Cyclic GMP

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Peter C. Newell - One of the best experts on this subject based on the ideXlab platform.

  • Calcium, Cyclic GMP and the control of myosin II during chemotactic signal transduction ofDictyostelium
    Journal of Biosciences, 1995
    Co-Authors: Peter C. Newell
    Abstract:

    Evidence is presented for Ca^2+ and Cyclic GMP being involved in signal transduction between the cell surface Cyclic AMP receptors and cytoskeletal myosin II involved in chemotactic cell movement. Ca^2+ is shown to be required for chemotactic aggregation of amoebae. The evidence for uptake and/or eflux of this ion being regulated by the nucleotide Cyclic GMP is discussed. The connection between Ca^2+, Cyclic GMP and chemotactic cell movement has been explored using “streamer F” mutants. The primary defect in these mutants is in the structural gene for the Cyclic GMP-specific phosphodiesterase which results in the mutants producing an abnormally prolonged peak of accumulation of Cyclic GMP in response to stimulation with the chernoattractant Cyclic AMP. While events associated with production and relay of Cyclic AMP signals are normal, certain events associated with movement are (like the Cyclic GMP response) abnormally prolonged in the mutants. These events include Ca^2+ uptake, myosin II association with the cytoskeleton and inhibition of myosin heavy and light chain phosphorylation. These changes can be correlated with the amoebae becoming elongated and transiently decreasing their locomotive speed after chemotactic stimulation. Other mutants studied in which the accumulation of Cyclic GMP in response to Cyclic AMP stimulation was absent produced no myosin II responses. Models are described in which Cyclic GMP (directly or indirectly via Ca^2+) regulates accumulation of myosin II on the cytoskeleton by inhibiting phosphorylation of the myosin heavy and light chain kinases.

Ferid Murad - One of the best experts on this subject based on the ideXlab platform.

  • Effects of Cyclic GMP on smooth muscle relaxation.
    Advances in pharmacology (San Diego), 2008
    Co-Authors: Timothy D Warner, Hong Sheng, Jane A. Mitchell, Ferid Murad
    Abstract:

    Publisher Summary The elevation of Cyclic guanosine monophosphate (GMP) within smooth muscle leads to relaxation. This elevation can be the result of the activity of two distinct guanylyl cyclase enzymes, cytoplasmic and membrane-bound, respectively, which convert guanosine triphosphate (GTP) to Cyclic GMP. Although both of these enzymes produce the same second messenger, they become stimulated to do this by clearly different agents and possess different molecular structures. This chapter provides information on neural pathways that may stimulate Cyclic GMP formation in smooth muscle, variations in regional and tissue responses to agents that elevate Cyclic GMP, and other evidence showing the diversity of Cyclic GMP responses in smooth muscle. Cyclic GMP levels within smooth muscle are affected then by a number of different pathways. Physiologically, nitric oxide (NO) and atrial natriuretic factor (ANF) are probably the two most important regulators for smooth-muscle function, but a variety of other mediators and pharmacological agents may also influence this system. Cyclic GMP plays an important role in the control of smooth muscle tone indicating it to be an important physiological and biochemical target for research and a pharmacological target for therapeutic agents.

Diamond J - One of the best experts on this subject based on the ideXlab platform.

T.a. Brock - One of the best experts on this subject based on the ideXlab platform.

  • Peroxynitrite stimulates vascular smooth muscle cell Cyclic GMP synthesis.
    FEBS Letters, 1995
    Co-Authors: Margaret M. Tarpey, Joseph S. Beckman, Harry Ischiropoulos, J.z. Gore, T.a. Brock
    Abstract:

    Peroxynitrite stimulated the synthesis of Cyclic GMP by rat aortic smooth muscle in a time- and dose-dependent manner. Peak formation of Cyclic GMP occurred at 1 min with 100 μM peroxynitrite and was inhibited by oxyhemoglobin. Peroxynitrite was less potent than nitric oxide in stimulating Cyclic GMP synthesis. Peroxynitrite also enhanced endothelial-dependent Cyclic GMP synthesis, via generation of a long-lived substance, which was prevented by inhibition of glutathione synthesis. These data show that peroxynitrite stimulates Cyclic GMP synthesis, inferring production of low yields of nitric oxide or associated derivatives. Additionally, vascular exposure to peroxynitrite potentiates endothelial-dependent activation of guanylate cyclase.

Timothy D Warner - One of the best experts on this subject based on the ideXlab platform.

  • Effects of Cyclic GMP on smooth muscle relaxation.
    Advances in pharmacology (San Diego), 2008
    Co-Authors: Timothy D Warner, Hong Sheng, Jane A. Mitchell, Ferid Murad
    Abstract:

    Publisher Summary The elevation of Cyclic guanosine monophosphate (GMP) within smooth muscle leads to relaxation. This elevation can be the result of the activity of two distinct guanylyl cyclase enzymes, cytoplasmic and membrane-bound, respectively, which convert guanosine triphosphate (GTP) to Cyclic GMP. Although both of these enzymes produce the same second messenger, they become stimulated to do this by clearly different agents and possess different molecular structures. This chapter provides information on neural pathways that may stimulate Cyclic GMP formation in smooth muscle, variations in regional and tissue responses to agents that elevate Cyclic GMP, and other evidence showing the diversity of Cyclic GMP responses in smooth muscle. Cyclic GMP levels within smooth muscle are affected then by a number of different pathways. Physiologically, nitric oxide (NO) and atrial natriuretic factor (ANF) are probably the two most important regulators for smooth-muscle function, but a variety of other mediators and pharmacological agents may also influence this system. Cyclic GMP plays an important role in the control of smooth muscle tone indicating it to be an important physiological and biochemical target for research and a pharmacological target for therapeutic agents.