The roles of multiple pathways in regulating bombesin-stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Briscoe, Celia P.; Martin, Ashley; Wakelam, Michael J.O.

doi:10.1042/bj3060115

Cited by 26 publications

(25 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although a PKC inhibitor, staurosporine (5 tiM), blocked PMA-induced PLD activation by 77%, it had no effect on the CCh-induced phosphatidylethanol formation (Kanoh et al, 1992). A more selective PKC inhibitor, Ro 31-8425 (5 pM) gave almost identical results (Table 1) Several recent studies have indicated that protein tyrosine phosphorylation participates in PLD activation via an as yet unidentified mechanism (Uings et al, 1992;Liu et al, 1994;Briscoe et a!., 1995;Ward et a!., 1995). Here we have investigated the involvement of protein tyrosine phosphorylation in CCh-induced PLD activation in PC 12 cells.…”

Section: Resultssupporting

confidence: 62%

“…Furthermore, the stimulation of PLD activity through enhancement of protein tyrosine phosphorylation via G protein-coupled receptors has also been reported, with examples being fMet-Leu-Phe receptor (Uings et a!., 1992), bombesin receptor (Briscoe et a!., 1995), noradrenaline receptor (Ward et al, 1995), and platelet-activating factor (PAF) receptor (Liu et al, 1994). Elevation of intracellular Ca 2~may also be involved in the PKC-independent pathways of PLD activation (Exton, 1994;Kumada et a!., 1995).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Implication of Ca²⁺‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Ito

Kanoh

Nozawa

1997

Journal of Neurochemistry

View full text Add to dashboard Cite

Abstract:The mechanism for carbachol (CCh)-induced phospholipase D (PLD) activation was investigated in [3H]palmitic acid-labeled pheochromocytoma P012 cells with respect to the involvement of protein tyrosine phosphorylationand Ca2~. PLD activity was assessed by measuring the formation of [3H]phosphatidylbutanol in the presence of 0.3% butanol. Pretreatment of cells with the tyrosine kinase inhibitors herbimycin A, genistein, and tyrphostin inhibited PLD activation by CCh. Western blot analysis revealed several apparent tyrosine-phosphorylated protein bands (111,91, 84, 74,(65)(66)(67)(68)(69)(70) 44, and 42 kDa) in P012 cells treated with CCh. Phosphorylation of the 111-, 91-, 84-, and 65-70-kDa proteins peaked within 1 mm, and their time-dependent changes seemingly correlated with that of PLD activation. Others (74, 44MAPK,and 42MAPK kDa) were phosphorylated rather slowly, and maximal tyrosine phosphorylation was observed at 2 mm. Herbimycin A inhibited PLD activity and tyrosine phosphorylation of four proteins (111, 91, 84,(65)(66)(67)(68)(69)(70) in a preincubation time-and concentration-dependent fashion. In Ca 2~-freebuffer, CCh-induced [3H]phosphatidylbutanol formation and protein tyrosine phosphorylation were abolished. A Ca2~ionophore, A23187, caused PLD activation and tyrosine phosphorylation of four proteins of 111, 91, 84, and 65-70 kDa only in the presence of extracellular Ca2~. Extracellular Ca2~depen-dency for CCh-induced PLD activation was well correlated with that for tyrosine phosphorylation of the four proteins listed above, especially the 111 -kDa protein.These results suggest that Ca2-dependent protein tyrosine phosphorylation is closely implicated in OCh-induced PLO activation in P012 cells.

show abstract

Section: Resultssupporting

confidence: 62%

mentioning

confidence: 99%

Implication of Ca²⁺‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Ito

Kanoh

Nozawa

1997

Journal of Neurochemistry

View full text Add to dashboard Cite

show abstract

“…The linkage of PKC to the PLD signal transduction pathway may depend on the tissue and the stage of development studied (Briscoe et al, 1995;Exton, 1997;Klein et al, 1997;Schmidt et al, 1996). Additionally, it has been reported that PKC activation of PLD may occur by ATP independent mechanism (Conricode et al, 1992;Singer et al, 1996), and this mechanism would not be inhibited by the bisindolemalemide family of PKC inhibitors since their action is due to a competitive inhibition of the ATP binding site (Gordge & Ryves, 1994).…”

Section: Discussionmentioning

confidence: 99%

Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Shinomura

Río

Breen

et al. 2000

British J Pharmacology

View full text Add to dashboard Cite

1 The pharmacological pro®le of metabotropic glutamate receptor (mGluR) activation of phospholipase D (PLD), and the associated signalling pathways, were examined in rat cerebrocortical synaptosomes. The assay was conducted using a transphosphatidylation reaction in synaptosomes which were pre-labelled with either [ 3 H]-arachidonic acid or [ 32 P]-orthophosphate. 2 The mGluR agonists (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid (1S,3R-ACPD) and (RS)-3,5-dihydroxyphenylglycine (DHPG), both activated PLD, while phorbol 12,13-dibutyrate (PDBu) treatment caused receptor-independent activation of PLD and had an additive e ect on 1S,3R-ACPD induced PLD activity. 3 A protein kinase C (PKC) inhibitor, GF109203X, failed to antagonize mGluR receptor-coupled PLD activity. We could not detect any increase in the products of PI (phosphoinositide)-speci®c phospholipase C (PI-PLC), inositol(1,4,5)trisphosphate or diacylglycerol, by 1S, 3R-ACPD at 15 s. However, diacylglycerol increased monophasically in response to mGluR agonists and remained elevated for at least 15 min. Phosphatidic acid phosphohydrolase (PAP) activity, which converts PA to DAG, was present in the synaptosomes. 4 These data suggest that, in rat cerebrocortical synaptosomes, the 1S,3R-ACPD-sensitive mGluR is coupled to PLD through a mechanism that is independent of both PKC and PI-PLC.

show abstract

“…Bombesin is among several peptide agonists known to induce the rapid tyrosine phosphorylation of a number of proteins in Swiss 3T3 cells [14,22]. The finding that genistein partially inhibited bombesin-stimulated PLD activity suggested that tyrosine kinases may be involved in the PKCindependent pathway of agonist-stimulated [3H]PtdBut generation.…”

Section: ~ Results and Discussionmentioning

confidence: 99%

“…Bombesin and vasopressin receptors in Swiss 3T3 cells couple through the pertussis-toxin insensitive G-protein, Gq to the activation of phospholipase Cfll. We have previously reported that bombesin-stimulated PLD activity was also regulated by guanine-nucleotides, though whether a G-protein other than Gq was involved was not determined [14]. However there is evidence that the small molecular weight G-proteins ARF [6,7] and rho [15] can regulate activity.…”

Section: ~ Results and Discussionmentioning

confidence: 99%

Heterologous desensitization of bombesin‐ and vasopressin‐stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Briscoe

Wakelam

1995

FEBS Letters

View full text Add to dashboard Cite

Bombesin-and vasopressin-stimulated phospholipase D (PLD) activities are rapidly desensitized in 3T3 cells, in addition both agonists are subject to heterologous desensitization. Binding studies showed that homologous desensitization was partly a result of loss of cell surface receptors, whilst heterologous desensitization was independent of receptor changes. Pretreatment with either agonist reduced subsequent GTPyS-stimulated PLD activity by 50% whereas a pretreatment with GTPyS did not attenuate the response, suggesting that the G-protein or downstream effector systems were affected by receptor activation resulting in desensitization. The desensitization of receptor-stimulated PLD activation provides support for the phospholipase functioning in a key signalling pathway.

show abstract

The roles of multiple pathways in regulating bombesin-stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Cited by 26 publications

References 30 publications

Implication of Ca²⁺‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Implication of Ca²⁺‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Heterologous desensitization of bombesin‐ and vasopressin‐stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Contact Info

Product

Resources

About

The roles of multiple pathways in regulating bombesin-stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Cited by 26 publications

References 30 publications

Implication of Ca2+‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Implication of Ca2+‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Activation of phospholipase D by metabotropic glutamate receptor agonists in rat cerebrocortical synaptosomes

Heterologous desensitization of bombesin‐ and vasopressin‐stimulated phospholipase D activity in Swiss 3T3 fibroblasts

Contact Info

Product

Resources

About

Implication of Ca²⁺‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells

Implication of Ca²⁺‐Dependent Protein Tyrosine Phosphorylation in Carbachol‐Induced Phospholipase D Activation in Rat Pheochromocytoma PC12 Cells