The Experts below are selected from a list of 3390 Experts worldwide ranked by ideXlab platform

Toshihiko Momiyama - One of the best experts on this subject based on the ideXlab platform.

  • nci h295r a human Adrenal Cortex derived Cell line expresses purinergic receptors linked to ca2 mobilization influx and cortisol secretion
    PLOS ONE, 2013
    Co-Authors: Haruhisa Nishi, Hirokazu Arai, Toshihiko Momiyama
    Abstract:

    Purinergic receptor expression and involvement in steroidogenesis were examined in NCI-H295R (H295R), a human Adrenal Cortex Cell line which expresses all the key enzymes necessary for steroidogenesis. mRNA/protein for multiple P1 (A2A and A2B), P2X (P2X5 and P2X7), and P2Y (P2Y1, P2Y2, P2Y6, P2Y12, P2Y13, and P2Y14) purinergic receptors were detected in H295R. 2MeS-ATP (10–1000 µM), a P2Y1 agonist, induced glucocorticoid (GC) secretion in a dose-dependent manner, while other extraCellular purine/pyrimidine agonists (1–1000 µM) had no distinct effect on GC secretion. ExtraCellular purines, even non-steroidogenic ones, induced Ca2+-mobilization in the Cells, independently of the extraCellular Ca2+ concentration. Increases in intraCellular Ca2+ concentration induced by extraCellular purine agonists were transient, except when induced by ATP or 2MeS-ATP. Angiotensin II (AngII: 100 nM) and dibutyryl-cyclic AMP (db-cAMP: 500 µM) induced both GC secretion and Ca2+-mobilization in the presence of extraCellular Ca2+ (1.2 mM). GC secretion by AngII was reduced by nifedipine (10–100 µM); whereas the Ca2+ channel blocker did not inhibit GC secretion by 2MeS-ATP. Thapsigargin followed by extraCellular Ca2+ exposure induced Ca2+-influx in H295R, and the Cells expressed mRNA/protein of the component molecules for store-operated calcium entry (SOCE): transient receptor C (TRPC) channels, calcium release-activated calcium channel protein 1 (Orai-1), and the stromal interaction molecule 1 (STIM1). In P2Y1-knockdown, 2MeS-ATP-induced GC secretion was significantly inhibited. These results suggest that H295R expresses a functional P2Y1 purinergic receptor for intraCellular Ca2+-mobilization, and that P2Y1 is linked to SOCE-activation, leading to Ca2+-influx which might be necessary for glucocorticoid secretion.

Haruhisa Nishi - One of the best experts on this subject based on the ideXlab platform.

  • nci h295r a human Adrenal Cortex derived Cell line expresses purinergic receptors linked to ca2 mobilization influx and cortisol secretion
    PLOS ONE, 2013
    Co-Authors: Haruhisa Nishi, Hirokazu Arai, Toshihiko Momiyama
    Abstract:

    Purinergic receptor expression and involvement in steroidogenesis were examined in NCI-H295R (H295R), a human Adrenal Cortex Cell line which expresses all the key enzymes necessary for steroidogenesis. mRNA/protein for multiple P1 (A2A and A2B), P2X (P2X5 and P2X7), and P2Y (P2Y1, P2Y2, P2Y6, P2Y12, P2Y13, and P2Y14) purinergic receptors were detected in H295R. 2MeS-ATP (10–1000 µM), a P2Y1 agonist, induced glucocorticoid (GC) secretion in a dose-dependent manner, while other extraCellular purine/pyrimidine agonists (1–1000 µM) had no distinct effect on GC secretion. ExtraCellular purines, even non-steroidogenic ones, induced Ca2+-mobilization in the Cells, independently of the extraCellular Ca2+ concentration. Increases in intraCellular Ca2+ concentration induced by extraCellular purine agonists were transient, except when induced by ATP or 2MeS-ATP. Angiotensin II (AngII: 100 nM) and dibutyryl-cyclic AMP (db-cAMP: 500 µM) induced both GC secretion and Ca2+-mobilization in the presence of extraCellular Ca2+ (1.2 mM). GC secretion by AngII was reduced by nifedipine (10–100 µM); whereas the Ca2+ channel blocker did not inhibit GC secretion by 2MeS-ATP. Thapsigargin followed by extraCellular Ca2+ exposure induced Ca2+-influx in H295R, and the Cells expressed mRNA/protein of the component molecules for store-operated calcium entry (SOCE): transient receptor C (TRPC) channels, calcium release-activated calcium channel protein 1 (Orai-1), and the stromal interaction molecule 1 (STIM1). In P2Y1-knockdown, 2MeS-ATP-induced GC secretion was significantly inhibited. These results suggest that H295R expresses a functional P2Y1 purinergic receptor for intraCellular Ca2+-mobilization, and that P2Y1 is linked to SOCE-activation, leading to Ca2+-influx which might be necessary for glucocorticoid secretion.

Yoshiaki Fujiikuriyama - One of the best experts on this subject based on the ideXlab platform.

  • analysis of functional domains of a gc box binding protein bteb
    Journal of Biochemistry, 1995
    Co-Authors: Akira Kobayashi, Kazuhiro Sogawa, Hiroaki Imataka, Yoshiaki Fujiikuriyama
    Abstract:

    BTEB is a small GC box-binding protein containing three contiguous zinc finger structures in the C-terminal region of the molecule, and activates or represses the transcription of genes with the GC box sequence in the promoter, depending on the repetitiveness of the GC box sequence [Imataka et al. (1992) EMBO J. 11, 3663-3671]. We have analyzed functional domains of BTEB in a transient expression system using Y-1 Cells (a mouse Adrenal Cortex Cell line). BTEB contained two regions responsible for the transcriptional activation. These regions showed a sequence similarity to each other and appeared to enhance the transcription independently. The two sequences were rich in hydrophobic amino acids and showed no similarity to the sequences of transactivation domains so far elucidated. The DNA-binding properties of BTEB were also analyzed by means of the gel mobility shift assay. Three contiguous zinc finger motifs were needed for the binding activity. Furthermore, it was revealed that a short basic region immediately N-terminal to the zinc finger motifs was required for the DNA binding.

Hirokazu Arai - One of the best experts on this subject based on the ideXlab platform.

  • nci h295r a human Adrenal Cortex derived Cell line expresses purinergic receptors linked to ca2 mobilization influx and cortisol secretion
    PLOS ONE, 2013
    Co-Authors: Haruhisa Nishi, Hirokazu Arai, Toshihiko Momiyama
    Abstract:

    Purinergic receptor expression and involvement in steroidogenesis were examined in NCI-H295R (H295R), a human Adrenal Cortex Cell line which expresses all the key enzymes necessary for steroidogenesis. mRNA/protein for multiple P1 (A2A and A2B), P2X (P2X5 and P2X7), and P2Y (P2Y1, P2Y2, P2Y6, P2Y12, P2Y13, and P2Y14) purinergic receptors were detected in H295R. 2MeS-ATP (10–1000 µM), a P2Y1 agonist, induced glucocorticoid (GC) secretion in a dose-dependent manner, while other extraCellular purine/pyrimidine agonists (1–1000 µM) had no distinct effect on GC secretion. ExtraCellular purines, even non-steroidogenic ones, induced Ca2+-mobilization in the Cells, independently of the extraCellular Ca2+ concentration. Increases in intraCellular Ca2+ concentration induced by extraCellular purine agonists were transient, except when induced by ATP or 2MeS-ATP. Angiotensin II (AngII: 100 nM) and dibutyryl-cyclic AMP (db-cAMP: 500 µM) induced both GC secretion and Ca2+-mobilization in the presence of extraCellular Ca2+ (1.2 mM). GC secretion by AngII was reduced by nifedipine (10–100 µM); whereas the Ca2+ channel blocker did not inhibit GC secretion by 2MeS-ATP. Thapsigargin followed by extraCellular Ca2+ exposure induced Ca2+-influx in H295R, and the Cells expressed mRNA/protein of the component molecules for store-operated calcium entry (SOCE): transient receptor C (TRPC) channels, calcium release-activated calcium channel protein 1 (Orai-1), and the stromal interaction molecule 1 (STIM1). In P2Y1-knockdown, 2MeS-ATP-induced GC secretion was significantly inhibited. These results suggest that H295R expresses a functional P2Y1 purinergic receptor for intraCellular Ca2+-mobilization, and that P2Y1 is linked to SOCE-activation, leading to Ca2+-influx which might be necessary for glucocorticoid secretion.

Akira Kobayashi - One of the best experts on this subject based on the ideXlab platform.

  • analysis of functional domains of a gc box binding protein bteb
    Journal of Biochemistry, 1995
    Co-Authors: Akira Kobayashi, Kazuhiro Sogawa, Hiroaki Imataka, Yoshiaki Fujiikuriyama
    Abstract:

    BTEB is a small GC box-binding protein containing three contiguous zinc finger structures in the C-terminal region of the molecule, and activates or represses the transcription of genes with the GC box sequence in the promoter, depending on the repetitiveness of the GC box sequence [Imataka et al. (1992) EMBO J. 11, 3663-3671]. We have analyzed functional domains of BTEB in a transient expression system using Y-1 Cells (a mouse Adrenal Cortex Cell line). BTEB contained two regions responsible for the transcriptional activation. These regions showed a sequence similarity to each other and appeared to enhance the transcription independently. The two sequences were rich in hydrophobic amino acids and showed no similarity to the sequences of transactivation domains so far elucidated. The DNA-binding properties of BTEB were also analyzed by means of the gel mobility shift assay. Three contiguous zinc finger motifs were needed for the binding activity. Furthermore, it was revealed that a short basic region immediately N-terminal to the zinc finger motifs was required for the DNA binding.