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Article: Post-translational mechanisms of endothelial nitric oxide synthase regulation by bradykinin.

Venema, Richard C

2002 Volume 2, Issue 13-14, Page(s) 1755–1762

Abstract: The endothelial nitric oxide synthase (eNOS) plays a key role in blood pressure regulation and vascular homeostasis. Among the more potent inducers of eNOS activity in vascular endothelial cells is bradykinin (BK). This brief review summarizes the ... ...

Abstract	The endothelial nitric oxide synthase (eNOS) plays a key role in blood pressure regulation and vascular homeostasis. Among the more potent inducers of eNOS activity in vascular endothelial cells is bradykinin (BK). This brief review summarizes the current state of knowledge with regard to regulation of eNOS through several distinct molecular mechanisms, each of which acts in concert with Ca2+-calmodulin (CaM) signaling in post-translational activation of eNOS. These mechanisms include alterations in protein-protein interactions with caveolin-1, the BK B2 receptor, and heat shock protein 90 (Hsp90). In addition, BK stimulates an increase in eNOS activity through phosphorylation of the enzyme at three specific amino acid residues as well as through dephosphorylation at a fourth residue.
MeSH term(s)	Animals ; Bradykinin/metabolism ; Bradykinin/physiology ; Caveolin 1 ; Caveolins/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/enzymology ; Endothelium, Vascular/metabolism ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Nitric Oxide Synthase/metabolism ; Phosphorylation ; Protein Binding ; Protein Processing, Post-Translational ; Receptor, Bradykinin B2 ; Receptors, Bradykinin/metabolism
Chemical Substances	CAV1 protein, human ; Caveolin 1 ; Caveolins ; HSP90 Heat-Shock Proteins ; Receptor, Bradykinin B2 ; Receptors, Bradykinin ; Nitric Oxide Synthase (EC 1.14.13.39) ; Bradykinin (S8TIM42R2W)
Language	English
Publishing date	2002-12-17
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	2043785-7
ISSN	1567-5769
ISSN	1567-5769
DOI	10.1016/s1567-5769(02)00185-6
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Article ; Online: TNFα reduces eNOS activity in endothelial cells through serine 116 phosphorylation and Pin1 binding: Confirmation of a direct, inhibitory interaction of Pin1 with eNOS.

Kennard, Simone / Ruan, Ling / Buffett, Ryan J / Fulton, David / Venema, Richard C

Vascular pharmacology

2016 Volume 81, Page(s) 61–68

Abstract: Production of NO by the endothelial nitric oxide synthase (eNOS) has a major role in blood pressure control and suppression of atherosclerosis. In a previous study, we presented evidence implicating the Pin1 prolyl isomerase in negative modulation of ... ...

Abstract	Production of NO by the endothelial nitric oxide synthase (eNOS) has a major role in blood pressure control and suppression of atherosclerosis. In a previous study, we presented evidence implicating the Pin1 prolyl isomerase in negative modulation of eNOS activity in bovine aortic endothelial cells (BAECs). Pin1 recognizes phosphoserine/phosphothreonine-proline motifs in target proteins and catalyzes prolyl isomerization at the peptide bond. In the present study, we show, first, with purified proteins, that Pin1 binds to eNOS directly via the Pin1 WW domain. Binding is enhanced by mimicking phosphorylation of eNOS at S116. Interaction of Pin1 with eNOS markedly reduces eNOS enzymatic activity. Second, in BAECs, we show that TNFα induces ERK 1/2-mediated S116 phosphorylation of eNOS, accompanied by Pin1 binding. TNFα treatment of BAECs results in a reduction in NO release from the cells in a manner that depends on the activities of both Pin1 and ERK 1/2. Evidence is also presented that this mechanism of eNOS regulation cannot occur in rat and mouse cells because there is no proline residue in the mouse and rat amino acid sequences adjacent to the putative phosphorylation site. Moreover, we find that phosphorylation of this site is not detectable in mouse eNOS.
MeSH term(s)	Animals ; Binding Sites ; Cattle ; Cells, Cultured ; Endothelial Cells/drug effects ; Endothelial Cells/enzymology ; Enzyme Inhibitors/pharmacology ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; Mice ; NIMA-Interacting Peptidylprolyl Isomerase/metabolism ; Nitric Oxide/metabolism ; Nitric Oxide Synthase Type III/antagonists & inhibitors ; Nitric Oxide Synthase Type III/metabolism ; Phosphorylation ; Protein Binding ; Protein Interaction Domains and Motifs ; Rats ; Serine ; Species Specificity ; Tumor Necrosis Factor-alpha/pharmacology
Chemical Substances	Enzyme Inhibitors ; NIMA-Interacting Peptidylprolyl Isomerase ; Tumor Necrosis Factor-alpha ; Nitric Oxide (31C4KY9ESH) ; Serine (452VLY9402) ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; Nos3 protein, mouse (EC 1.14.13.39) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; PIN1 protein, human (EC 5.2.1.8)
Language	English
Publishing date	2016-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2082846-9
ISSN	1879-3649 ; 1537-1891 ; 1879-3649
ISSN (online)	1879-3649 ; 1537-1891
ISSN	1879-3649
DOI	10.1016/j.vph.2016.04.003
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Zs.A 591: Show issues

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Article ; Online: Phytonutrients Differentially Stimulate NAD(P)H:Quinone Oxidoreductase, Inhibit Proliferation, and Trigger Mitotic Catastrophe in Hepa1c1c7 Cells.

Jackson, Steven J T / Singletary, Keith W / Murphy, Laura L / Venema, Richard C / Young, Andrew J

Journal of medicinal food

2015 Volume 19, Issue 1, Page(s) 47–53

Abstract: Phytonutrients have rapidly emerged as natural food chemicals possessing multifaceted biological actions that may support beneficial health outcomes. Among the vast array of phytonutrients currently being studied, sulforaphane, curcumin, quercetin, and ... ...

Abstract	Phytonutrients have rapidly emerged as natural food chemicals possessing multifaceted biological actions that may support beneficial health outcomes. Among the vast array of phytonutrients currently being studied, sulforaphane, curcumin, quercetin, and resveratrol have been frequently reported to stimulate the expression of endogenous detoxification enzymes and may thereby facilitate the neutralization of otherwise harmful environmental agents. Some of these same phytonutrients, however, have also been implicated in disrupting normal cell proliferation and hence may possess toxic properties in and of themselves. In this study, we characterize the respective minimum threshold concentrations of the aforementioned phytonutrients in Hepa1c1c7 cells that stimulate Nad(p)h: quinone oxidoreductase (NQO1), a key enzyme in the hepatic neutralization of menadione, other biological oxidants, and some environmental carcinogens. Moreover, our findings demonstrate that relatively low concentrations of either sulforaphane or curcumin significantly (P < .05) increase NQO1 protein expression and activity without triggering G2/M cell cycle arrest or mitotic catastrophe. The minimal quercetin concentration inducing NQO1, however, was 100-fold higher than that which disrupted mitosis. Also, while resveratrol modestly stimulated NQO1, the minimally effective resveratrol concentration concomitantly induced evidence of cellular apoptosis. Taken together, these findings indicate that only particular phytonutrients are likely efficacious in upregulating NQO1 activity without also leading to hepatic cytotoxicity.
MeSH term(s)	Animals ; Apoptosis/drug effects ; Cell Line ; Hepatocytes/cytology ; Hepatocytes/drug effects ; Hepatocytes/enzymology ; Mice ; Mitosis/drug effects ; NAD(P)H Dehydrogenase (Quinone)/genetics ; NAD(P)H Dehydrogenase (Quinone)/metabolism ; Phytochemicals/pharmacology
Chemical Substances	Phytochemicals ; NAD(P)H Dehydrogenase (Quinone) (EC 1.6.5.2) ; Noq1 protein, mouse (EC 1.6.5.2)
Language	English
Publishing date	2015-12-01
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1427365-2
ISSN	1557-7600 ; 1096-620X
ISSN (online)	1557-7600
ISSN	1096-620X
DOI	10.1089/jmf.2015.0079
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Zs.A 5916: Show issues

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Article ; Online: Calcineurin-mediated dephosphorylation of eNOS at serine 116 affects eNOS enzymatic activity indirectly by facilitating c-Src binding and tyrosine 83 phosphorylation.

Ruan, Ling / Torres, Christina M / Buffett, Ryan J / Kennard, Simone / Fulton, David / Venema, Richard C

Vascular pharmacology

2013 Volume 59, Issue 1-2, Page(s) 27–35

Abstract: It has been shown previously that phosphorylation of the endothelial nitric oxide synthase (eNOS) at serine 116 (S116) under basal conditions suppresses eNOS enzymatic activity in endothelial cells. It has also been shown that vascular endothelial growth ...

Abstract	It has been shown previously that phosphorylation of the endothelial nitric oxide synthase (eNOS) at serine 116 (S116) under basal conditions suppresses eNOS enzymatic activity in endothelial cells. It has also been shown that vascular endothelial growth factor (VEGF) treatment of endothelial cells produces a rapid S116 dephosphorylation, which is blocked by the calcineurin inhibitor, cyclosporin A (CsA). In this study, we show that activation of eNOS in response to a variety of other eNOS-activating agonists and the cytosolic calcium-elevating agent, thapsigargin also involves CsA-inhibitable S116 dephosphorylation. Studies with the purified eNOS enzyme also demonstrate that neither mimicking phosphorylation at S116 nor phosphorylation of the purified enzyme at S116 in vitro has any effect on enzymatic activity. Phospho-mimicking, however, does interfere with the interaction of eNOS with c-Src, an interaction which is known to activate eNOS by phosphorylation at tyrosine 83 (Y83). Agonist-stimulated eNOS-Src complex formation, as well as agonist-stimulated Y83 phosphorylation, are blocked by calcineurin inhibition by CsA and by a cell-permeable calcineurin inhibitory peptide. Taken together, these data suggest a mechanism of eNOS regulation whereby calcineurin-mediated dephosphorylation of eNOS at S116 affects eNOS enzymatic activity indirectly, rather than directly, by facilitating c-Src binding and Y83 phosphorylation.
MeSH term(s)	Animals ; COS Cells ; Calcineurin/metabolism ; Calcium/metabolism ; Cattle ; Cyclosporine/pharmacology ; Endothelial Cells/drug effects ; Endothelial Cells/enzymology ; Endothelial Cells/metabolism ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/enzymology ; Endothelium, Vascular/metabolism ; Enzyme Inhibitors/pharmacology ; Nitric Oxide Synthase Type III/antagonists & inhibitors ; Nitric Oxide Synthase Type III/metabolism ; Permeability/drug effects ; Phosphorylation ; Serine/metabolism ; Thapsigargin/pharmacology ; Tyrosine/metabolism
Chemical Substances	Enzyme Inhibitors ; Tyrosine (42HK56048U) ; Serine (452VLY9402) ; Thapsigargin (67526-95-8) ; Cyclosporine (83HN0GTJ6D) ; Nitric Oxide Synthase Type III (EC 1.14.13.39) ; Calcineurin (EC 3.1.3.16) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2013-05-30
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2082846-9
ISSN	1879-3649 ; 1537-1891 ; 1879-3649
ISSN (online)	1879-3649 ; 1537-1891
ISSN	1879-3649
DOI	10.1016/j.vph.2013.05.004
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Zs.A 591: Show issues

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Article ; Online: Curcumin binds tubulin, induces mitotic catastrophe, and impedes normal endothelial cell proliferation.

Jackson, Steven J T / Murphy, Laura L / Venema, Richard C / Singletary, Keith W / Young, Andrew J

Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association

2013 Volume 60, Page(s) 431–438

Abstract: Curcumin, a component of turmeric spice that imparts flavor and color to curry, is thought to possess anti-inflammatory and antioxidant properties in biological tissues. However, while such efficacies have been described in the context of carcinogenesis, ...

Abstract	Curcumin, a component of turmeric spice that imparts flavor and color to curry, is thought to possess anti-inflammatory and antioxidant properties in biological tissues. However, while such efficacies have been described in the context of carcinogenesis, the impact of curcumin on normal cell cycle regulation is poorly understood. Here, we provide evidence of curcumin toxicity in proliferating bovine aortic endothelial cells, at concentrations relevant to the diet and below those previously reported in cancer models. Upon confirming curcumin's ability to upregulate hemeoxygenase-1 in a dose-dependent fashion, we found the minimally efficacious curcumin concentration to also inhibit endothelial cell DNA synthesis. Moreover, curcumin concentrations below the minimum 2 μM threshold required to induce hemeoxygenase-1 bound tubulin protein in vitro and triggered hallmark evidence of mitotic catastrophe in vivo. Concentrations as low as 0.1 μM curcumin led to disproportionate DNA segregation, karyorrhexis, and micronucleation in proliferating endothelial cells. While suggesting a mechanism by which physiological curcumin concentrations inhibit cell cycle progression, these findings describe heretofore unappreciated curcumin toxicity with potential implications for endothelial growth, development, and tissue healing.
MeSH term(s)	Animals ; Antioxidants/pharmacology ; Cattle ; Cell Cycle Checkpoints/drug effects ; Cell Division/drug effects ; Cell Line ; Cell Proliferation/drug effects ; Curcumin/pharmacology ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Heme Oxygenase-1/genetics ; Heme Oxygenase-1/metabolism ; Microtubules/drug effects ; Microtubules/metabolism ; Mitosis/drug effects ; Tubulin/metabolism
Chemical Substances	Antioxidants ; Tubulin ; Heme Oxygenase-1 (EC 1.14.14.18) ; Curcumin (IT942ZTH98)
Language	English
Publishing date	2013-08-11
Publishing country	England
Document type	Journal Article
ZDB-ID	782617-5
ISSN	1873-6351 ; 0278-6915
ISSN (online)	1873-6351
ISSN	0278-6915
DOI	10.1016/j.fct.2013.08.008
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Zs.A 529: Show issues

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Article: Sulforaphane suppresses angiogenesis and disrupts endothelial mitotic progression and microtubule polymerization.

Jackson, Steven J T / Singletary, Keith W / Venema, Richard C

Vascular pharmacology

2006 Volume 46, Issue 2, Page(s) 77–84

Abstract: Sulforaphane (SUL), an isothiocyanate derived from broccoli and other cruciferous vegetables, is known to induce phase II detoxification enzymes, disrupt cancer cell microtubule polymerization, and trigger cell cycle arrest in breast and colon cancer ... ...

Abstract	Sulforaphane (SUL), an isothiocyanate derived from broccoli and other cruciferous vegetables, is known to induce phase II detoxification enzymes, disrupt cancer cell microtubule polymerization, and trigger cell cycle arrest in breast and colon cancer cells. Here, we provide the first evidence that SUL also acts to inhibit angiogenesis via suppression of endothelial cell proliferation. Bovine aortic endothelial (BAE) cells were exposed to concentrations of up to 15 microM SUL prior to cell cycle analysis and mitotic index quantification. Within 24 h, 15 microM SUL clearly induced G(2)/M accumulation and pre-metaphase arrest in BAE cells. Moreover, immunofluorescence tubulin staining indicated that this same SUL concentration was efficacious in not only disrupting mitotic progression, but also in perturbing normal polymerization of mitotic (and cytoplasmic) microtubules. Furthermore, daily administration of SUL (100 nmol/day, i.v. for 7 days) to female Balb/c mice bearing VEGF-impregnated Matrigel plugs strongly and significantly (P<0.05) suppressed angiogenesis progression as measured by hemoglobin concentration. Taken together, these findings suggest that the endothelial cell population is a novel target of SUL action both in vitro and in vivo. This mechanism of SUL-induced endothelial microtubule disruption and early mitotic arrest may further discern a potential role of SUL as a chemopreventive agent.
MeSH term(s)	Angiogenesis Inhibitors/pharmacology ; Angiogenesis Inhibitors/therapeutic use ; Animals ; Anticarcinogenic Agents/pharmacology ; Cattle ; Cell Proliferation/drug effects ; Cells, Cultured ; Collagen/administration & dosage ; Dose-Response Relationship, Drug ; Drug Combinations ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Female ; Injections, Subcutaneous ; Isothiocyanates ; Laminin/administration & dosage ; Mice ; Mice, Inbred BALB C ; Microtubules/drug effects ; Microtubules/metabolism ; Mitosis/drug effects ; Neovascularization, Pathologic/prevention & control ; Proteoglycans/administration & dosage ; Spindle Apparatus/drug effects ; Spindle Apparatus/metabolism ; Subcutaneous Tissue/blood supply ; Thiocyanates/pharmacology ; Thiocyanates/therapeutic use ; Time Factors ; Tubulin Modulators/pharmacology ; Tubulin Modulators/therapeutic use ; Vascular Endothelial Growth Factor A/administration & dosage
Chemical Substances	Angiogenesis Inhibitors ; Anticarcinogenic Agents ; Drug Combinations ; Isothiocyanates ; Laminin ; Proteoglycans ; Thiocyanates ; Tubulin Modulators ; Vascular Endothelial Growth Factor A ; matrigel (119978-18-6) ; Collagen (9007-34-5) ; sulforaphane (GA49J4310U)
Language	English
Publishing date	2006-07-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2082846-9
ISSN	1537-1891 ; 1537-1891 ; 1879-3649
ISSN (online)	1537-1891
ISSN	1537-1891 ; 1879-3649
DOI	10.1016/j.vph.2006.06.015
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Zs.A 591: Show issues

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Article: Curcumin binds tubulin, induces mitotic catastrophe, and impedes normal endothelial cell proliferation

Jackson, Steven J.T / Murphy, Laura L / Venema, Richard C / Singletary, Keith W / Young, Andrew J

Food and chemical toxicology. 2013 Oct., v. 60

2013

Abstract	Curcumin, a component of turmeric spice that imparts flavor and color to curry, is thought to possess anti-inflammatory and antioxidant properties in biological tissues. However, while such efficacies have been described in the context of carcinogenesis, the impact of curcumin on normal cell cycle regulation is poorly understood. Here, we provide evidence of curcumin toxicity in proliferating bovine aortic endothelial cells, at concentrations relevant to the diet and below those previously reported in cancer models. Upon confirming curcumin’s ability to upregulate hemeoxygenase-1 in a dose-dependent fashion, we found the minimally efficacious curcumin concentration to also inhibit endothelial cell DNA synthesis. Moreover, curcumin concentrations below the minimum 2μM threshold required to induce hemeoxygenase-1 bound tubulin protein in vitro and triggered hallmark evidence of mitotic catastrophe in vivo. Concentrations as low as 0.1μM curcumin led to disproportionate DNA segregation, karyorrhexis, and micronucleation in proliferating endothelial cells. While suggesting a mechanism by which physiological curcumin concentrations inhibit cell cycle progression, these findings describe heretofore unappreciated curcumin toxicity with potential implications for endothelial growth, development, and tissue healing.
Keywords	DNA ; DNA replication ; anti-inflammatory activity ; antioxidant activity ; carcinogenesis ; cattle ; cell cycle ; cell proliferation ; curcumin ; diet ; dose response ; endothelial cells ; models ; tissues ; toxicity ; tubulin ; turmeric
Language	English
Dates of publication	2013-10
Size	p. 431-438.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	782617-5
ISSN	1873-6351 ; 0278-6915
ISSN (online)	1873-6351
ISSN	0278-6915
DOI	10.1016/j.fct.2013.08.008
Database	NAL-Catalogue (AGRICOLA)

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Z 4035: Show issues

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Article: Quercetin Inhibits eNOS, Microtubule Polymerization, and Mitotic Progression in Bovine Aortic Endothelial Cells

Jackson, Steven J. T / Venema, Richard C

Journal of nutrition. 2006 May, v. 136, no. 5

2006

Abstract: Quercetin (QRN), one of the most abundant flavonoids in the human diet, is a known antioxidant and inhibitor of cancer cell cycle progression. Here, we provide the first evidence that QRN inhibits angiogenesis via a mechanism involving both suppression ... ...

Abstract	Quercetin (QRN), one of the most abundant flavonoids in the human diet, is a known antioxidant and inhibitor of cancer cell cycle progression. Here, we provide the first evidence that QRN inhibits angiogenesis via a mechanism involving both suppression of endothelial nitric oxide synthase (eNOS) and early M-phase cell cycle arrest. Bovine aortic endothelial (BAE) cells were exposed to doses of up to 100 [micro]mol/L QRN and assayed for eNOS activity and phosphorylation status. Phosphorylation of eNOS at Ser 617 (bovine sequence) is thought to occur in response to Akt stimulation and to be required for eNOS activity. Together with basal eNOS activity, eNOS phosphorylation at Ser 617 and Akt Ser 473 phosphorylation were dose dependently and concomitantly suppressed by QRN within 30 min. Furthermore, although the significant (P < 0.05) inhibitory effect of a single 100 [micro]mol/L QRN dose on eNOS activity was overcome within [approximately]24 h, chronic QRN exposures (24-48 h) led to early M-phase arrest and disruption of mitotic microtubule polymerization. In vivo, QRN administered i.p. to female Balb/C mice bearing both syngeneic mammary tumors and Matrigel implants suppressed angiogenesis as measured by endothelial cell immunohistochemistry and hemoglobin concentration. Taken together, these findings suggest a dual mechanism by which QRN suppresses endothelial cell proliferation, both acutely via inhibition of eNOS Ser 617 phosphorylation, and chronically via perturbation of mitotic microtubule polymerization. This novel mechanism of QRN in endothelial cells may in part explain its inhibitory action on angiogenesis and further discern a potential role of QRN as a chemopreventive agent.
Keywords	cattle ; endothelial cells ; cell culture ; quercetin ; nitric oxide synthase ; endothelium ; enzyme inhibition ; mitosis ; microtubules ; polymerization ; biochemical mechanisms ; cell cycle ; enzyme activity ; protein phosphorylation ; mice ; animal disease models ; breast neoplasms ; human diseases ; human nutrition ; angiogenesis
Language	English
Dates of publication	2006-05
Size	p. 1178-1184.
Publishing place	American Society for Nutrition
Document type	Article
ZDB-ID	218373-0
ISSN	1541-6100 ; 0022-3166
ISSN (online)	1541-6100
ISSN	0022-3166
Database	NAL-Catalogue (AGRICOLA)

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Z 774: Show issues

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Article: Quercetin inhibits eNOS, microtubule polymerization, and mitotic progression in bovine aortic endothelial cells.

Jackson, Steven J T / Venema, Richard C

The Journal of nutrition

2003 Volume 136, Issue 5, Page(s) 1178–1184

Abstract	Quercetin (QRN), one of the most abundant flavonoids in the human diet, is a known antioxidant and inhibitor of cancer cell cycle progression. Here, we provide the first evidence that QRN inhibits angiogenesis via a mechanism involving both suppression of endothelial nitric oxide synthase (eNOS) and early M-phase cell cycle arrest. Bovine aortic endothelial (BAE) cells were exposed to doses of up to 100 micromol/L QRN and assayed for eNOS activity and phosphorylation status. Phosphorylation of eNOS at Ser 617 (bovine sequence) is thought to occur in response to Akt stimulation and to be required for eNOS activity. Together with basal eNOS activity, eNOS phosphorylation at Ser 617 and Akt Ser 473 phosphorylation were dose dependently and concomitantly suppressed by QRN within 30 min. Furthermore, although the significant (P < 0.05) inhibitory effect of a single 100 micromol/L QRN dose on eNOS activity was overcome within approximately 24 h, chronic QRN exposures (24-48 h) led to early M-phase arrest and disruption of mitotic microtubule polymerization. In vivo, QRN administered i.p. to female Balb/C mice bearing both syngeneic mammary tumors and Matrigel implants suppressed angiogenesis as measured by endothelial cell immunohistochemistry and hemoglobin concentration. Taken together, these findings suggest a dual mechanism by which QRN suppresses endothelial cell proliferation, both acutely via inhibition of eNOS Ser 617 phosphorylation, and chronically via perturbation of mitotic microtubule polymerization. This novel mechanism of QRN in endothelial cells may in part explain its inhibitory action on angiogenesis and further discern a potential role of QRN as a chemopreventive agent.
MeSH term(s)	Animals ; Aorta ; Arginine/metabolism ; Cattle ; Cell Division/drug effects ; Cell Line ; Citrulline/metabolism ; Endothelium, Vascular/cytology ; Endothelium, Vascular/drug effects ; Endothelium, Vascular/enzymology ; Microtubules/drug effects ; Microtubules/enzymology ; Mitosis/drug effects ; Nitric Oxide Synthase Type III/drug effects ; Nitric Oxide Synthase Type III/genetics ; Nitric Oxide Synthase Type III/metabolism ; Quercetin/pharmacology
Chemical Substances	Citrulline (29VT07BGDA) ; Arginine (94ZLA3W45F) ; Quercetin (9IKM0I5T1E) ; Nitric Oxide Synthase Type III (EC 1.14.13.39)
Language	English
Publishing date	2003-05-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	218373-0
ISSN	1541-6100 ; 0022-3166
ISSN (online)	1541-6100
ISSN	0022-3166
DOI	10.1093/jn/136.5.1178
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Uc I Zs.205: Show issues

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Article: Endostatin induces acute endothelial nitric oxide and prostacyclin release.

Li, Chunying / Harris, M Brennan / Venema, Virginia J / Venema, Richard C

Biochemical and biophysical research communications

2005 Volume 329, Issue 3, Page(s) 873–878

Abstract: Chronic exposure to endostatin (ES) blocks endothelial cell (EC) proliferation, and migration and induces EC apoptosis thereby inhibiting angiogenesis. Nitric oxide (NO) and prostacyclin (PGI(2)), in contrast, play important roles in promoting ... ...

Abstract	Chronic exposure to endostatin (ES) blocks endothelial cell (EC) proliferation, and migration and induces EC apoptosis thereby inhibiting angiogenesis. Nitric oxide (NO) and prostacyclin (PGI(2)), in contrast, play important roles in promoting angiogenesis. In this study, we examined the acute effects of ES on endothelial NO and PGI(2) production. Unexpectedly, a cGMP reporter cell assay showed that ES-induced acute endothelial NO release in cultured bovine aortic endothelial cells (BAECs). Enzyme immunoassay showed that ES also induced an acute increase in PGI(2) production in BAECs. These results were confirmed by ex vivo vascular ring studies that showed vascular relaxation in response to ES. Immunoblot analysis showed that ES stimulated acute phosphorylation of endothelial nitric oxide synthase (eNOS) at Ser116, Ser617, Ser635, and Ser1179, and dephosphorylation at Thr497 in BAECs, events associated with eNOS activation. Short-term exposure of EC to ES, therefore, unlike long-term exposure which is anti-angiogenic, may be pro-angiogenic.
MeSH term(s)	Animals ; Cattle ; Cells, Cultured ; Endostatins/pharmacology ; Endothelial Cells/drug effects ; Endothelial Cells/metabolism ; Epoprostenol/metabolism ; Nitric Oxide/metabolism ; Nitric Oxide Synthase/metabolism ; Nitric Oxide Synthase Type III
Chemical Substances	Endostatins ; Nitric Oxide (31C4KY9ESH) ; Epoprostenol (DCR9Z582X0) ; Nitric Oxide Synthase (EC 1.14.13.39) ; Nitric Oxide Synthase Type III (EC 1.14.13.39)
Language	English
Publishing date	2005-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2005.02.055
Database	MEDical Literature Analysis and Retrieval System OnLINE

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