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Biochemical characterization and expression analysis of neural thrombospondin-1-like proteins NELL1 and NELL2.
The results strongly suggest that the NELL2 protein, similar to but not identical with TSP-1, is involved in the growth and differentiation of neural cells.
Reactive Oxygen Species Derived from NOX1/NADPH Oxidase Enhance Inflammatory Pain
It is indicated that NOX1/NADPH oxidase accelerates the translocation of PKCε in DRG neurons, thereby enhancing the TRPV1 activity and the sensitivity to painful stimuli.
Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1
It is shown that mammalian Sprouty4 suppresses vascular epithelial growth factor-induced, Ras-independent activation of Raf1 but does not affect epidermal growth factor (EGF-induced) and Ras-dependent activated Raf1, and that SproutY4 differentially regulates these pathways.
Production of specific antibodies against GABA transporter subtypes (GAT1, GAT2, GAT3) and their application to immunocytochemistry.
Mammalian Sprouty4 Suppresses Ras-Independent ERK Activation by Binding to Raf1
No abstract available.
Duox maturation factors form cell surface complexes with Duox affecting the specificity of reactive oxygen species generation
- Stanislas C. Morand, T. Ueyama, S. Tsujibe, N. Saito, A. Korzeniowska, T. Leto
- BiologyFASEB journal : official publication of the…
- 1 April 2009
Findings suggest Duox activators not only promote Duox maturation, but they function as part of the hydrogen peroxide‐generating enzyme.
Glucagon-like Peptide 1 Activates Protein Kinase C through Ca2+-dependent Activation of Phospholipase C in Insulin-secreting Cells*
- Yuko Suzuki, Hui H Zhang, N. Saito, I. Kojima, T. Urano, H. Mogami
- BiologyJournal of Biological Chemistry
- 29 September 2006
GLp-1 can activate PKCα and PKCϵ, and these GLP-1-activated PKCs may contribute considerably to insulin secretion at a substimulatory concentration of glucose.
Enzymological Analysis of Mutant Protein Kinase Cγ Causing Spinocerebellar Ataxia Type 14 and Dysfunction in Ca2+ Homeostasis*
Pharmacological experiments showed that canonical transient receptor potential (TRPC) channels are responsible for the Ca2+ influx regulated by PKCγ, and in vitro kinase assays revealed that most C1 domain mutants are constitutively active, they could not phosphorylate TRPC3 channels in vivo.
Increased sensitivity of desensitized TRPV1 by PMA occurs through PKCepsilon-mediated phosphorylation at S800.
PCepsilon and S800 are identified as important therapeutic targets that may help regulate inhibitory effects on TRPV1 and hence its desensitization and phosphorylation.
Protein Kinase C-induced Phosphorylation of Orai1 Regulates the Intracellular Ca2+ Level via the Store-operated Ca2+ Channel*
- Takumi Kawasaki, T. Ueyama, I. Lange, S. Feske, N. Saito
- Biology, Computer ScienceThe Journal of Biological Chemistry
- 9 June 2010
It is demonstrated that protein kinase C (PKC) suppresses store-operated Ca2+ entry (SOCE) by phosphorylation of Orai1, and proposed that PKC suppresses SOCE and CRAC channel function byosphorylated of ORAi1 at N-terminal serine residues Ser-27 and Ser-30.