Cell cycle-dependent inhibition of human vascular smooth muscle cell proliferation by prostaglandin E1

Loesberg, C.; Wijk, R. Van; Zandbergen, J.; Aken, W.G. van; Mourik, Jan A. van; Groot, P. G. De

doi:10.1016/0014-4827(85)90241-1

Cited by 119 publications

(39 citation statements)

References 23 publications

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“…This result is consistent with cGMP-elevating vasodilators exerting their anti-proliferative action by inhibiting progression from the G1-to the S-phase of the cell cycle [15,21,32]. Our results are also consistent with previous work [7,11,32] showing that elevated cGMP concentrations at a latter stage of the G1-phase of the cell cycle would be necessary to inhibit proliferation. Figure 7 InhIbfflon of VSMC growth by YC-1…”

Section: Concnsupporting

confidence: 92%

“…Theoretically, a selective inhibitor of VSMC proliferation is therefore required [5]. Several agents that suppress VSMC proliferation have already been identified: prostaglandins E1, E2 [6,7], heparin [8], interferon a [9], f-transforming growth factor [10] and protein kinase C activator [11]. However, no significant inhibition of atherosclerosis or restenosis has been achieved with the above agents [5].…”

Section: Introductionmentioning

confidence: 99%

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Mechanism of anti-proliferation caused by YC-1, an indazole derivative, in cultured rat A10 vascular smooth-muscle cells

YU¹,

CHENG²,

GUH³

et al. 1997

Biochemical Journal

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An indazole derivative, YC-1, was identified in this study to be capable of reversibly and effectively inhibiting proliferation of rat AIO vascular smooth-muscle cells (VSMCs) in vitro. YC-1 (1-100 1uM) dose-dependently inhibited [3H]thymidine incorporation into DNA in rat AlO VSMCs that were synchronized by serum depletion and then restimulated by addition of 10 % foetal calf serum (FCS), whereas FCS-induced [3H]thymidine incorporation into rat synchronized endothelial cells was unaffected by this agent. The dose of YC-1 required to cause inhibition of FCS-induced proliferation was similar to that necessary for the formation of cellular cyclic GMP (cGMP). Guanylate cyclase activity in soluble fractions of VSMCs was activated by (1-100 ,uM), whereas cGMP-specific phosphodiesterase activity was unaffected by this compound. The anti-proliferative effect of YC-1 was mimicked by 8-bromo-cGMP, a membrane-permeable cGMP analogue, and was antagonized by KT 5823 (0.2,M), a selective inhibitor of protein kinase G. The anti-proliferative

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Section: Concnsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Mechanism of anti-proliferation caused by YC-1, an indazole derivative, in cultured rat A10 vascular smooth-muscle cells

YU¹,

CHENG²,

GUH³

et al. 1997

Biochemical Journal

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“…In thyroid cells, cAMP is mitogenic without an apparent activation of MAPK (40). In SMCs, increased cAMP inhibits PDGF-stimulated DNA synthesis and cell proliferation (37,41,42). However, inhibition of DNA synthesis by forskolin cannot be attributed solely to antagonism of the initial MAPK signaling, since DNA synthesis was blocked when forskolin was added 1-6 hr after PDGF-BB (data not shown).…”

Section: Discussionmentioning

confidence: 94%

Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells.

Graves

Bornfeldt

Raines

et al. 1993

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

442

289

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Stimulation ofaortic smooth muscle cells with platelet-derived growth factor BB homodimer (PDGF-BB) leads to the rapid activation ofmitogen-activated protein kinase (MAPK) and MAPK kinase (MAPKK). Compounds that increase cAMP and activate protein kinase A (PKA) prostaglandin E2, isoproterenol, cholera toxin, and forskolinwere found to inhibit the PDGF-BB-induced activation of MAPKK and MAPK. Forskolin, but not the inactive analogue 1,9-dideoxyforskolin, inhibited PDGF-BB-stimulated MAPKK and MAPK activation in a dose-dependent manner. PKA antagonism of MAPK signaling was observed at all doses of PDGF-BB or PDGF-AA. PKA did not inhibit MAPKK and MAPK activity in vitro, and MAPKK and MAPK from extracts of forskolin-treated cells could be activated normally with purified Raf-1 and MAPKK, respectively, suggesting that PKA blocked signaling upstrea of MAPKK. Neither PDGF-BBstimulated tyrosine autophosphorylation of the PDGF receptor (3 subunit nor inositol monophosphate accumulation was affected by increased PKA activity, suggesting that PKA inhibits events downstream of the PDGF receptor. This study provides an example of cross talk between two important signaling systems activated by physiological stimuli in smooth muscle cells-namely, the PKA pathway and the growth factoractivated MAPK cascade.The p44 and p42 mitogen-activated protein kinases (MAPKs) (Erkl and Erk2) are central components of a growth factorstimulated protein kinase cascade found in organisms as diverse as mammals and yeast (reviewed in refs.

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“…We have shown recently that PDGF-induced MAPK activation is associated with phosphorylation, and activation of cPLA 2 with the subsequent release of PGE 2 (and most likely other inhibitory prostaglandins, such as PGE 1 and PGI 2 ) in some strains of arterial SMC (24). PGE 2 is a strong activator of PKA, a wellknown inhibitor of SMC proliferation, through binding to its adenylate cyclase-coupled receptors (26)(27)(28)(29)(30). The results presented here show that the effects of PDGF on cPLA 2 , PGE 2 (and other PKA-activating PGs) release, and PKA activation can be blocked by the MAPKK inhibitor PD 098059, verifying that these events are mediated by the MAPK cascade in SMCs (see Fig.…”

Section: Discussionmentioning

confidence: 99%

The mitogen-activated protein kinase pathway can mediate growth inhibition and proliferation in smooth muscle cells. Dependence on the availability of downstream targets.

Bornfeldt¹,

Campbell²,

Koyama³

et al. 1997

J. Clin. Invest.

148

108

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Cell cycle-dependent inhibition of human vascular smooth muscle cell proliferation by prostaglandin E1

Cited by 119 publications

References 23 publications

Mechanism of anti-proliferation caused by YC-1, an indazole derivative, in cultured rat A10 vascular smooth-muscle cells

Mechanism of anti-proliferation caused by YC-1, an indazole derivative, in cultured rat A10 vascular smooth-muscle cells

Protein kinase A antagonizes platelet-derived growth factor-induced signaling by mitogen-activated protein kinase in human arterial smooth muscle cells.

The mitogen-activated protein kinase pathway can mediate growth inhibition and proliferation in smooth muscle cells. Dependence on the availability of downstream targets.

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