cyclic-gmp and zinc-chloride

cyclic-gmp has been researched along with zinc-chloride* in 2 studies

Other Studies

2 other study(ies) available for cyclic-gmp and zinc-chloride

ArticleYear
NO mobilizes intracellular Zn2+ via cGMP/PKG signaling pathway and prevents mitochondrial oxidant damage in cardiomyocytes.
    Cardiovascular research, 2007, Jul-15, Volume: 75, Issue:2

    Our aim was to determine if NO prevents mitochondrial oxidant damage by mobilizing intracellular free zinc (Zn(2+)).. Zn(2+) levels were determined by imaging enzymatically isolated adult rat cardiomyocytes loaded with Newport Green DCF. Mitochondrial membrane potential (DeltaPsi(m)) was assessed by imaging cardiomyocytes loaded with tetramethylrhodamine ethyl ester (TMRE).. S-nitroso-N-acetylpenicillamine (SNAP) dramatically increased Zn(2+), which was blocked by both ODQ and NS2028, two specific inhibitors of guanylyl cyclase. The protein kinase G (PKG) inhibitor KT5823 blocked the effect of SNAP while the PKG activator 8-Br-cGMP mimicked the action of SNAP, indicating that the cGMP/PKG pathway is responsible for the effect of SNAP. The increased Zn(2+) was prevented by 5-hydroxydecanoate (5HD) but was mimicked by diazoxide, implying that mitochondrial K(ATP) channel opening may account for this effect. Since chelation of Zn(2+) blocked the preventive effect of SNAP on H(2)O(2)-induced loss of DeltaPsi(m) and exogenous zinc (1 microM ZnCl(2)) prevented dissipation of DeltaPsi(m), Zn(2+) may play a critical role in the protective effect of NO. The MEK (mitogen-activated protein kinase or extracellular signal-regulated kinase) inhibitor PD98059 blocked the preventive effects of SNAP and zinc on DeltaPsi(m), indicating that extracellular signal-regulated kinase (ERK) mediates the protective effect of both these compounds on mitochondrial oxidant damage. A Western blot analysis further showed that ZnCl(2) significantly enhances phosphorylation of ERK, confirming the involvement of ERK in the action of Zn(2+).. In isolated cardiomyocytes, NO mobilizes endogenous zinc by opening mitochondrial K(ATP) channels through the cGMP/PKG pathway. In these cells, Zn(2+) may be an important mediator of the action of NO on the mitochondrial death pathway.

    Topics: Animals; Cells, Cultured; Chlorides; Cyclic GMP; Cyclic GMP-Dependent Protein Kinases; Flavonoids; Guanylate Cyclase; Membrane Potential, Mitochondrial; Microscopy, Confocal; Mitochondria, Heart; Mitogen-Activated Protein Kinase Kinases; Myocytes, Cardiac; Nitric Oxide; Nitric Oxide Donors; Oxadiazoles; Oxazines; Oxidation-Reduction; Penicillamine; Phosphorylation; Quinoxalines; Rats; Signal Transduction; Zinc; Zinc Compounds

2007
Cytochemical localization of guanylyl cyclase activity in rabbit taste bud cells.
    Chemical senses, 1995, Volume: 20, Issue:2

    Guanylyl cyclase activity was cytochemically demonstrated in rabbit foliate taste buds. The enzymatic activity was localized in the apical portion (microvilli and neck) of taste bud cells. Especially strong activity was observed on the microvillous membrane of type I (dark) cells and often on a blunt process of type III cells. The microvilli of type II (light) cells showed weak enzymatic activity. Considering that the apical portion of taste cells is a likely site of interaction between taste stimuli and the cells, the results support the idea that cyclic GMP is involved in taste transduction.

    Topics: Animals; Cadmium; Cadmium Chloride; Chlorides; Cyclic GMP; Guanylate Cyclase; Histocytochemistry; Male; Mercuric Chloride; Rabbits; Signal Transduction; Taste; Taste Buds; Zinc Compounds

1995