Pathway of phospholipase C activation initiated with platelet-derived growth factor is different from that initiated with vasopressin and bombesin.

Hasegawa-Sasaki, Hiroko; Lutz, F.; Sasaki, Terukatsu

doi:10.1016/s0021-9258(18)37658-0

Cited by 76 publications

(2 citation statements)

References 57 publications

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“…However, the inositol phosphate species formed in response to P. multocida toxin and bombesin are remarkably similar (Staddon et al ., 1991) . The bombesin receptor is believed to couple to phospholipase C via a pertussis toxin-insensitive and yet to be identified G protein (Zachary et al ., 1987;Erusalimsky et al ., 1988;Fisher and Schonbrunn, 1988 ;Hasegawa-Sasaki et al ., 1988 ;Cattaneo and Vicentini, 1989;Coffer et al ., 1990 ;Sinnett-Smith et al, 1990;Plevin et al ., 1990;Battey et al ., 1991) . Recently, a likely candidate The Journal of Cell Biology, Volume 115, 1991 for this G protein has been identified as Gq (Shenker et al ., 1991 ;Smrcka et al, 1991 ;Taylor et al, 1991) .…”

Section: Irreversibility Of Toxin Actionmentioning

confidence: 99%

A novel approach to detect toxin-catalyzed ADP-ribosylation in intact cells: its use to study the action of Pasteurella multocida toxin.

Staddon

Bouzyk

1991

The Journal of Cell Biology

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Abstract. Certain microbial toxins are ADP-ribosyltransferases, acting on specific substrate proteins. Although these toxins have been of great utility in studies of cellular regulatory processes, a simple procedure to directly study toxin-catalyzed ADPribosylation in intact cells has not been described . Our approach was to use [2?H]adenine to metabolically label the cellular NAD+ pool. Labeled proteins were then denatured with SDS, resolved by PAGE, and detected by fluorography. In this manner, we show that pertussis toxin, after a dose-dependent lag period, [3H]-labeled a 40-kD protein in intact cells. Furthermore, incubation of the gel with trichloroacetic acid at 95°C before fluorography caused the release of label from bands other than the pertussis toxin substrate, thus, allowing its selective visualization . The modification of the 40-kD protein was ascribed to ADP-ribosylation of a T HE pathological basis of the action of certain bacteria is accounted for by their ability to produce toxins that enter eukaryotic cells and subvert cellular regulatory processes. Some ofthese toxins catalyze the transfer of ADP-ribose from NAD+ to specific target proteins, resulting in a protein that may be either inactive or altered in properties. Diphtheria toxin and Pseudomonas aeruginosa exotoxin A block protein synthesis by ADP-ribosylatiog elongation factor-2 (Collier, 1990;Wick and Iglewski, 1990). Clostridium botulinum C2 toxin ADP-ribosylates nonmuscle actin ) and the C3 toxin ADP-ribosylates rho, a ras-related GTPase (Aktories and Just, 1990) . P. aeruginosa exoenzyme S preferentially ADP-ribosylates p21a-"-s in vitro (Coburn et al., 1989b) and has also been described to ADP-ribosylate vimentin (Coburn et al ., 1989a). Pertussis toxin, cholera toxin, and Escherichia coli heat-labile enterotoxin ADP-ribosylate the a subunits of heterotrimeric signal transducing G proteins (Moss and Vaughan, 1988 ;Pfeuffer and Helmreich, 1988;Ui, 1990). The specificity of the action of these toxins and the modification of target protein function can be exploited to make them extremely useful as probes of cellular regulatory processes .The classic approach to investigate the role of ADPribosylation in toxin action has been to identify ADPribosylated toxin substrates in cell extracts using radiola- Pasteurella multocida toxin has recently been described as a novel and potent mitogen for Swiss 3T3 cell and acts to stimulate the phospholipase C-mediated hydrolysis of polyphosphoinositides . The basis of the action of the toxin is not known. Using the methodology described here, P. multocida toxin was not found to act by ADP-ribosylation . beled NAD+ . This requires activation of the holotoxin in vitro and its use at concentration orders ofmagnitude greater than those used on intact cells . Furthermore, this approach can be thwarted by the absence of ADP-ribosylation factors and excessive NADase activity in the cell extracts. It can also be sensitive to the composition of the reaction mixture (see, e.g., Ribeiro-Neto et al., 1985, andWoo...

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Section: Irreversibility Of Toxin Actionmentioning

confidence: 99%

A novel approach to detect toxin-catalyzed ADP-ribosylation in intact cells: its use to study the action of Pasteurella multocida toxin.

Staddon

Bouzyk

1991

The Journal of Cell Biology

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“…Certain receptor tyrosine kinases, e.g. those for platelet-derived and epidermal growth factors, activate PIC (probably PICY1; Wahl et al, 1989) without the involvement of G-proteins (Hasegawa-Sasaki et al, 1988). The mechanism of this action is not yet clear, although phosphorylation of PICY, either directly or indirectly by the receptor tyrosine kinase, is likely to underlie its activation (see Martin, 1991).…”

Section: Introductionmentioning

confidence: 99%

Heparin and other polyanions uncouple α1-adrenoceptors from G-proteins

Dassò

Taylor

1991

Biochemical Journal

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Several polyanionic compounds antagonize the interaction between receptors and the G-proteins that regulate adenylate cyclase or K+ channels, possibly by binding to a basic stretch of the receptor that is proposed to mediate its interaction with the G-proteins. We have studied the effects of polyanions on the interaction between the liver alpha 1-adrenoceptor and the G-protein through which it stimulates polyphosphoinositide turnover. Heparin [concn. causing 50% of maximal effect (EC50) = 0.5 microM], Trypan Blue (EC50 7.1 microM) or suramin (EC50 2.1 microM) prevented formation of the high-affinity adrenaline-receptor-G-protein complex without affecting antagonist binding. After alkaline treatment of the membranes, previously reported to cause G-protein removal, binding of agonists was insensitive to both guanine nucleotides and heparin. We conclude that these polyanions uncouple the alpha 1-adrenoceptor from its G-protein, suggesting that similar coupling mechanisms may underlie receptor activation of the G-proteins that activate polyphosphoinositide hydrolysis and those that regulate adenylate cyclase. This action of heparin severely limits its utility as a selective antagonist of the Ins(1,4,5)P3 receptor in intact cells.

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Phospholipid‐Derived Second Messengers

Exton

1998

Comprehensive Physiology

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The sections in this article are: Inositol Phospholipid Hydrolysis Functional Significance Phosphoinositide Phospholipases as Targets of Hormones and Growth Factors Phosphatidylinositol 3,4,5‐Trisphosphate Synthesis Phosphatidylinositol 3‐Kinases as Targets of Hormones and Growth Factors Role of Phosphatidylinositol 3‐Kinase in Cell Function Phosphatidylcholine Hydrolysis Phosphatidylcholine Hydrolysis by Phospholipase D and Its Functional Significance Phospholipase D as a Target of Hormones and Growth Factors Agonist‐Stimulated Phosphatidylcholine Hydrolysis by Phospholipase C Agonist‐Stimulated Phosphatidylcholine Hydrolysis by Phospholipase A 2 Sphingomyelin Hydrolysis and Its Functional Significance Summary

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Pathway of phospholipase C activation initiated with platelet-derived growth factor is different from that initiated with vasopressin and bombesin.

Cited by 76 publications

References 57 publications

A novel approach to detect toxin-catalyzed ADP-ribosylation in intact cells: its use to study the action of Pasteurella multocida toxin.

A novel approach to detect toxin-catalyzed ADP-ribosylation in intact cells: its use to study the action of Pasteurella multocida toxin.

Heparin and other polyanions uncouple α1-adrenoceptors from G-proteins

Phospholipid‐Derived Second Messengers

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