Inositol-1,4,5-trisphosphate-binding proteins controlling the phototransduction cascade of invertebrate visual cells

2001 ◽  
Vol 204 (3) ◽  
pp. 487-493
Author(s):  
A. Kishigami ◽  
T. Ogasawara ◽  
Y. Watanabe ◽  
M. Hirata ◽  
T. Maeda ◽  
...  
Keyword(s):  
Phospholipase C ◽  
Binding Proteins ◽  
Affinity Column ◽  
Receptor Kinase ◽  
Nucleotide Exchange ◽  
Visual Cells ◽  
Signal Cascade ◽  
Phosphatidylinositol Turnover ◽  
Inositol 1,4,5 Trisphosphate ◽  
Phototransduction Cascade

The main phototransduction cascade in invertebrate visual cells involves the turnover of phosphatidylinositol, an important biochemical mechanism common to many signal-transduction systems. Light-activated rhodopsin stimulates guanine nucleotide exchange on the Gq class of G-protein, which activates phospholipase C to hydrolyze phosphatidylinositol 4,5-bisphosphate to inositol-1,4,5-trisphosphate and diacylglycerol. Subsequently, inositol-1,4,5-trisphosphate-binding proteins continue the signal cascade. Here, we report on the first inositol-1,4,5-trisphosphate-binding proteins demonstrated in an invertebrate visual system with our investigation of the photosensitive rhabdoms of squid. We screened the ability of proteins to interact with inositol-1,4,5-trisphosphate by affinity column chromatography with an inositol-1,4,5-trisphosphate analogue. We detected an inositol-1,4,5-trisphosphate-binding affinity in phospholipase C, receptor kinase and five other proteins in the cytosolic fraction and, surprisingly, rhodopsin in the membrane fraction. A binding assay with (3)H-labelled inositol-1,4,5-trisphosphate demonstrated the inositol-1,4,5-trisphosphate affinity of each of the purified proteins. Since rhodopsin, receptor kinase and phospholipase C are involved upstream of phosphatidylinositol turnover in the signal cascade, our result suggests that phosphatidylinositol turnover is important in feedback pathways in the signalling system.

scholarly journals A new inositol 1,4,5-trisphosphate binding protein similar to phospholipase C-δ1

1996 ◽  
Vol 313 (1) ◽  
pp. 319-325 ◽  
Author(s):  
Takashi KANEMATSU ◽  
Yoshio MISUMI ◽  
Yutaka WATANABE ◽  
Shoichiro OZAKI ◽  
Toshitaka KOGA ◽  
...  
Keyword(s):  
Amino Acids ◽  
Catalytic Activity ◽  
Rat Brain ◽  
Phospholipase C ◽  
Functional Significance ◽  
Binding Proteins ◽  
Binding Protein ◽  
Inositol 1,4,5 Trisphosphate ◽  
Molecular Masses ◽  
Novel Protein

We have reported that two inositol 1,4,5-trisphosphate binding proteins, with molecular masses of 85 and 130 kDa, were purified from rat brain; the former protein was found to be the ∆1-isoenzyme of phospholipase C (PLC-∆1) and the latter was an unidentified novel protein [Kanematsu, Takeya, Watanabe, Ozaki, Yoshida, Koga, Iwanaga and Hirata (1992) J. Biol. Chem. 267, 6518-6525]. Here we describe the isolation of the full-length cDNA for the 130 kDa Ins(1,4,5)P3 binding protein, which encodes 1096 amino acids. The predicted sequence of the 130 kDa protein had 38.2% homology to that of PLC-∆1. Three known domains of PLC-∆1 (pleckstrin homology and putative catalytic X and Y domains) were located at residues 110-222, 377-544 and 585-804 with 35.2%, 48.2% and 45.8% homologies respectively. However, the protein showed no PLC activity to phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol. The 130 kDa protein expressed by transfection in COS-1 cells bound Ins(1,4,5)P3 in the same way as the molecule purified from brain. Thus the 130 kDa protein is a novel Ins(1,4,5)P3 binding protein homologous to PLC-∆1, but with no catalytic activity. The functional significance of the 130 kDa protein is discussed.

scholarly journals Phosphatidylinositol-specific phospholipase C activity of chromaffin granule-binding proteins.

1985 ◽  
Vol 260 (12) ◽  
pp. 7171-7173 ◽  
Author(s):  
C E Creutz ◽  
L G Dowling ◽  
E M Kyger ◽  
R C Franson
Keyword(s):  
Phospholipase C ◽  
Binding Proteins ◽  
Chromaffin Granule

scholarly journals Stereospecific recognition of inositol 1,4,5-trisphosphate analogs by the phosphatase, kinase, and binding proteins.

1990 ◽  
Vol 265 (15) ◽  
pp. 8404-8407
Author(s):  
M Hirata ◽  
F Yanaga ◽  
T Koga ◽  
T Ogasawara ◽  
Y Watanabe ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Inositol 1,4,5 Trisphosphate

Phospholipase C activity in rat kidney Effect of deoxycholate on phosphatidylinositol turnover

1982 ◽  
Vol 712 (1) ◽  
pp. 65-70 ◽  
Author(s):  
Norma B. Speziale ◽  
Emir H.S. Speziale ◽  
Alicia Terragno ◽  
Noberto A. Terragno
Keyword(s):  
Phospholipase C ◽  
Rat Kidney ◽  
Phosphatidylinositol Turnover

Inhibition of TASK-1 potassium channel by phospholipase C

2001 ◽  
Vol 281 (2) ◽  
pp. C700-C708 ◽  
Author(s):  
Gábor Czirják ◽  
Gábor L. Petheő ◽  
András Spät ◽  
Péter Enyedi
Keyword(s):  
Phospholipase C ◽  
Lysophosphatidic Acid ◽  
Protein S ◽  
Receptor Activation ◽  
Xenopus Laevis Oocytes ◽  
Ang Ii ◽  
Inositol 1,4,5 Trisphosphate ◽  
Glomerulosa Cells ◽  
Pore Domain ◽  
Stimulation Of

The two-pore-domain K+ channel, TASK-1, was recently shown to be a target of receptor-mediated regulation in neurons and in adrenal glomerulosa cells. Here, we demonstrate that TASK-1 expressed in Xenopus laevis oocytes is inhibited by different Ca2+-mobilizing agonists. Lysophosphatidic acid, via its endogenous receptor, and ANG II and carbachol, via their heterologously expressed ANG II type 1a and M1 muscarinic receptors, respectively, inhibit TASK-1. This effect can be mimicked by guanosine 5′- O-(3-thiotriphosphate), indicating the involvement of GTP-binding protein(s). The phospholipase C inhibitor U-73122 reduced the receptor-mediated inhibition of TASK-1. Downstream signals of phospholipase C action (inositol 1,4,5-trisphosphate, cytoplasmic Ca2+ concentration, and diacylglycerol) do not mediate the inhibition. Unlike the Gq-coupled receptors, stimulation of the Gi-activating M2 muscarinic receptor coexpressed with TASK-1 results in an only minimal decrease of the TASK-1 current. However, additional coexpression of phospholipase C-β2 (which is responsive also to Giβγ-subunits) renders M2 receptor activation effective. This indicates the significance of phospholipase C activity in the receptor-mediated inhibition of TASK-1.

ATP stimulates Ca2+oscillations and contraction in airway smooth muscle cells of mouse lung slices

2002 ◽  
Vol 283 (6) ◽  
pp. L1271-L1279 ◽  
Author(s):  
Albrecht Bergner ◽  
Michael J. Sanderson
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Phospholipase C ◽  
Airway Smooth Muscle ◽  
Muscle Cells ◽  
Mouse Lung ◽  
Airway Smooth Muscle Cells ◽  
Airway Caliber ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

In airway smooth muscle cells (SMCs) from mouse lung slices, ≥10 μM ATP induced Ca2+oscillations that were accompanied by airway contraction. After ∼1 min, the Ca2+oscillations subsided and the airway relaxed. By contrast, ≥0.5 μM adenosine 5′- O-(3-thiotriphosphate) (nonhydrolyzable) induced Ca2+oscillations in the SMCs and an associated airway contraction that persisted for >2 min. Adenosine 5′- O-(3-thiotriphosphate)-induced Ca2+oscillations occurred in the absence of external Ca2+but were abolished by the phospholipase C inhibitor U-73122 and the inositol 1,4,5-trisphosphate receptor inhibitor xestospongin. Adenosine, AMP, and α,β-methylene ATP had no effect on airway caliber, and the magnitude of the contractile response induced by a variety of nucleotides could be ranked in the following order: ATP = UTP > ADP. These results suggest that the SMC response to ATP is impaired by ATP hydrolysis and mediated via P2Y2or P2Y4receptors, activating phospholipase C to release Ca2+via the inositol 1,4,5-trisphosphate receptor. We conclude that ATP can serve as a spasmogen of airway SMCs and that Ca2+oscillations in SMCs are required to sustain airway contraction.

scholarly journals μ-opioids activate phospholipase C in SH-SY5Y human neuroblastoma cells via calcium-channel opening

1995 ◽  
Vol 305 (2) ◽  
pp. 577-581 ◽  
Author(s):  
D Smart ◽  
G Smith ◽  
D G Lambert
Keyword(s):  
Phospholipase C ◽  
Opioid Receptor ◽  
Neuroblastoma Cells ◽  
Receptor Occupancy ◽  
Mu Opioid Receptor ◽  
Human Neuroblastoma ◽  
Mu Opioid ◽  
Inositol 1,4,5 Trisphosphate ◽  
Dependent Inhibition ◽  
Dose Dependent

We have recently reported that, in SH-SY5Y cells, mu-opioid receptor occupancy activates phospholipase C via a pertussis toxin-sensitive G-protein. In the present study we have further characterized the mechanisms involved in this process. Fentanyl (0.1 microM) caused a monophasic increase in inositol 1,4,5-trisphosphate mass formation, with a peak (20.5 +/- 3.6 pmol/mg of protein) at 15 s. Incubation in Ca(2+)-free buffer abolished this response, while Ca2+ replacement 1 min later restored the stimulation of inositol 1,4,5-trisphosphate formation (20.1 +/- 0.6 pmol/mg of protein). In addition, nifedipine (1 nM-0.1 mM), an L-type Ca(2+)-channel antagonist, caused a dose-dependent inhibition of inositol 1,4,5-trisphosphate formation, with an IC50 of 60.3 +/- 1.1 nM. Elevation of endogenous beta/gamma subunits by selective activation of delta-opioid and alpha 2 adrenoceptors failed to stimulate phospholipase C. Fentanyl also caused a dose-dependent (EC50 of 16.2 +/- 1.0 nM), additive enhancement of carbachol-induced inositol 1,4,5-trisphosphate formation. In summary, we have demonstrated that in SH-SY5Y cells activation of the mu-opioid receptor allows Ca2+ influx to activate phospholipase C. However, the possible role of this mechanism in the process of analgesia remains to be elucidated.

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