Spelling suggestions: "subject:"1protein 3kinase C"" "subject:"1protein 6kinase C""
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The role of protein kinase C in the regulation of intracellular signalling and stimulus-secretion coupling in parathyroid cellsRacke, Frederick Karl January 1993 (has links)
No description available.
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Regulation of the PDGF genes and translocation patterns of protein kinase C isotypes in human glioblastomasMisra-Press, Anita January 1991 (has links)
No description available.
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Propofol-Anesthesia, Diabetes and Myocardial Signal Transduction: Role of Protein Kinase C and Nitric OxideWickley, Peter J. 27 March 2008 (has links)
No description available.
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Regulation of Folate Receptor Raft RecyclingElnakat, Hala 14 April 2007 (has links)
No description available.
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Inhibition of HOX/PBX dimer formation leads to necroptosis in acute myeloid leukemia cellsAlharbi, R.A., Pandha, H.S., Simpson, G.R., Pettengell, R., Poterlowicz, Krzysztof, Thompson, A., Harrington, K.J., El-Tanani, Mohamed, Morgan, Richard 08 July 2017 (has links)
Yes / The HOX genes encode a family of transcription factors that have key roles in both development and malignancy. Disrupting the interaction between HOX proteins and their binding partner, PBX, has been shown to cause apoptotic cell death in a range of solid tumors. However, despite HOX proteins playing a particularly significant role in acute myeloid leukemia (AML), the relationship between HOX gene expression and patient survival has not been evaluated (with the exception of HOXA9), and the mechanism by which HOX/PBX inhibition induces cell death in this malignancy is not well understood. In this study, we show that the expression of HOXA5, HOXB2, HOXB4, HOXB9, and HOXC9, but not HOXA9, in primary AML samples is significantly related to survival. Furthermore, the previously described inhibitor of HOX/PBX dimerization, HXR9, is cytotoxic to both AML-derived cell lines and primary AML cells from patients. The mechanism of cell death is not dependent on apoptosis but instead involves a regulated form of necrosis referred to as necroptosis. HXR9-induced necroptosis is enhanced by inhibitors of protein kinase C (PKC) signaling, and HXR9 combined with the PKC inhibitor Ro31 causes a significantly greater reduction in tumor growth compared to either reagent alone. / Funded in part through a grant to RA from the Cultural Bureau of the Kingdom of Saudi Arabia.
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Protein kinase C-eta (PKC-ē) is required for the expression of the inducible nitric oxide synthase (NOS II) in human monocytic cells : a correlation in transcription between PKC-ē and NOS II in inflammatory arthritides /Pham, Tram Ngoc Quynh, January 2003 (has links)
Thesis (Ph.D.)--Memorial University of Newfoundland, 2004. / Bibliography: leaves 217-246.
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Initial characterization and determination of the molecular mechanism(s) that control transcription of the human PKC epsilon gene in lung cancer cellsAkinyi, Linnet. January 2004 (has links)
Thesis (M.S.)--University of Florida, 2004. / Typescript. Title from title page of source document. Document formatted into pages; contains 52 pages. Includes Vita. Includes bibliographical references.
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Pl3-kinase mediates cSrc activation and podosome formation through the adaptor protein, AFAP-110, in response to PKC[alpha] activationWalker, Valerie Glynis. January 2007 (has links)
Thesis (Ph. D.)--West Virginia University, 2007. / Title from document title page. Document formatted into pages; contains viii, 306 p. : ill. (some col.). Vita. Includes abstract. Includes bibliographical references.
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Protein Kinase C Activation in Hyperglycemic Bovine Lens Epithelial CellsFan, Wen-Lin 12 1900 (has links)
This study demonstrates the presence of protein kinase C activity in both cytosolic and membrane fractions of bovine lens epithelial cells in culture. Protein kinase C activity is similar in normal and hyperglycemic cells. Furthermore, the ability of the enzyme to translocate from the cytosol to the membrane following phorbol ester treatment is unimpeded by hyperglycemic conditions. Moreover, protein kinase C activation had no effect on myoinositol uptake either in normal cells or in cells exposed to hyperglycemic conditions.
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Differential responses of mouse nasal and temporal retinal neurites to chondroitin sulphates: the role of protein kinase C.January 2005 (has links)
Lam Shi Ying Joyce. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2005. / Includes bibliographical references (leaves 107-114). / Abstract in English and Chinese. / Chapter CHAPTER 1 --- GENERAL INTRODUCTION --- p.1-19 / Chapter CHAPTER 2 --- EXPRESSION OF PROTEIN KINASE C (PKC) ISOFORMS IN THE VENTRAL TEMPORAL (VT) AND DORSAL NASAL (DN) RETINAL GROWTH CONES OF MOUSE EMBRYOS / INTRODUCTION --- p.20-22 / MATERIALS AND METHODS --- p.22-24 / RESULTS --- p.24-31 / DISCUSSION --- p.31-37 / FIGURES --- p.38-46 / Chapter CHAPTER 3 --- EFFECTS ON MOUSE NASAL AND TEMPORAL RETINAL NEURITES TO CHONDROITIN SULPHATES (CS) AFTER ALTERATION OF PKC ACTIVITY / INTRODUCTION --- p.47-48 / MATERIALS AND METHODS --- p.49-51 / RESULTS --- p.51-59 / DISCUSSION --- p.60-67 / FIGURES --- p.68-74 / Chapter CHAPTER 4 --- EFFECTS ON AXON ROUTING AFTER ALTERATION OF PKC ACTIVITY ON GUIDANCE OF RETINAL GANGLION CELL AXONS AT THE OPTIC CHIASM OF MOUSE EMBRYOS / INTRODUCTION --- p.75-76 / MATERIALS AND METHODS --- p.77-80 / RESULTS --- p.80-89 / DISCUSSION --- p.89-95 / FIGURES --- p.96-103 / Chapter CHAPTER 5 --- GENERAL CONCLUSION --- p.104-106 / REFERENCES --- p.107-114
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