Activation of phospholipase C associated with isolated rabbit platelet membranes by guanosine 5′-[γ-thio]triphosphate and by thrombin in the presence of GTP

Hrbolich, Janet K.; Culty, Martine; Haslam, Richard J.

doi:10.1042/bj2430457

Cited by 48 publications

(20 citation statements)

References 61 publications

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“…The results reported here show that IP z , instead of IP, itself, stimulates the increase in cytoskeletal actin in saponin-permeated platelets. These findings seem to relate the accumulation ofIP z (Watson et al, 1984;Hrbolich et al, 1987;Ohta et al, 1985) during cell activation to the assembly of actin filaments (Carlsson et al, 1979;Jennings et al, 1981;Howard and Meyer, 1984), and suggest that IP 2 is the second messenger, just like IP, for Ca2+ release.…”

Section: Discussionmentioning

confidence: 95%

Increase in cytoskeletal actin induced by inositol 1,4‐bisphosphate in saponin‐permeated pig platelets

Huang

1994

Cell Biology International

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Inositol 1,4-bisphosphate (IP2) which rapidly accumulates during cell activation, strongly stimulates an increase in cytoskeletal actin in saponin-permeated platelets, and the effect is insensitive to 5'-Chloro-5'-deoxyadenosine. Within 10 s, the amount of cytoskeletal actin in platelets rapidly increases by 41%, and then slowly increases further. IP2 induces the increase in cytoskeletal actin in a dose-dependent manner. The half-maximal effect requires approximately 2 microM of IP2. Inositol 1,4,5- triphosphate, the messenger for Ca2+ release, causes the increase in cytoskeletal actin, but is less effective than IP2. Inositol 1-monophosphate and inositol 2-monophosphate have no effect on cytoskeletal actin. Phorbol 12-myristate 13-acetate, which has been shown to activate IP3 5'-phosphatase through protein kinase C, stimulates the increase in cytoskeletal actin. Spermine, an inhibitor of IP3 5'-phosphatase, inhibits the thrombin stimulated increase in cytoskeletal actin. These results suggest that IP2 may be a messenger that controls the organization of actin filaments during cell activation. This study presents the first evidence for IP2 as a messenger during cell activation.

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Section: Discussionmentioning

confidence: 95%

Increase in cytoskeletal actin induced by inositol 1,4‐bisphosphate in saponin‐permeated pig platelets

Huang

1994

Cell Biology International

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“…This should occur at a lower rate than PtdInsP2 hydrolysis, since PtdInsP2 content which results from the balance between its synthesis and degradation rates, never returned to control values over the period tested. Alternatively, one cannot exclude that PtdInsp is also attacked by phospolipase C, as reported for thrombin in platelet membranes [43].…”

Section: Discussionmentioning

confidence: 97%

Activation of the phosphatidylinositol metabolic pathway by low molecular weight B cell growth factor

et al. 1988

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The possible role of phosphatidylinositol breakdown in the induction of proliferation of human activated B cells by low molecular weight B cell growth factor (LMW-BCGF) was examined. LMW-BCGF was found to induce a rapid rise in the concentration of inositol trisphosphate (InsP3) in [3H]inositol-loaded B cell blasts, obtained by prior anti-mu antibody activation. A concomitant decrease in the concentration of phosphatidylinositol 4,5-bisphosphate could be detected at the same time. Maximum generation of InsP3 occurred within 15-30 s after the addition of the LMW-BCGF ligand to the activated B cells, then was followed by a slow decrease and return to control values. The amount of InsP3 generated by phosphatidylinositol hydrolysis was dependent on the concentration of LMW-BCGF. This effect was only detected in B cells already preactivated by a first signal such as anti-mu antibody and not in resting unstimulated B cells. In contrast, under similar conditions, interleukin 2, another B cell growth-promoting lymphokine, did not alter the rate of formation of the various phosphatidylinositol breakdown products. An augmentation of the [Ca2+]i concentration was also detected in activated B cells upon addition of LMW-BCGF and this increase could be blocked by TMB-8, a specific inhibitor of endoplasmic reticulum calcium release. Hydrolysis of phosphoinositides thus represents an essential component in the mechanism of transduction of the signal provided by LMW-BCGF.

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“…All of these studies in either permeable cells or isolated membranes could be interpreted to indicate that some of the IP and IP, produced in stimulated systems might be formed via the direct breakdown of PIP or PI. Likewise, investigators working with platelet membranes and permeabilized leukemia cells concluded that there was a substantial amount of direct agonist-mediated breakdown of PIP in their systems since the addition of excess unlabeled Ins(1,4,5)P3 or (2,3)diphosphoglycerate resulted in fairly small changes in the levels of labeled Ins(1,4,5)P3 and IP2 produced (Hrbolich et al, 1987;Ali et al, 1989).…”

Section: Discussionmentioning

confidence: 99%

Norepinephrine stimulates the direct breakdown of phosphatidyl inositol in rat tail artery

LaBelle

Trajković

1992

Journal Cellular Physiology

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When segments of rat tail artery were labeled with [3H]inositol and then stimulated with norepinephrine (NE), the inositol phosphates produced were primarily IP and IP2, together with a small but significant amount of Ins(1,4,5)P3 and a very small amount of Ins(1,3,4,5)P4. It has been unclear in many studies whether or not the relatively large levels of IP and IP2 produced in [3H]inositol-labeled tissue represent indirect products of phosphatidyl inositol(4,5)bis phosphate breakdown (through Ins(1,4,5)P3) or direct products of phosphatidyl inositol 4 monophosphate and phosphatidyl inositol breakdown. In order to answer this question tail artery segments were prelabeled with [3H]inositol and then permeabilized with beta escin and stimulated with norepinephrine and GTP gamma S, so that increases in IP, IP2, and Ins(1,4,5)P3 were still observed. If these permeable segments were stimulated with agonist in the presence of compounds known to inhibit Ins(1,4,5)P3 5-phosphatase, such as glucose 6P, (2,3)diphosphoglycerate, or Ins(1,4,5)P3, the levels of labeled Ins(1,4,5)P3 and labeled IP2 were increased, while the level of stimulated labeled IP was unchanged. This indicated that some of the IP2 and IP formed in these cells was produced from PIP2 but that some of these compounds might be formed from PIP or PI. When the isomers of inositol monophosphate, Ins 1P and Ins 4P, were separated by HPLC, it was shown that after prelabeled tail artery was stimulated by norepinephrine for periods of 1-2 min, the predominant isomer formed was Ins 4P, indicating either PIP2 or PIP as the source. However, after 5-20 min stimulation, both Ins 1P and Ins 4P were formed in equal amounts, suggesting that during sustained stimulation of smooth muscle PI itself was broken down directly. Therefore it appears that within 1-2 min of norepinephrine addition to vascular smooth muscle the bulk of the IP and IP2 produced are derived from PIP2 via IP3, while after 20 min of norepinephrine treatment much of the IP comes directly from PI. This suggests that the regulation of PLC in this tissue is more complicated than has been previously believed.

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Activation of phospholipase C associated with isolated rabbit platelet membranes by guanosine 5′-[γ-thio]triphosphate and by thrombin in the presence of GTP

Cited by 48 publications

References 61 publications

Increase in cytoskeletal actin induced by inositol 1,4‐bisphosphate in saponin‐permeated pig platelets

Increase in cytoskeletal actin induced by inositol 1,4‐bisphosphate in saponin‐permeated pig platelets

Activation of the phosphatidylinositol metabolic pathway by low molecular weight B cell growth factor

Norepinephrine stimulates the direct breakdown of phosphatidyl inositol in rat tail artery

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