Bombesin/GRP Stimulates a Protein Kinase in Swiss 3T3 Cells That Phosphorylates Microtubule-Associated Protein Kinase.

Miyasaka, Junko; Miyasaka, T.; Hayashi, Kyozo

doi:10.3164/jcbn.12.11

Cited by 21 publications

(29 citation statements)

References 29 publications

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“…MAPKs are key components of signaling pathways downstream of a variety of cell surface receptors including tyrosine kinase receptors, integrins, G proteincoupled receptors, and perhaps by as yet not identified shear stress receptors (Miyasaka et al, 1990;Duff et al, 1992;Karin, 1994;Schlaepfer et al, 1994;Morino et al, 1995;Zhu and Assoian, 1995;Arai and Escobedo, 1996;Jo et al, 1997). MAPKs phosphorylate and regulate key intracellular enzymes and transcription factors required for cell cycle progression and cell proliferation.…”

Section: Discussionmentioning

confidence: 99%

Integrin-mediated Signaling Events in Human Endothelial Cells

Short¹,

Talbott

Juliano³

1998

MBoC

154

112

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Vascular endothelial cells are important in a variety of physiological and pathophysiological processes. The growth and functions of vascular endothelial cells are regulated both by soluble mitogenic and differentiation factors and by interactions with the extracellular matrix; however, relatively little is known about the role of the matrix. In the present study, we investigate whether integrin-mediated anchorage to a substratum coated with the extracellular matrix protein fibronectin regulates growth factor signaling events in human endothelial cells. We show that cell adhesion to fibronectin and growth factor stimulation trigger distinct initial tyrosine phosphorylation events in endothelial cells. Thus, integrin-dependent adhesion of endothelial cells leads to tyrosine phosphorylation of both focal adhesion kinase and paxillin, but not of several growth factor receptors. Conversely, EGF stimulation causes receptor autophosphorylation, with no effect on focal adhesion kinase or paxillin tyrosine phosphorylation. Adhesion to fibronectin, in the absence of growth factors, leads to activation of MAPK. In addition, adhesion to fibronectin also potentiates growth factor signaling to MAPK. Thus, polypeptide growth factor activation of MAPK in anchored cells is far more effective than in cells maintained in suspension. Other agonists known to activate MAPK were also examined for their ability to activate MAPK in an anchorage-dependent manner. The neuropeptide bombesin, the bioactive lipid lysophosphatidic acid (LPA), and the cytokine tumor necrosis factor α, which signal through diverse mechanisms, were all able to activate MAPK to a much greater degree in fibronectin-adherent cells than in suspended cells. In addition, tumor necrosis factor α activation of c-Jun kinase (JNK) was also much more robust in anchored cells. Together, these data suggest a cooperation between integrins and soluble mitogens in efficient propagation of signals to downstream kinases. This cooperation may contribute to anchorage dependence of mitogenic cell cycle progression.

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Section: Discussionmentioning

confidence: 99%

Integrin-mediated Signaling Events in Human Endothelial Cells

Short¹,

Talbott

Juliano³

1998

MBoC

154

112

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“…Indeed, there is good evidence that trk, which is involved in high-affinity NGF binding, acts via a tyrosine kinase pathway (Kaplan et al, 199 1;Nebreda et al, 1991). Furthermore, it has been shown that NGF stimulates the tyrosine phosphorylation of several intracellular proteins including MAP2 kinase 199 l), which itself phosphorylates MAP2 (Landreth et al, 1990;Miyasaka et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

NGF induces neonatal rat sensory neurons to extend dendrites in culture after removal of satellite cells

1993

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Vertebrate sensory neurons have a pseudo-unipolar morphology; their somata are covered by satellite cells and lack dendrites or synaptic contacts. However, when neonatal rat sensory neurons from the nodose ganglia develop in culture in absence of satellite cells and with NGF, they form synapses among themselves. In this study, we investigated whether neonatal rat nodose neurons express dendrites under the same culture conditions. We show by Lucifer yellow injection that nodose neurons remain typically unipolar when cocultured with their ganglionic satellite cells. However, when these neurons are cultured without satellite cells, virtually all neurons acquire a multipolar morphology. Moreover, when NGF is added to satellite cell-free cultures, several neurons extend dendrites; these processes stain positively for microtubule-associated protein-2. NGF induces a 17-fold increase in dendritic outgrowth after 3 weeks but has little effect on axon number. In addition, we find that the ability of nodose neurons to extend dendrites is developmentally regulated. Furthermore, in a combined morphological and electrophysiological study, using whole-cell voltage- clamp technique with Lucifer yellow in the recording solution, we demonstrate a positive correlation between the extent of dendritic outgrowth and the density of ACh currents, suggesting that these dendrites have ACh receptors. Our results indicate that neonatal rat nodose neurons are capable of extending dendrites and that extrinsic factors can induce or suppress their extension. In addition, the results suggest that these dendrites may act as principal post-synaptic structures for synapse formation that occurs in these cultures.

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“…The MAP/MBP kinases also have been dubbed extracellular-regulated kinases (ERKs) because they are activated by signals, such as nerve growth factor, that result in differentiation, as well as by signals that result in proliferation (Ray and Sturgill, 1987;Shaw et al, 1988;Rossomando et al, 1989;Ahn et al, 1990;Gotoh et al, 1990b;Miyasaka et al, 1990a;Boulton et al, 1991). There are two well-characterized MAP/MBP kinases of Mr 42 000 and 44 000 that are activated by phosphorylation on threonine and tyrosine ) by a Mr 45 000 protein kinase related to the yeast protein kinases encoded by the byrl and STE7 genes .…”

Section: Introductionmentioning

confidence: 99%

Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

Wang

Erikson

1992

MBoC

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We have used myelin basic protein immobilized in sodium dodecyl sulfate-polyacrylamide gels to identify protein kinases after gel electrophoresis, followed by protein kinase reactions. This technique has permitted us to detect three protein kinases in serum-deprived cells transformed by p60src. On induction of cellular transformation by a temperature-sensitive v-src, a p87 protein kinase is activated within 30 min and remains activated in fully transformed cells. The p63 protein kinase is not fully activated until 24 h but remains activated in transformed cells. The commonly studied p42MBPK is rapidly activated within 30 min, and its kinase activity decreases significantly by 24 h, when the p63 enzyme is fully activated. The p42MBPK, as well as the p63 and p87 enzymes, are stimulated by transforming p60c-src mutants but not normal c-src or nonmyristylated p60c-src. In addition, the kinase activity of p63 enzyme, but not of p42MBPK, can be induced in okadaic acid-treated chicken embryo fibroblasts, indicating that phosphatase 2A and/or phosphatase 1 may be involved in the regulation of its activity. Additional data indicate that either p42MBPK or p63 activity correlates with the stimulation of the protein kinase p90RSK. Thus, there may be two independent pathways leading to the activation of the RSK gene product.

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Bombesin/GRP Stimulates a Protein Kinase in Swiss 3T3 Cells That Phosphorylates Microtubule-Associated Protein Kinase.

Cited by 21 publications

References 29 publications

Integrin-mediated Signaling Events in Human Endothelial Cells

Integrin-mediated Signaling Events in Human Endothelial Cells

NGF induces neonatal rat sensory neurons to extend dendrites in culture after removal of satellite cells

Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

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