Ionic responses rapidly elicited by activation of protein kinase C in quiescent Swiss 3T3 cells.

Vara, F; Schneider, Jerry A.

doi:10.1073/pnas.82.8.2384

Cited by 88 publications

(43 citation statements)

References 43 publications

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“…Thus, it is possible that activation of protein kinase C has a similar effect on inhibiting the apical Na conductance of both A6 epithelia and the rabbit CCT. There is precedence for phorbol esters to affect both apical sodium conductance (8,31) and Na-K ATPase turnover (29,34,35,44). Both would result in a decrease in Na' absorption and K+ secretion as seen in our studies.…”

Section: Discussionsupporting

confidence: 53%

“…The activation of protein kinase C and its subsequent effects on cells have been investigated utilizing phorbol esters and diacylglycerols (1,2). Activation of protein kinase C has been shown to alter the transport of Na (8,(27)(28)(29)(30)(31)(32)(33)(34)(35), K (36-38), Cl (24)(25)(26)(27), HCO3 (24,25), and water (7) in different transporting epithelia. Several hormones, neurotransmitters, and growth factors induce PI turnover and thus activation ofprotein kinase C (1, 2).…”

Section: Discussionmentioning

confidence: 99%

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Effects of protein kinase C activation on sodium, potassium, chloride, and total CO2 transport in the rabbit cortical collecting tubule.

Hays¹,

Baum

Kokko³

1987

J. Clin. Invest.

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Several hormones induce phosphatidylinositol turnover in cell membranes and thus activate protein kinase C. Activation of protein kinase C can, in turn, have effects on epithelial transport. These experiments were designed to investigate the effects of two activators of protein kinase C, phorbol 12-myristate,13-acetate (PMA) and L-a-1,2-dioctanoylglycerol (L-a-1,2-DOG), and two inactive analogues, 4a-phorbol and 4-0-methyl phorbol 12-myristate,13-acetate, on sodium, potassium, chloride, and total CO2 transport in the rabbit cortical collecting tubule.Utilizing in vitro microperfusion techniques, we found that activation of protein kinase C with either PMA or L-a-1,2-DOG significantly inhibited net sodium absorption, net potassium secretion and transepithelial voltage in a dose-dependent manner. There was no effect on net chloride or total CO2 transport. In contrast, the inactive phorbol analogues did not alter either sodium or potassium transport.These studies demonstrate that in the rabbit cortical collecting tubule sodium and potassium transport can be inhibited by compounds known to activate protein kinase C. Thus, hormones that induce phosphatidylinositol turnover in the rabbit cortical collecting tubule may lead to inhibition of sodium transport by activation of protein kinase C.

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Section: Discussionsupporting

confidence: 53%

Section: Discussionmentioning

confidence: 99%

Effects of protein kinase C activation on sodium, potassium, chloride, and total CO2 transport in the rabbit cortical collecting tubule.

Hays¹,

Baum

Kokko³

1987

J. Clin. Invest.

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“…Well known targets of protein kinase C are an 80-kDa protein of unknown function (26), the epidermal growth factor receptor (27,28), and the Na+/H+ pump-either directly or indirectly (29)(30)(31)(32) (24,34), none of the aforementioned "classic" responses to protein kinase C activation has been observed (35). Nevertheless, interferon-dependent protein kinase activities have been noted with mouse 3T3-F442A and 3T3-C2 fibroblasts.…”

Section: Resultsmentioning

confidence: 99%

Angiogenin activates endothelial cell phospholipase C.

Bicknell

Vallée

1988

Proc. Natl. Acad. Sci. U.S.A.

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Low concentrations of angiogenin activate the inositol-specific phospholipase C of cultured pulmonary artery, umbilical vein, and capillary endothelial cells, promoting a transient increase in the intracellular levels of 1,2-diacylglycerol and inositol trisphosphate. The response is strongly dose dependent with a maximum in the ng/ml concentration range and, for some cell lines, a marked decrease at concentrations >1 ng/ml; e.g., arterial endothelial cells respond weakly to angiogenin concentrations comparable to that in normal human plasma (-400 ng/ml). Chemical modification of the active site of angiogenin or inhibition with placental ribonuclease inhibitor abolishes its activation of endothelial cell phospholipase C; this correlates with the concomitant loss of both intrinsic ribonucleolytic and angiogenic activity. The response to low concentrations of angiogenin is consistent with its potency of inducing vascularization in classical angiogenesis assays. In vivo, endothelial cells are exposed to concentrations of angiogenin higher than that required to elicit a cellular response; it seems likely, therefore, that expression of a surface receptor or some other process must be rate limiting in the cellular response.Angiogenin, secreted by HT-29 human colon adenocarcinoma cells (1), is a potent inducer of vascular development in the chicken chorioallantoic membrane (1, 2). The primary structure of this 14-kDa protein exhibits significant sequence homology to pancreatic ribonuclease (3). Moreover, it has intrinsic ribonucleolytic activity distinct from that of "'classic" ribonucleases (4). Angiogenin is a very effective inhibitor of cell-free protein synthesis in the rabbit reticulocyte lysate. Inhibition is a direct result of specific angiogenin cleavage of ribosomal RNA and consequent inactivation of the protein synthesis machinery (5). To date there is no evidence that angiogenin either inhibits protein synthesis in vivo or enters undamaged cells; hence, the physiological significance of these findings remains to be clarified.Several other structurally characterized proteins-notably, tumor necrosis factor, transforming growth factors a and ,3, epidermal growth factor, as well as acidic and basic fibroblast growth factor-initially identified on the basis of other biological activities, have also been shown to be angiogenic (6-8). All of these proteins have been the subject of extensive cell biological research and the details of their interactions with various cell types have been carefully documented. In contrast, little is known about the interaction of angiogenin with cells, including the specificity of this interaction, the nature of the cellular response, how this relates to the ribonucleolytic activity of angiogenin, and how this ultimately leads to vascularization. In particular, it was not known whether angiogenin interacts directly or indirectly with the capillary endothelium. The results presented here demonstrate that angiogenin activates endothelial cell phospholipase C at concentrations wel...

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“…The alterations of cell shape, like many other effects of PMA, are spontaneously reversed after prolonged incubation. Possibly, this reversion is due to the down-regulation of the main cellular target of PMA, protein kinase C (14).…”

Section: Discussionmentioning

confidence: 99%

Special type of morphological reorganization induced by phorbol ester: reversible partition of cell into motile and stable domains.

Dugina¹,

Svitkina²,

Vasiliev³

et al. 1987

Proc. Natl. Acad. Sci. U.S.A.

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The phorbol ester phorbol 12-myristate 13-acetate (PMA) induced reversible alteration of the shape of fibroblastic cells of certain transformed lines-namely, partition of the cells into two types of domains: motile body actively extending large lamellas and stable narrow cytoplasmic processes. Dynamic observations have shown that stable processes are formed from partially retracted lamellas and from contracted tail parts of cell bodies. Immunofluorescence microscopy and electron microscopy of platinum replicas of cytoskeleton have shown that PMA-induced narrow processes are rich in microtubules and intermediate filaments but relatively poor in actin microfilaments; in contrast, lamellas and cell bodies contained numerous microfilaments. Colcemid-induced depolymerization of microtubules led to contraction of PMAinduced processes; cytochalasin B prevented this contraction. It is suggested that PMA-induced separation of cell into motile and stable parts is due to directional movement of actin structures along the microtubular framework. Similar movements may play an important role in various normal morphogenetic processes.Reversible morphological reorganizations of fibroblasts and other cultured cells are actively studied as prototypes of normal morphogenetic processes; alterations of cytoskeleton regulated by the membrane-generated signals seem to play central roles in these reorganizations (for reviews, see refs. 1-3). In this paper we describe a special type of reversible alteration of cell shape and cytoskeleton induced in certain fibroblastic lines by the tumor promoter phorbol 12-myristate 13-acetate (PMA). This agent caused reversible cell partition into a motile pseudopod-forming body and nonmotile elongated processes rich in microtubules and intermediate filaments. Analysis of this reorganization suggests that alterations of interactions between the actin cortex and microtubules are of key importance in its development. It is possible that reorganizations of a similar type are involved in normal morphogenetic processes-e.g., in the formation of neurites by neural cells, in forward translocation of polarized fibroblasts, etc. MATERIALS AND METHODSSeveral types of cultured fibroblastic cells were used: secondary cultures of mouse embryo fibroblasts, minimally transformed mouse BALB/3T3 line, rat NRK (normal rat kidney) line, transformed PS-103 and PS-104 lines obtained in this laboratory from mouse sarcomas induced by implanted plastic films, and cloned subline 152/15 of the spontaneously transformed CAK-7 line of mouse fibroblasts (4). The cells were grown at 37°C in Eagle's medium with 10% fetal calf serum. The cells were seeded on the coverslips placed into Petri dishes at a concentration of 104 cells per ml. The experiments were started at 48 hr after seeding.Colcemid, PMA, and its analogues were from Serva (Heidelberg), and cytochalasin B was from Aldrich. Rhodamine-labeled phalloidin was a gift of T. Wieland (Max Planck Institute for Medical Research, Heidelberg). Polyclonal antibodies to tubul...

show abstract

Ionic responses rapidly elicited by activation of protein kinase C in quiescent Swiss 3T3 cells.

Cited by 88 publications

References 43 publications

Effects of protein kinase C activation on sodium, potassium, chloride, and total CO2 transport in the rabbit cortical collecting tubule.

Effects of protein kinase C activation on sodium, potassium, chloride, and total CO2 transport in the rabbit cortical collecting tubule.

Angiogenin activates endothelial cell phospholipase C.

Special type of morphological reorganization induced by phorbol ester: reversible partition of cell into motile and stable domains.

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