Determination of triacylglycerol composition in vegetable oils using high-performance liquid chromatography: a collaborative study.

Triacylglycerol (TAG) composition in vegetable oils was collaboratively analyzed in 9 laboratories using high-performance liquid chromatography (HPLC) equipped with a refractive index detector. Dococyl (C22) and triacontyl (C30) silica columns were used for analysis. The TAG molecular species in soybean, rapeseed, and palm oils were individually separated on the chromatogram.

Trm2p-dependent derepression is essential for methanol-specific gene activation in the methylotrophic yeast Candida boidinii.

We identified a gene, designated TRM2, responsible for methanol-inducible gene expression in the methylotrophic yeast Candida boidinii. The encoded protein Trm2p contains two C(2)H(2)-type zinc finger motifs near the N terminus and shows high similarity to Saccharomyces cerevisiae Adr1p and Pichia pastoris Mxr1p. A C.

Interaction of endothelial cell-selective adhesion molecule and MAGI-1 promotes mature cell-cell adhesion via activation of RhoA.

Endothelial cell-selective adhesion molecule (ESAM) is a member of the immunoglobulin superfamily and mediates homophilic adhesion between endothelial cells. ESAM has been shown to bind to membrane-associated guanylate kinase (MAGUK) with inverted domain structure 1 (MAGI-1), but the interaction between these molecules remains unknown. We investigated the role of ESAM in the subcellular localization of MAGI-1 and cell adhesion by means of transfection experiments using Chinese hamster ovary (CHO) cells.

Anti-tumor effect of pegylated interferon in the rat hepatocarcinogenesis model.

Interferon (IFN) is a multifunctional cytokine which works as a suppressor of hepatocarcinogenesis. Pegylated interferon (PEG-IFN) is a modified form of IFN with different pharmacokinetics. We evaluated the anti-tumor effect of PEG-IFN using a rat hepatocarcinogenesis model.

Phosphorylation and up-regulation of diacylglycerol kinase gamma via its interaction with protein kinase C gamma.

Diacylglycerol (DAG) acts as an allosteric activator of protein kinase C (PKC) and is converted to phosphatidic acid by DAG kinase (DGK). Therefore, DGK is thought to be a negative regulator of PKC activation. Here we show molecular mechanisms of functional coupling of the two kinases.

Activation and translocation of PKCdelta is necessary for VEGF-induced ERK activation through KDR in HEK293T cells.

VEGF-KDR/Flk-1 signal utilizes the phospholipase C-gamma-protein kinase C (PKC)-Raf-MEK-ERK pathway as the major signaling pathway to induce gene expression and cPLA2 phosphorylation. However, the spatio-temporal activation of a specific PKC isoform induced by VEGF-KDR signal has not been clarified. We used HEK293T (human embryonic kidney) cells expressing transiently KDR to examine the activation mechanism of PKC.

Mammalian Sprouty4 suppresses Ras-independent ERK activation by binding to Raf1.

The signalling cascade including Raf, mitogen-activated protein kinase (MAPK) kinase and extracellular-signal-regulated kinase (ERK) is important in many facets of cellular regulation. Raf is activated through both Ras-dependent and Ras-independent mechanisms, but the regulatory mechanisms of Raf activation remain unclear. Two families of membrane-bound molecules, Sprouty and Sprouty-related EVH1-domain-containing protein (Spred) have been identified and characterized as negative regulators of growth-factor-induced ERK activation.

Importance of C1B domain for lipid messenger-induced targeting of protein kinase C.

The molecular mechanisms by which arachidonic acid (AA) and ceramide elicit translocation of protein kinase C (PKC) were investigated. Ceramide translocated epsilonPKC from the cytoplasm to the Golgi complex, but with a mechanism distinct from that utilized by AA. Using fluorescence recovery after photobleaching, we showed that, upon treatment with AA, epsilonPKC was tightly associated with the Golgi complex; ceramide elicited an accumulation of epsilonPKC which was exchangeable with the cytoplasm.