A5052438029- Protein Kinase Regulation and GTPase Signaling
- Lipid metabolism and biosynthesis
- Metabolism, Diabetes, and Cancer
- Pancreatic function and diabetes
- Endoplasmic Reticulum Stress and Disease
- Peroxisome Proliferator-Activated Receptors
- Cellular transport and secretion
- Sphingolipid Metabolism and Signaling
- Caveolin-1 and cellular processes
- Receptor Mechanisms and Signaling
- Adipose Tissue and Metabolism
- Lipid Membrane Structure and Behavior
- Ubiquitin and proteasome pathways
- Glycosylation and Glycoproteins Research
- 14-3-3 protein interactions
- PI3K/AKT/mTOR signaling in cancer
- Cancer, Hypoxia, and Metabolism
- Immune Cell Function and Interaction
- Melanoma and MAPK Pathways
- Mitochondrial Function and Pathology
- Autophagy in Disease and Therapy
- Neuroscience and Neuropharmacology Research
- Viral Infectious Diseases and Gene Expression in Insects
- Retinal Development and Disorders
- Bipolar Disorder and Treatment
Chiba University
2016-2025
Weatherford College
2016
Hokkaido University
1983-2013
Yamagata University
2013
Sapporo Medical University
1999-2009
University of Eastern Finland
2008
Huntsman Cancer Institute
2001-2006
University of Utah
2001-2005
RMIT University
2004
Louisiana State University Health Sciences Center New Orleans
2001
A fourth member of the diacylglycerol kinase (DGK) gene family termed DGKδ was cloned from human testis cDNA library. The sequence contains an open reading frame 3,507 nucleotides encoding a putative DGK protein 130,006 Da. Interestingly, new isozyme pleckstrin homology domain found in number proteins involved signal transduction. Furthermore, C-terminal tail this is very similar to those EPH receptor tyrosine kinases. primary structure δ-isozyme also has two cysteine-rich zinc finger-like...
We obtained two human cDNA clones encoding phosphatidic acid phosphatase (PAP) isozymes named PAP-2a (M r = 32,158) and -2b 35, 119), both of which contained six putative transmembrane domains. Both enzymes were glycosylated cleaved by N-glycanase endo-β-galactosidase, thus suggesting their post-Golgi localization. shared 47% identical sequence judged to be the counterparts previously sequenced mouse 35-kDa PAP(83% identity) rat Dri42 protein (94% identity), respectively. Furthermore,...
Arachidonoyldiacylglycerol (20:4-DAG) is a second messenger derived from phosphatidylinositol 4,5-bisphosphate and generated by stimulation of glutamate metabotropic receptors linked to G proteins activation phospholipase C. 20:4-DAG signaling terminated its phosphorylation phosphatidic acid, catalyzed diacylglycerol kinase (DGK). We have cloned the murine DGKɛ gene that showed, when expressed in COS-7 cells, selectivity for 20:4-DAG. The significance synaptic function was investigated mice...
A unique type of chaperone that requires glucose trimming the target proteins has been shown to be important for their maturation in endoplasmic reticulum (ER). Calnexin, an ER membrane chaperone, is first example such a class. Here, we focus on calreticulin, major luminal protein, which shares with calnexin two sets characteristic sequence repeat. We evaluated function calreticulin by expressing it surface. constructed membrane-anchored chimera fusing truncated membrane-anchoring tagged...
We attempted to assess the regulatory role of EF-hand motifs recently detected in primary structure porcine 80-kDa diacylglycerol kinase (DGK) (Sakane, F., Yamada, K., Kanoh, H., Yokoyama, C., and Tanabe, T. (1990) Nature 344, 345-348). By using DGK purified from thymus cytosol, we found that this isozyme indeed bound 2 mol Ca2+ per enzyme with high affinity (apparent dissociation constant, kd = 0.3 microM). The binding was cooperative a Hill coefficient 1.4. next studied effect 1 x 10(-5) M...
Porcine thymus cytosol contains two immunologically distinct forms of diacylglycerol kinase (DGK) [Yamada, K. and Kanoh, H. (1988) Biochem. J. 255, 601–608]. These 2 DGK species, having apparent molecular masses 80 150 kDa, were purified from the cytosol. Upon sodium dodecyl sulfate‐polyacrylamide gel electrophoresis, 150‐kDa gave polypeptide bands 50 75 whereas 80‐kDa yielded a single protein band. The was markedly activated by 10–20 μM sphingosine as well known anionic activators such...
Ten mammalian diacylglycerol kinase (DGK) isozymes (a-γ) have been identified. Recent studies revealed that DGK play pivotal roles in a wide variety of pathophysiological functions. Thus, it is important to be able easily check activity each event. Moreover, the conventional assay quite laborious because requires use radioisotope and thin-layer chromatography including multiple extraction steps. In order minimize procedures, we established non-radioactive, single well, two-step...
Diacylglycerol kinase (DGK) consists of 10 isozymes. The α-isozyme enhances the proliferation cancer cells. However, DGKα facilitates nonresponsive state immunity known as T-cell anergy; therefore, malignant traits and suppresses immune surveillance. aim this study was to identify a novel small molecule that selectively potently inhibits activity. We screened library containing 9,600 chemical compounds using newly established high-throughput DGK assay. As result, we have obtained promising...
In order to clone novel diacylglycerol kinase (DGK) isozymes, we first obtained a DGK-related cDNA fragment by polymerase chain reaction using the human hepatoma cell line HepG2 mRNA and degenerated primers. The amplified was subsequently used as probe for screening library from cells. We coding DGK isozyme (designated gamma) comprised of 791 amino acid residues. sequence gamma 52 62% identical those previously sequenced porcine 80-kDa rat 90-kDa enzymes, respectively. gamma, although...
We previously described the purification of an 83-kDa phosphatidic acid phosphatase (PAP) from porcine thymus membranes (Kanoh, H., Imai, S.-i., Yamada, K. and Sakane, F. (1992) J. Biol. Chem. 267, 25309-25314). However, we found that a minor 35-kDa protein could account for PAP activity when purified enzyme preparation was further analyzed. thus determined N-terminal sequence candidate prepared antipeptide antibody against sequence, MFDKTRLPYVALDVL. The almost completely precipitated...
Diacylglycerol kinase (DGK) plays an important role in signal transduction through modulating the balance between two signaling lipids, diacylglycerol and phosphatidic acid. Here we identified a tenth member of DGK family designated DGKκ. The κ-isozyme (1271 amino acids, calculated molecular mass, 142 kDa) contains pleckstrin homology domain, cysteine-rich zinc finger-like structures, separated catalytic region as have been found commonly for type II isozymes previously cloned (DGKδ DGKη)....
Diacylglycerol kinases (DGKs) phosphorylate diacylglycerol (DAG) to terminate its signaling. To study DGKdelta, we disrupted gene in mice and found that DGKdelta deficiency reduced EGF receptor (EGFR) protein expression activity. Similar EGFR knockout mice, DGKdelta-deficient pups were born with open eyelids died shortly after birth. PKCs are activated by DAG reduce We accumulation, increased threonine phosphorylation of EGFR, enhanced other PKC substrates, autophosphorylation cells,...