Receptor-mediated regulation of calcium mobilization and cyclic GMP synthesis in neuroblastoma cells

Ohsako, Shunji; Deguchi, Takao

doi:10.1016/0006-291x(84)90479-0

Cited by 37 publications

(20 citation statements)

References 14 publications

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“…The Na+ channel protein has phosphorylation sites that could be affected by protein kinase A and protein kinase C, and several reports demonstrated modulation by these second messenger pathways (Catterall, 1992; see also Smith & Goldin, 1992). On the other hand, Ca2+, as an intracellular messenger, can cross-talk with phosphorylation or dephosphorylation pathways (Kennedy, 1989;Cohen, 1992;Yoshinori, Nakamura, Yoshida & Nishizuka, 1992 [CaS+L values used are within physiological range As discussed above, in our study, (Ohsako & Deguchi, 1984;Thayer &A Miller, 1990;Knbpfel & Gahwiler, 1992;Tatsumi & Katayama, 1993 …”

supporting

confidence: 62%

Functional availability of sodium channels modulated by cytosolic free Ca2+ in cultured mammalian neurons (N1E‐115).

Bulatko¹,

Greeff²

1995

The Journal of Physiology

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1. Whole-cell sodium currents (IN.) The excitation of nerve and muscle fibres is determined mainly by voltage-dependent Na+ channels. Therefore, the density of channels available for excitation may be critical for neuronal excitability, and so it was of interest to search for factors that modulate the functional availability of channels already inserted in the neuronal membrane. Several reports using heterologous expression of Na+ channels from rat brain have recently demonstrated such modulation by phosphorylation via protein kinase C or protein kinase A (see review by Catterall, 1992 (Sillen & Martell, 1964) as log Ka of 6'90 and logK'g of 1-69.

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supporting

confidence: 62%

Functional availability of sodium channels modulated by cytosolic free Ca2+ in cultured mammalian neurons (N1E‐115).

Bulatko¹,

Greeff²

1995

The Journal of Physiology

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“…Details of Ca ++ movement subsequent to binding have not been defined. Ohsako and Deguchi (1981) found that exogenous as well as endogenous phosphatidic acid stimulated Ca ++ influx in neuroblastoma and in cultured heart cells. Salmon and Honeyman (1980) proposed that increased phosphatidate may mediate the increased cellular Ca ++ levels produced by cholinergic stimulation and noted that phosphatidate at concentrations as low as 10~8 M produced contractions in isolated smooth muscle cells.…”

Section: Discussionmentioning

confidence: 95%

Phospholipase D produces increased contractile force in rabbit ventricular muscle.

Langer¹,

Rich²

1985

Circulation Research

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SUMMARY. Inclusion of phospholipase D (Streptomyces chromofuscus, 5 U/ml) in the medium perfusing rabbit papillary muscles increased peak force development by 78% and peak dF/dt by 89%. The maximal contractile response occurred 40-50 minutes after addition of the enzyme to the perfusate. As peak contractile response developed, aftercontractions appeared in most muscles. The inotropic response was slowly reversible, with disappearance of aftercontractions, upon discontinuation of the enzyme. Phospholipase D produces a specific increase of phosphatidic acid in the sarcolemma and, therefore, an increase in net anionic charge on the membrane. It has been shown previously that phospholipase D induces a large increase in sarcolemmal calcium binding. We propose, on the basis of the present study, that phospholipid-bound calcium may play a significant role in the control of contractile force in mammalian myocardium. (Circ Res 56: 146-149, 1985)

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“…At present, the mechanism by which physiologic stimuli mediate the activation of guanylate cyclase in intact cells is poorly understood. Although Ca2' is required for full expression of guanylate cyclase activity in cell-free systems (13), it is not known whether Ca2+ is the primary mediator of hormonal activation of guanylate cyclase in intact cells (14). In some cell types, hormonally induced increases in cyclic GMP can be blocked by agents that interfere with the release or metabolism of unsaturated fatty acids (15,16).…”

Section: Discussionmentioning

confidence: 99%

Induction of prostacyclin biosynthesis is closely associated with increased guanosine 3',5'-cyclic monophosphate accumulation in cultured human endothelium.

Brotherton¹

1986

J. Clin. Invest.

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Stimuli of prostacyclin (PGI2) biosynthesis such as thrombin, bradykinin, histamine, and A23187 increase guanosine 3',-cyclic monophosphate (cyclic GMP) levels in primary monolayer cultures of human umbilical vein endothelium by about twofold.This effect is dependent on the presence of extracellular Ca2".Increases of about tenfold are observed when cyclic GMP phosphodiesterase activity is inhibited, which suggests that the observed increases in cyclic GMP involve the activation of guanylate cyclase. Activation of guanylate cyclase appears to involve an early event in the induction of PGI2 biosynthesis, as neither arachidonic acid nor its metabolites stimulate cyclic GMP accumulation. Although activators of guanylate cyclase such as atriopeptin III, sodium nitroprusside, and tert-butylhydroperoxide increase cyclic GMP levels by -2-3-fold, they do not stimulate or modulate PGI2 production. We conclude that cyclic GMP does not play a primary role in mediating the induction or regulation of PGI2 biosynthesis in vascular endothelium.

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Receptor-mediated regulation of calcium mobilization and cyclic GMP synthesis in neuroblastoma cells

Cited by 37 publications

References 14 publications

Functional availability of sodium channels modulated by cytosolic free Ca2+ in cultured mammalian neurons (N1E‐115).

Functional availability of sodium channels modulated by cytosolic free Ca2+ in cultured mammalian neurons (N1E‐115).

Phospholipase D produces increased contractile force in rabbit ventricular muscle.

Induction of prostacyclin biosynthesis is closely associated with increased guanosine 3',5'-cyclic monophosphate accumulation in cultured human endothelium.

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