeta) PKCs, we show that glucose selectively alters the subcellular localization of these enzymes dynamically in primary islet and MIN6 beta-cells. Examined by laser scanning confocal or total internal reflection fluorescence microscopy, elevated glucose concentrations induced oscillatory translocations of PKCbetaII to spatially confined regions of the plasma membrane...
October 4, 2002: Journal of Biological Chemistry
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