Membrane Phospholipid Turnover, Receptor Function and Protein Phosphorylation

Takai, Yoshimi; Minakuchi, Ryoji; Kikkawa, Ushio; Sano, Kimihiko; Kaibuchi, Kozo; Yu, Binzu; Matsubara, Tsukasa; Nishizuka, Yasutomi

doi:10.1016/s0079-6123(08)63780-2

Cited by 56 publications

(42 citation statements)

References 46 publications

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“…cAMP has been shown to exert its biological action through activating cAMPdependent protein kinase (kinase-A) [57]. As shown previously, CAMP greatly enhances the cell communication capacity of cultured cells, which may be due to the activation of this kinase by cAMP and subsequent induction of de novo synthesis of gap junction proteins.…”

Section: Regulation Of Cell Communication and Cell Growthmentioning

confidence: 78%

“…Therefore, physiological factors that affect the activity of these receptors and kinases could modulate gap junctional communication. Interestingly, intracellular cAMP can inhibit diacylglycerolmediated activation of protein kinase C through blocking receptor-mediated synthesis of diacylglycerol [43,57]. On the other hand, phorbol esters inhibit an increase of CAMP by the stimulation of jS-adrenergic receptor [40].…”

Section: Regulation Of Cell Communication and Cell Growthmentioning

confidence: 99%

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Modulation of cell communication and carcinogenesis.

Kanno

1985

Jpn.J.Physiol

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In many types of tissue and culture cells, the interiors of adjacent cells communicate with each other through cell-to-cell channels. The fine structure of the cell-to-cell channel has been well studied and defined as a gap junction which consists of six identical, rod-shaped protein subunits [59]. This transmembrane channel permits free exchange of ions and small molecules between contacting cells [53]. This type of interaction between cells has been called "gap junctionalThis communication is readily proved by three different methods : electrophysiological, fluorescent dye transfer and metabolic cooperation methods [33].Cell communication has been thought to be regulated by the concentration of intracellular Ca2+ [45,46] and CAMP [17]. Calcium ion produces graded changes in cell communication [47]. cAMP modulates cell communication by stimulating the de novo synthesis of gap junctional protein [17].Since extensive reviews on the general properties of the gap junction and its physiological role have appeared in recent years [33,34], this short review will deal with a limited topic, namely, recent studies on the physiological role of gap junctional cell communication in the phenotypic manifestation of cancer. I. CELL COMMUNICATION IN CANCER CELLSInvestigation of cell communication in cancer cells was first made in rat liver tumors including primary, Morris and Novikoff hepatomas by electrophysiological methods [35]. Subsequently, similar studies were performed in transplanted rat and hamster thyroid tumors [24] and human stomach carcinoma [28]. These earlier studies showed a lack or a decrease of cell communication between contacting cancer cells, indicating the predominance of communication-incompetent cells in malignant tumors. A solid tumor, which was developed by transplantation of MH 134 cells into the subcutaneous space of C3H/He mice showed a decreased level of communication as revealed by electrical coupling. The decrease of cell communication appeared to correlate with the characteristics of metastasis in the case of MH 134 cells [23]. In benign tumors, such as human follicular adenoma, human diffuse toxic goiter and nontoxic nodular goiter, con-

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Section: Regulation Of Cell Communication and Cell Growthmentioning

confidence: 78%

Section: Regulation Of Cell Communication and Cell Growthmentioning

confidence: 99%

Modulation of cell communication and carcinogenesis.

Kanno

1985

Jpn.J.Physiol

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“…The present contribution wants to concentrate on the intracellular processes that influence renin release from juxtaglomerular cells. The available information will be discussed in front of the background of the present knowledge about the general mechanisms of secretion.For a variety of secretory cells including adrenal medulla and cortex, pituitary, exocrine and endocrine pancreas, neutrophils and platelets it has been found that the secretory process is triggered by the intracellular levels of calcium and cyclic nucleotides and further by the activity of protein kinase C [12,33,64,68,[70][71][72]. I shall therefore discuss in special the role of intracellular calcium, intracellular cyclic AMP and cyclic GMP and protein kinase C activity in the control of renin release from juxtaglomerular cells.…”

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confidence: 99%

Intracellular control of renin release — An overview

Kurtz

1986

Klin Wochenschr

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The renin angiotensin aldosterone system is an important regulator of the extracellular volume and of the control of blood pressure. It is mainly controlled in its activity by the rate of renin release from the kidney. Within the kidney renin is produced, stored and released from the so-called granular juxtaglomerular cells. These cells are modified smooth muscle cells and are found in the tunica media of the afferent arteriole, just adjacent to the glomerulus. They resemble morphologically vascular smooth muscle cells but have also characteristic features of secretory cells with respect to a welldeveloped endoplasmic reticulum, a prominent Golgi-apparatus and membrane bound granules containing renin [6,73].Since the rate of renin release from juxtaglomerular cells has a direct effect on blood pressure and because an enhanced rate of renin release is known to be a major reason of hypertension, the mechanisms controlling renal renin release have attracted considerable interest among physiologists, pharmacologists and clinicians.So far four basic mechanisms controlling renin release from the kidney have been described [26]. These comprise 1. The intra-renal blood pressure, which influences renin release by an as yet undefined baroreceptor.2. The amount of NaCl-load sensed by the macula densa segment of the distal tubule (macula densa sensor).3. The sympathetic nervous system 4. A large number of humoral factors like catecholamines, angiotensin II, vasopressin, atrial natriuretic peptide as well as metabolites as for example adenosine.In spite of the large body of findings about the modulation and alteration of renal renin release, the intracellular mechanisms by which renin release is controlled within the juxtaglomerular cells are not clearly understood.During the last years the mechanisms of physiological and pharmacological alterations of renin release have been reviewed [26, 36, 39]. The present contribution wants to concentrate on the intracellular processes that influence renin release from juxtaglomerular cells. The available information will be discussed in front of the background of the present knowledge about the general mechanisms of secretion.For a variety of secretory cells including adrenal medulla and cortex, pituitary, exocrine and endocrine pancreas, neutrophils and platelets it has been found that the secretory process is triggered by the intracellular levels of calcium and cyclic nucleotides and further by the activity of protein kinase C [12,33,64,68,[70][71][72]. I shall therefore discuss in special the role of intracellular calcium, intracellular cyclic AMP and cyclic GMP and protein kinase C activity in the control of renin release from juxtaglomerular cells. In this context I will also present our own results obtained from studies on the intracellular control of renin release from isolated juxtaglomerular cells. Role of Calcium in the Intracellular Control of Renin ReleaseThe typical secretory process in a large number of secreting cells has been found to be biphasic. The secretory process ...

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“…As diacylglycerol is readily converted to PA, an increase in PA is observed after platelet activation (9). IP3 and diacylglycerol, intermediates of PI turnover, induce intracellular Ca 2+ mobilization (10,11) and PKC activation (12), respectively. The intracellular Ca 2+ increase promotes the release of AA from platelet phospholipids through activation of PLA2 (13).…”

mentioning

confidence: 99%

“…On the contrary, negative signals such as PGI2 activate platelet adenylate cyclase and increase cyclic AMP content in the platelets. This increase in cyclic AMP inhibits the receptorlinked degradation of inositol phospholipids and the Ca 2+ mobilization, which result in activation of PLA2 and PKC during activation of platelets by the positive signals, and suppresses the cellular response of platelets (12,15).…”

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confidence: 99%

A new anti-platelet drug, E5510, has multiple suppressive sites during receptor-mediated signal transduction in human platelets.

et al. 1991

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ABSTRACT-The mode of action of E5510, 4-cyano-5,5-bis(4-methoxyphenyl)-4-pentenoic acid, which has very potent anti-platelet activities, was investigated by examining its effects on the biochemical responses in the process of human platelet activation. In a whole-cell system, E5510 inhibited the increased turnover of inositol phospholipids arising from phospholipase C activation, arachidonic acid release from phospholipids by phospholipase A2, mobilization of intracellular free Cat+, protein kinase C activation, and thromboxane A2 production. In a cell-free system, E5510 inhibited cyclooxygenase activity and cyclic AMP-dependent phosphodiesterase activity in a dose-dependent manner. An elevation of cyclic AMP in platelets was also observed at a relatively high concentration of E5510. It was suggested that receptor-mediated turnover of inositol phospholipids, intracellular Ca 2+ increase, arachidonic acid release from phospholipids and protein kinase C activation might be indirectly inhibited by the increased cyclic AMP level in platelets. Thromboxane A2 production in the whole-cell system was very strongly inhibited by E5510, and the IC50 for this effect was 100 times lower than that of direct inhibition of cyclooxygenase in the cell-free system. It was concluded that although the primary mode of action of E5510 is the inhibition of the cyclooxygenase pathway of positive signal transduction in platelets, E5510 has another mode of action by increasing platelet cyclic AMP, which can act as a negative messenger in platelet signal transduction, and these multiple sites of action synergistically antagonize platelet cellular activation.

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Membrane Phospholipid Turnover, Receptor Function and Protein Phosphorylation

Cited by 56 publications

References 46 publications

Modulation of cell communication and carcinogenesis.

Modulation of cell communication and carcinogenesis.

Intracellular control of renin release — An overview

A new anti-platelet drug, E5510, has multiple suppressive sites during receptor-mediated signal transduction in human platelets.

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