Enhancement of collagen‐induced phosphoinositide turnover by thromboxane A<sub>2</sub> analogue through Ca<sup>2+</sup> mobilization in human platelets

Kaibuchi, Kozo; Tsuda, Terutaka; Kikuchi, Akira; Tanimoto, Tetsuji; Takai, Yoshimi

doi:10.1016/0014-5793(85)80052-1

Cited by 36 publications

(36 citation statements)

References 26 publications

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“…After the incubation for 3 days, the cells were deprived of FCS by washing twice with serum-free DMEM and incubating in the same medium for 48 h. During the period of this serum-deprivation, the down-regulation of protein kinase C was performed by adding 100 ng/ml of PDBu to the cells. After these cells were washed three times with DMEM containing 0.1°70 BSA, the Triton XoI00 extract was prepared as described [22]. The protein kinase C activity in the Triton X-100 extract (equivalent to 4 × 104 cells) prepared from the control and PDBupretreated ceils was assayed by measuring the incorporation of 32p into HI histone from [7-3zp]ATP as specified earlier [17].…”

Section: Resultsmentioning

confidence: 99%

Distinct functions of down‐regulation‐sensitive and ‐resistant types of protein kinase C in rabbit aortic smooth muscle cells

Kariya

Takai

1987

FEBS Letters

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In quiescent cultures of rabbit aortic smooth muscle cells, 12-O-tetradecanoylphorbol-13-acetate (TPA) induced DNA synthesis to some extent in the presence of rabbit plasma-derived serum but inhibited the rabbit whole blood serum (WBS)-induced DNA synthesis and increase in cytoplasmic free Ca 2 ÷ concentration ([Ca 2 + ]i). Prolonged treatment of the cells with phorbol-12,13-dibutyrate (PDBu) caused the partial downregulation of protein kinase C to a level of 25-35% of that in control cells. In these PDBu-pretreated cells, TPA neither induced DNA synthesis nor inhibited the WBS-induced DNA synthesis, but still inhibited the WBS-induced increase in [Ca2+]i. These results suggest (i) that there are down-regulation-sensitive and -resistant types of protein kinase C in rabbit aortic smooth muscle cells; (ii) that the down-regulation-sensitive type has the proliferative and antiproliferative actions whereas the down-regulation-resistant type lacks them; and (iii) that the down-regulation-resistant type has the activity to inhibit the WBS-induced increase in [Ca 2 +]i.

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Section: Resultsmentioning

confidence: 99%

Distinct functions of down‐regulation‐sensitive and ‐resistant types of protein kinase C in rabbit aortic smooth muscle cells

Kariya

Takai

1987

FEBS Letters

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“…Water-soluble InsP3 also acts as a second messenger for Ca2l mobilization from intracellular Ca2l stores (12). These two second messengers, as well as cAMP, may play crucial roles in the transition from the Go/Gj phase of the cell cycle in mammalian cells (13,14). Other materials were obtained from commercial sources.…”

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confidence: 99%

Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae.

Kaibuchi¹,

Miyajima²,

Arai³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

111

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Incubation of yeast Saccharomyces cerevisiae at very low (0.02%) glucose levels led to arrest of the cell cycle at the GO/Gj phase. Readdition of glucose to these "starved" yeast resulted in cell proliferation. In RAS1 and RAS2, that are homologous to mammalian ras-encoded proteins (3,4). Genetic analysis indicates that both RASI-and RAS2-encoded proteins are involved in activation of adenylate cyclase (5). RAS2 protein has been shown to activate adenylate cyclase activity in a cell-free system (6, 7). Yeast containing RAS2va'l9 (a RAS2 allele with a missense mutation, which is analogous to the oncogenic mammalian ras gene) has enhanced GTP-independent adenylate cyclase activity and increases intracellular cAMP (5). The RAS2vall9 strain tends to continue growth without undergoing Go/G1 arrest, presumably because of the high intracellular cAMP concentrations (5). Thus, yeast provides a useful model for studying the roles of oncogenes such as the ras gene in cell proliferation.Growth factors, such as platelet-derived growth factor and fibroblast growth factor, activate phospholipase C to induce hydrolysis of membrane inositolphospholipids (8,9). The initial products of this reaction are diacylglycerol and inositol trisphosphate (InsP3). Diacylglycerol remains in the membrane and serves as a second messenger for activation of protein kinase C (10, 11). Diacylglycerol is then metabolized to inositolphospholipids by way of phosphatidic acid (PtdOH) and CDP-diacylglycerol. Water-soluble InsP3 also acts as a second messenger for Ca2l mobilization from intracellular Ca2l stores (12). These two second messengers, as well as cAMP, may play crucial roles in the transition from the Go/Gj phase of the cell cycle in mammalian cells (13,14). Other materials were obtained from commercial sources.Yeast Strains and Plasmids. The S. cerevisiae strain SP1 (MATa leu2 ura3 trpl his3 ade8 canl) was used as the host for yeast plasmids. Starting from SP1, the isogenic mutants KKY1 (MATa leu2 ura3 trpl his3 ade8 can] rasl:: URA3) and KKY2 (MATa leu2 ura3 trpl his3 ade8 canl ras2:: URA3)

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“…Although there are conflicting data [12,13], intracellular Ca*+ and/or C-kinase might be another candidate for the regulation of c-myc activation as suggested by Kaibuchi et al [14]. Further experiments are necessary to confirm the possibility that abnormal PI turnover, as shown in this report, might be involved in the activation of the c-myc gene.…”

Section: Discussionmentioning

confidence: 57%

The enhanced ³²P labeling of CDP‐diacylglycerol in c‐myc gene expressed human kidney cancer cells

et al. 1987

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Correlation between c-myc gene expression and phosphatidylinositol (PI) metabolism was studied using seven human kidney cancer cell lines. We found that the exceptional incorporation of 32P into CDP-diacylglycerol (CDP-DG) was observed in only two cell lines, in which c-myc expression was increased among seven cell lines tested. In these two cell lines, PI was also labeled. The other five cell lines indicated the accumulation of radioactive PI, whereas CDP-DG was unlabeled.c-myc gene; Phosphatidylinositol metabolism; CDP-diacylglycerol; (Kidney cancer cell)

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Enhancement of collagen‐induced phosphoinositide turnover by thromboxane A₂ analogue through Ca²⁺ mobilization in human platelets

Cited by 36 publications

References 26 publications

Distinct functions of down‐regulation‐sensitive and ‐resistant types of protein kinase C in rabbit aortic smooth muscle cells

Distinct functions of down‐regulation‐sensitive and ‐resistant types of protein kinase C in rabbit aortic smooth muscle cells

Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae.

The enhanced ³²P labeling of CDP‐diacylglycerol in c‐myc gene expressed human kidney cancer cells

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Enhancement of collagen‐induced phosphoinositide turnover by thromboxane A2 analogue through Ca2+ mobilization in human platelets

Cited by 36 publications

References 26 publications

Distinct functions of down‐regulation‐sensitive and ‐resistant types of protein kinase C in rabbit aortic smooth muscle cells

Distinct functions of down‐regulation‐sensitive and ‐resistant types of protein kinase C in rabbit aortic smooth muscle cells

Possible involvement of RAS-encoded proteins in glucose-induced inositolphospholipid turnover in Saccharomyces cerevisiae.

The enhanced 32P labeling of CDP‐diacylglycerol in c‐myc gene expressed human kidney cancer cells

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Enhancement of collagen‐induced phosphoinositide turnover by thromboxane A₂ analogue through Ca²⁺ mobilization in human platelets

The enhanced ³²P labeling of CDP‐diacylglycerol in c‐myc gene expressed human kidney cancer cells