Agonist and membrane depolarization induced activation of MAP kinase in the swine carotid artery

Katoch, Surender S.; Moreland, Robert S.

doi:10.1152/ajpheart.1995.269.1.h222

Cited by 44 publications

(76 citation statements)

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“…Exposure of bovine tracheal smooth muscle to histamine signi®cantly increased the phosphorylation of both ERK isoenzymes in a PD 098059-sensitive manner, consistent with a causal role of the MKK-1/ERK pathway in Ca 2+ -independent contraction. These results con®rm previous studies where agonist exposure of canine trachealis (Gerthoffer et al, 1997), ferret aortas (Dessy et al, 1998) and bovine tracheal myocytes (Kelleher et al, 1995;Hershenson et al, 1995) is associated with ERK phosphorylation, which follows a time-course that correlates with smooth muscle contraction (Dessy et al, 1998;Katoch et al, 1995;Gerthoer et al, 1997). However, our data con¯ict with a study by Hershenson et al (1995) who reported that histamine had no eect on basal ERK activity and, in fact, opposed the activation of ERK evoked by 5-HT in bovine cultured tracheal myocytes by a mechanism that was blocked by the histamine H 2 -receptor antagonist, cimetidine.…”

Section: Histamine-induced Contractionsupporting

confidence: 90%

Extracellular signal‐regulated kinase 1/2 control Ca²⁺‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Koch

Nasuhara

Barnes

et al. 2000

British J Pharmacology

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1 The role of extracellular signal-regulated kinase (ERK)-1 and ERK-2 in controlling histamineinduced tone in bovine trachealis was investigated. PD 098059, an inhibitor of mitogen-activated protein kinase kinase (MKK)-1, had no eect on the histamine concentration-response relationship that described contraction. However, in the presence of EGTA, PD 098059 produced a parallel 5 fold rightwards shift of the histamine concentration-response curve without reducing the maximum response. The b 2 -adrenoceptor agonist, procaterol, also displaced the histamine-concentration response curve to the right but the eect was much greater than that evoked by PD 098059, noncompetitive and seen in the absence and presence of EGTA. 2 A low basal level of pERK-1 and pERK-2 was always detected in untreated trachealis, which was signi®cantly higher in EGTA-treated tissues and inhibited by PD 098059 and procaterol. Histamine markedly enhanced the phosphorylation of ERK-1 and ERK-2 by a mechanism that was also enhanced by EGTA and signi®cantly attenuated by procaterol and PD 098059. 3 Neither cholera toxin nor Sp-8-Br-cAMPS mimicked the ability of procaterol to dephosphorylate ERK. Similarly, neither pertussis toxin (PTX) nor Rp-8-Br-cAMPS, an inhibitor of cyclic AMPdependent protein kinase (PKA), aected basal pERK levels or antagonized the inhibitory eect of procaterol. 4 These data implicate the MKK-1/ERK signalling cascade in Ca 2+ -independent, histamineinduced contraction of bovine trachealis. In addition, the ability of procaterol to dephosphorylate ERK in an Rp-8-Br-cAMPS-and PTX-insensitive manner suggests that this may contribute to the anti-spasmogenic activity of b 2 -adrenoceptor agonists by activating a novel PKA-independent pathway.

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Section: Histamine-induced Contractionsupporting

confidence: 90%

Extracellular signal‐regulated kinase 1/2 control Ca²⁺‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Koch

Nasuhara

Barnes

et al. 2000

British J Pharmacology

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“…Our laboratory has previously shown that there is a linear relationship between MAP kinase dual phosphorylation and MAP kinase activity, so, hence forth, we will refer to MAP kinase phosphorylation as MAP kinase activity (20). Histamine is a classical and potent in vitro agonist of swine carotid arterial smooth muscle that stimulates receptor G protein-mediated mechanisms (59) and has been shown to be an activator of MAP kinase (1,25). As expected, histamine significantly increased p42/p44 MAP kinase activity above resting values (Fig.…”

Section: Resultsmentioning

confidence: 99%

Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle

Trappanese

Sivilich

Ets

et al. 2016

American Journal of Physiology-Cell Physiology

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Trappanese DM, Sivilich S, Ets HK, Kako F, Autieri MV, Moreland RS. Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle. Am J Physiol Cell Physiol 310: C921-C930, 2016. First published April 6, 2016; doi:10.1152/ajpcell.00311.2015.-Vascular smooth muscle contraction is primarily regulated by phosphorylation of myosin light chain. There are also modulatory pathways that control the final level of force development. We tested the hypothesis that protein kinase C (PKC) and mitogen-activated protein (MAP) kinase modulate vascular smooth muscle activity via effects on MAP kinase phosphatase-1 (MKP-1). Swine carotid arteries were mounted for isometric force recording and subjected to histamine stimulation in the presence and absence of inhibitors of PKC [bisindolylmaleimide-1 (Bis)], MAP kinase kinase (MEK) (U0126), and MKP-1 (sanguinarine) and flash frozen for measurement of MAP kinase, PKC-potentiated myosin phosphatase inhibitor 17 (CPI-17), and caldesmon phosphorylation levels. CPI-17 was phosphorylated in response to histamine and was inhibited in the presence of Bis. Caldesmon phosphorylation levels increased in response to histamine stimulation and were decreased in response to MEK inhibition but were not affected by the addition of Bis. Inhibition of PKC significantly increased p42 MAP kinase, but not p44 MAP kinase. Inhibition of MEK with U0126 inhibited both p42 and p44 MAP kinase activity. Inhibition of MKP-1 with sanguinarine blocked the Bis-dependent increase of MAP kinase activity. Sanguinarine alone increased MAP kinase activity due to its effects on MKP-1. Sanguinarine increased MKP-1 phosphorylation, which was inhibited by inhibition of MAP kinase. This suggests that MAP kinase has a negative feedback role in inhibiting MKP-1 activity. Therefore, PKC catalyzes MKP-1 phosphorylation, which is reversed by MAP kinase. Thus the fine tuning of vascular contraction is due to the concerted effort of PKC, MAP kinase, and MKP-1.bisindolylmaleimide-1; U0126; sanguinarine; caldesmon; CPI-17; phos-tag gel electrophoresis EXTRACELLULAR SIGNAL-REGULATED kinase 1/2 mitogen-activated protein kinase (MAP kinase; also known as p42/p44 MAP kinase) is a serine/threonine protein kinase that has been identified in several types of smooth muscle (7,10,19). MAP kinase is activated via dual phosphorylation of Thr 187 and Tyr 185 catalyzed by MAP kinase kinase (MEK) and has been shown to play a significant role in activating several proteins required for cell growth in proliferating dedifferentiated smooth muscle cells (24,26). However, the role of MAP kinase in differentiated, contractile smooth muscle cells is not as well understood.In differentiated smooth muscle, it has been suggested that MAP kinase may be involved in calcium-independent regulation of smooth muscle contraction (17). MAP kinase has been shown to phosphorylate the thin filament protein caldesmon and relieve its inhibitory action on the actin-activated myosin ATPase, ...

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“…Activation of the MAP kinase pathway, and especially the ERK pathway, is necessary for protooncogene expression (including c-fos) and cell proliferation. studies have been performed on fully contractile smooth muscle cells, and those studies that have been done, a role for the MAP kinases in regulating contractile behavior has been suggested (32)(33)(34)(35). Therefore, it was of great interest to us to examine the role of PKG on MAP kinase activity in RASMC whose contractile phenotype had been restored.…”

Section: Discussionmentioning

confidence: 99%

“…Additionally, it has been demonstrated that ERK1 and -2 are partially activated in fully differentiated contractile smooth muscle by contractile agonists (29,(32)(33)(34). Several reports suggest that ERK activation may be involved in regulating contraction of differentiated smooth muscle (35), but others have found only small effects of ERK activation on contraction (34).…”

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confidence: 99%

Activation of Mitogen-activated Protein Kinase Pathways by Cyclic GMP and Cyclic GMP-dependent Protein Kinase in Contractile Vascular Smooth Muscle Cells

Komalavilas

Shah

et al. 1999

Journal of Biological Chemistry

136

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Vascular smooth muscle cells (VSMC) exist in either a contractile or a synthetic phenotype in vitro and in vivo.The molecular mechanisms regulating phenotypic modulation are unknown. Previous studies have suggested that the serine/threonine protein kinase mediator of nitric oxide (NO) and cyclic GMP (cGMP) signaling, the cGMP-dependent protein kinase (PKG) promotes modulation to the contractile phenotype in cultured rat aortic smooth muscle cells (RASMC). Because of the potential importance of the mitogen-activated protein kinase (MAP kinase) pathways in VSMC proliferation and phenotypic modulation, the effects of PKG expression in PKG-deficient and PKG-expressing adult RASMC on MAP kinases were examined. In PKG-expressing adult RASMC, 8-para-chlorophenylthio-cGMP activated extracellular signal-regulated kinases (ERK1/2) and c-Jun N-terminal kinase (JNK). The major effect of PKG activation was increased activation by MAP kinase kinase (MEK). The cAMP analog, 8-Br-cAMP inhibited ERK1/2 activation in PKG-deficient and PKG-expressing RASMC but had no effect on JNK activity. The effects of PKG on ERK and JNK activity were additive with those of platelet-derived growth factor (PDGF), suggesting that PKG activates MEK through a pathway not used by PDGF. The stimulatory effects of cGMP on ERK and JNK activation were also observed in low-passaged, contractile RASMC still expressing endogenous PKG, suggesting that the effects of PKG expression were not artifacts of cell transfections. These results suggest that in contractile adult RASMC, NO-cGMP signaling increases MAP kinase activity. Increased activation of these MAP kinase pathways may be one mechanism by which cGMP and PKG activation mediate c-fos induction and increased proliferation of contractile adult RASMC. Vascular smooth muscle cell (VSMC)1 proliferation and migration are associated with several vascular diseases such as atherosclerosis and restenosis following vascular injury (1-5). VSMC from several species when cultured in vitro undergo a change in phenotype from a contractile state to a synthetic state similar to the changes that occur with VSMC in vivo in response to vascular injury (6 -8). Several lines of evidence suggest that nitric oxide (NO) inhibits VSMC proliferation (9 -13), suggesting that signal transduction pathways regulated by NO may be important in VSMC phenotypic modulation. NO stimulates the production of cyclic GMP (14), which, in turn, regulates several functions of VSMC such as smooth muscle relaxation (15). The major receptor protein for cGMP in VSMC is cGMP-dependent protein kinase (PKG), a serine/ threonine kinase that catalyzes the phosphorylation of important proteins that regulate intracellular Ca 2ϩ levels and relaxation of vascular smooth muscle (16). Our laboratory has recently demonstrated that PKG also plays a major role in the regulation of the phenotype and morphology of VSMC (17, 18).The expression of PKG is highly variable in VSMC. When adult rat aortic SMC are subcultured in vitro, PKG expression is reduced to nearly un...

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Agonist and membrane depolarization induced activation of MAP kinase in the swine carotid artery

Cited by 44 publications

References 0 publications

Extracellular signal‐regulated kinase 1/2 control Ca²⁺‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Extracellular signal‐regulated kinase 1/2 control Ca²⁺‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle

Activation of Mitogen-activated Protein Kinase Pathways by Cyclic GMP and Cyclic GMP-dependent Protein Kinase in Contractile Vascular Smooth Muscle Cells

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Agonist and membrane depolarization induced activation of MAP kinase in the swine carotid artery

Cited by 44 publications

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Extracellular signal‐regulated kinase 1/2 control Ca2+‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Extracellular signal‐regulated kinase 1/2 control Ca2+‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Regulation of mitogen-activated protein kinase by protein kinase C and mitogen-activated protein kinase phosphatase-1 in vascular smooth muscle

Activation of Mitogen-activated Protein Kinase Pathways by Cyclic GMP and Cyclic GMP-dependent Protein Kinase in Contractile Vascular Smooth Muscle Cells

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Extracellular signal‐regulated kinase 1/2 control Ca²⁺‐independent force development in histamine‐stimulated bovine tracheal smooth muscle

Extracellular signal‐regulated kinase 1/2 control Ca²⁺‐independent force development in histamine‐stimulated bovine tracheal smooth muscle