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  1. Article: Nitric oxide as a unique signaling molecule in the vascular system: a historical overview.

    Ignarro, L J

    Journal of physiology and pharmacology : an official journal of the Polish Physiological Society

    2002  Volume 53, Issue 4 Pt 1, Page(s) 503–514

    Abstract: In retrospect, basic research in the fields of NO and cyclic GMP during the past two decades appears to have followed a logical course beginning with the findings that NO and cyclic GMP are vascular smooth muscle relaxants, that nitroglycerin relaxes ... ...

    Abstract In retrospect, basic research in the fields of NO and cyclic GMP during the past two decades appears to have followed a logical course beginning with the findings that NO and cyclic GMP are vascular smooth muscle relaxants, that nitroglycerin relaxes smooth muscle by metabolism to NO, progressing to the discovery that mammalian cells synthesize NO, and finally the revelation that NO is a neurotransmitter mediating vasodilation in specialized vascular beds. A great deal of basic and clinical research on the physiological and pathophysiological roles of NO in cardiovascular function has been conducted since the discovery that EDRF is NO. The new knowledge on NO should enable investigators in this field to develop novel and more effective therapeutic strategies for the prevention, diagnosis and treatment of numerous cardiovascular disorders. Since NO elicits a protective and beneficial action in many disease states, novel NO donor drugs for clinical use should prove to be very effective drugs for the treatment of essential hypertension, stroke, coronary artery disease, vascular complications of diabetes, impotency and other disorders involving the vascular system.
    MeSH term(s) Animals ; Blood Vessels/physiology ; Humans ; Muscle, Smooth, Vascular/physiology ; Nitric Oxide/physiology ; Nitroglycerin/metabolism ; Penile Erection/physiology ; Signal Transduction/physiology ; Vasomotor System/physiology
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; Nitroglycerin (G59M7S0WS3)
    Language English
    Publishing date 2002-12
    Publishing country Poland
    Document type Journal Article ; Review
    ZDB-ID 1125221-2
    ISSN 1899-1505 ; 0867-5910 ; 0044-6033
    ISSN (online) 1899-1505
    ISSN 0867-5910 ; 0044-6033
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  2. Article: The unique role of nitric oxide as a signaling molecule in the cardiovascular system.

    Ignarro, L J

    Italian heart journal : official journal of the Italian Federation of Cardiology

    2000  Volume 1 Suppl 3, Page(s) S28–9

    MeSH term(s) Cardiovascular System/metabolism ; Cell Communication ; Humans ; Nitric Oxide/metabolism
    Chemical Substances Nitric Oxide (31C4KY9ESH)
    Language English
    Publishing date 2000-09
    Publishing country Italy
    Document type Journal Article
    ZDB-ID 2012387-5
    ISSN 1972-6465 ; 1129-471X ; 1129-4728
    ISSN (online) 1972-6465
    ISSN 1129-471X ; 1129-4728
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  3. Article: Nitric oxide: a unique endogenous signaling molecule in vascular biology.

    Ignarro, L J

    Bioscience reports

    1999  Volume 19, Issue 2, Page(s) 51–71

    Abstract: The properties of nitric oxide as an endogenous cell signaling molecule in vascular biology are described. ...

    Abstract The properties of nitric oxide as an endogenous cell signaling molecule in vascular biology are described.
    MeSH term(s) Animals ; Blood Vessels/physiology ; Endothelium, Vascular/physiology ; Forecasting ; Guanylate Cyclase/metabolism ; Humans ; Nitric Oxide/pharmacology ; Nitric Oxide/physiology ; Nitroglycerin/metabolism ; Nobel Prize ; Platelet Aggregation Inhibitors/metabolism ; Platelet Aggregation Inhibitors/pharmacology ; Signal Transduction ; Vasodilator Agents/metabolism
    Chemical Substances Platelet Aggregation Inhibitors ; Vasodilator Agents ; Nitric Oxide (31C4KY9ESH) ; Guanylate Cyclase (EC 4.6.1.2) ; Nitroglycerin (G59M7S0WS3)
    Language English
    Publishing date 1999-04-19
    Publishing country England
    Document type Journal Article ; Lecture ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 764946-0
    ISSN 1573-4935 ; 0144-8463
    ISSN (online) 1573-4935
    ISSN 0144-8463
    DOI 10.1023/a:1020150124721
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  4. Article: Physiology and pathophysiology of nitric oxide.

    Ignarro, L J

    Kidney international. Supplement

    1996  Volume 55, Page(s) S2–5

    Abstract: Nitric oxide (NO) was discovered to be a potent vasodilator, inhibitor of platelet aggregation, and active species of nitroglycerin before the discovery of endothelium-derived relaxing factor (EDRF) in 1980. Subsequent studies revealed that EDRF is NO, ... ...

    Abstract Nitric oxide (NO) was discovered to be a potent vasodilator, inhibitor of platelet aggregation, and active species of nitroglycerin before the discovery of endothelium-derived relaxing factor (EDRF) in 1980. Subsequent studies revealed that EDRF is NO, and is synthesized by mammalian cells from L-arginine through a complex oxidation reaction catalyzed by the flavo-hemoprotein NO synthase (NOS). NOS catalyzes the NADPH- and oxygen-dependent oxygenation of L-arginine to NO plus L-citrulline in a reaction that requires at least six cofactors including NADPH, FAD, FMN, tetrahydrobiopterin, heme, and calmodulin. NO elicits its known physiological actions by activating cytosolic guanylate cyclase, which converts GTP to cyclic GMP. Endothelial NOS and neuronal NOS are constitutively present and activated by increases in intracellular calcium triggered by endogenous chemicals. NO then diffuses into nearby target cells to elevate cyclic GMP levels and thereby trigger cell function. NOS activity can also be regulated by a negative feedback mechanism involving NO itself. Much greater quantities of NO are produced pathophysiologically by a distinct form of NOS that can be induced in vascular endothelium, smooth muscle and macrophages by endotoxin and cytokines. This high-output production of NO is not regulated by calcium and is cytotoxic by mechanisms involving interaction with iron-containing proteins.
    MeSH term(s) Animals ; Humans ; Hypertension/physiopathology ; Nitric Oxide/physiology
    Chemical Substances Nitric Oxide (31C4KY9ESH)
    Language English
    Publishing date 1996-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 193442-9
    ISSN 2157-1716 ; 0098-6577 ; 2157-1724
    ISSN (online) 2157-1716
    ISSN 0098-6577 ; 2157-1724
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  5. Article: Regulation of cytosolic guanylyl cyclase by porphyrins and metalloporphyrins.

    Ignarro, L J

    Advances in pharmacology (San Diego, Calif.)

    1994  Volume 26, Page(s) 35–65

    Abstract: The experimental evidence is convincing that cytosolic guanylate cyclase is a hemoprotein containing stoichiometric amounts of heme, which functions as a prosthetic group for enzyme activation by NO. Nearly all of the studies described in this chapter ... ...

    Abstract The experimental evidence is convincing that cytosolic guanylate cyclase is a hemoprotein containing stoichiometric amounts of heme, which functions as a prosthetic group for enzyme activation by NO. Nearly all of the studies described in this chapter were conducted before we began to appreciate in 1986 that mammalian vascular endothelial cells could synthesize their own NO. We know now that many different cell types synthesize NO, and that in most instances the NO interacts in a paracrine manner with adjacent target cells to activate cytosolic guanylate cyclase and elevate intracellular levels of cyclic GMP (Ignarro, 1990). The studies on endothelium-derived relaxing factor and authentic NO have shown clearly that heme and hemoproteins have a very high binding affinity for, and inhibit the actions of, these substances (Ignarro, 1989). The interaction between NO and the heme prosthetic group of guanylate cyclase appears to constitute an important signal transduction mechanism whereby NO raises intracellular cyclic GMP levels. This novel signal transduction mechanism is highly conducive to the efficient functioning of NO as a paracrine mediator of cellular function. As a small, lipophilic, and chemically labile molecule, NO diffuses out of its cells of origin and into nearby target cells. The very high binding affinity of enzyme-bound heme for NO ensures interaction of the two to cause guanylate cyclase activation and cyclic GMP formation. Thus, relatively uncomplicated mechanism can account for the paracrine function of endogenous NO in transcellular communication.
    MeSH term(s) Animals ; Cytosol/enzymology ; Enzyme Activation/physiology ; Guanylate Cyclase/biosynthesis ; Guanylate Cyclase/metabolism ; Humans ; Metalloporphyrins/physiology ; Nitric Oxide/physiology ; Porphyrins/physiology ; Structure-Activity Relationship
    Chemical Substances Metalloporphyrins ; Porphyrins ; Nitric Oxide (31C4KY9ESH) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 1994
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1054-3589
    ISSN 1054-3589
    DOI 10.1016/s1054-3589(08)60050-2
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  6. Article: Nitric oxide-mediated vasorelaxation.

    Ignarro, L J

    Thrombosis and haemostasis

    1993  Volume 70, Issue 1, Page(s) 148–151

    MeSH term(s) Amino Acid Oxidoreductases/metabolism ; Humans ; Nitric Oxide/physiology ; Nitric Oxide Synthase ; Signal Transduction/physiology ; Vasodilation/drug effects ; Vasodilation/physiology
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; Nitric Oxide Synthase (EC 1.14.13.39) ; Amino Acid Oxidoreductases (EC 1.4.-)
    Language English
    Publishing date 1993-07-01
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 518294-3
    ISSN 0340-6245
    ISSN 0340-6245
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  7. Article: Haem-dependent activation of cytosolic guanylate cyclase by nitric oxide: a widespread signal transduction mechanism.

    Ignarro, L J

    Biochemical Society transactions

    1992  Volume 20, Issue 2, Page(s) 465–469

    MeSH term(s) Animals ; Cytosol/enzymology ; Enzyme Activation ; Guanylate Cyclase/metabolism ; Heme/pharmacology ; Heme/physiology ; Isoenzymes/metabolism ; Models, Biological ; Muscle, Smooth, Vascular/enzymology ; Nitric Oxide/metabolism ; Nitric Oxide/pharmacology ; Signal Transduction/drug effects
    Chemical Substances Isoenzymes ; Nitric Oxide (31C4KY9ESH) ; Heme (42VZT0U6YR) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 1992-05
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 184237-7
    ISSN 1470-8752 ; 0300-5127
    ISSN (online) 1470-8752
    ISSN 0300-5127
    DOI 10.1042/bst0200465
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  8. Article: Mechanism of action of nitric oxide: heme-dependent activation of guanylate cyclase represents a unifying signal transduction mechanism.

    Ignarro, L J

    Japanese journal of pharmacology

    1992  Volume 58 Suppl 2, Page(s) 207P–212P

    MeSH term(s) Animals ; Enzyme Activation ; Guanylate Cyclase/metabolism ; Heme/physiology ; Humans ; Nitric Oxide/pharmacology ; Signal Transduction/physiology
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; Heme (42VZT0U6YR) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 1992
    Publishing country Japan
    Document type Journal Article ; Review
    ZDB-ID 218222-1
    ISSN 1347-3506 ; 0021-5198
    ISSN (online) 1347-3506
    ISSN 0021-5198
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  9. Article: Physiological significance of endogenous nitric oxide.

    Ignarro, L J

    Seminars in perinatology

    1991  Volume 15, Issue 1, Page(s) 20–26

    MeSH term(s) Animals ; Arginine/metabolism ; Enzyme Activation/physiology ; Guanylate Cyclase/metabolism ; Half-Life ; Humans ; Nitric Oxide/metabolism ; Nitric Oxide/physiology ; Signal Transduction/physiology ; Vasodilation/physiology
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; Arginine (94ZLA3W45F) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 1991-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 752403-1
    ISSN 1558-075X ; 0146-0005
    ISSN (online) 1558-075X
    ISSN 0146-0005
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  10. Article: Heme-dependent activation of guanylate cyclase by nitric oxide: a novel signal transduction mechanism.

    Ignarro, L J

    Blood vessels

    1991  Volume 28, Issue 1-3, Page(s) 67–73

    Abstract: The interaction between nitric oxide (NO) synthesized in one cell and cytosolic guanylate-cyclase-bound heme located in adjacent target cells to generate the NO-heme adduct of guanylate cyclase represents a novel and widespread signal transduction ... ...

    Abstract The interaction between nitric oxide (NO) synthesized in one cell and cytosolic guanylate-cyclase-bound heme located in adjacent target cells to generate the NO-heme adduct of guanylate cyclase represents a novel and widespread signal transduction mechanism that links extracellular stimuli to the biosynthesis of cyclic GMP in target cells. A variety of chemical factors interact with selective extracellular receptors and trigger the biosynthesis of NO from L-arginine. The unique chemistry of NO endows this molecule with the capacity to diffuse rapidly into nearby cells and stimulate cyclic GMP formation. Cyclic GMP acts as a messenger in each cell type to trigger different but complementary cellular responses within a localized environment. This transcellular signaling is a form of rapid intercellular communication allowing the simultaneous local initiation of increased blood flow, inhibition of platelet-induced thrombosis and other cellular functions.
    MeSH term(s) Animals ; Arginine/analogs & derivatives ; Arginine/pharmacology ; Enzyme Activation/drug effects ; Guanylate Cyclase/metabolism ; Heme/physiology ; Humans ; Nitric Oxide/pharmacology ; Signal Transduction
    Chemical Substances Nitric Oxide (31C4KY9ESH) ; Heme (42VZT0U6YR) ; Arginine (94ZLA3W45F) ; Guanylate Cyclase (EC 4.6.1.2)
    Language English
    Publishing date 1991
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 125104-1
    ISSN 0303-6847 ; 0302-2765
    ISSN 0303-6847 ; 0302-2765
    DOI 10.1159/000158845
    Database MEDical Literature Analysis and Retrieval System OnLINE

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