نتایج جستجو برای: zn2

تعداد نتایج: 3550  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1976
G A Tejwani F O Pedrosa S Pontremoli B L Horecker

At neutral pH, Zn2+ is a potent and specific inhibitor of rat liver fructose 1,6-bisphosphatase (EC 3.1.3.11; D-fructose-1,6-bisphosphate 1-phosphohydrolase). Inhibition by Zn2+ is uncompetitive with respect to the activating cations Mg2+ and Mn2+, and the kinetic data suggest that the enzyme possesses a distinct high-affinity binding site for Zn2+, with Ki of approximately 0.3 muM. At higher c...

Journal: :Frontiers in bioscience 2017
Math P Cuajungco Kirill Kiselyov

Lysosomes are emerging as important players in cellular zinc ion (Zn2+) homeostasis. The series of work on Zn2+ accumulation in the neuronal lysosomes and the mounting evidence on the role of lysosomal Zn2+ in cell death during mammary gland involution set a biological precedent for the central role of the lysosomes in cellular Zn2+ handling. Such a role appears to involve cytoprotection on the...

Journal: :Neuron 2000
Kaspar Vogt Jack Mellor Gang Tong Roger Nicoll

Zn2+ is present at high concentrations in the synaptic vesicles of hippocampal mossy fibers. We have used Zn2+ chelators and the mocha mutant mouse to address the physiological role of Zn2+ in this pathway. Zn2+ is not involved in the unique presynaptic plasticities observed at mossy fiber synapses but is coreleased with glutamate from these synapses, both spontaneously and with electrical stim...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2017
Sunday A Abiria Grigory Krapivinsky Rajan Sah Ana G Santa-Cruz Dipayan Chaudhuri Jin Zhang Pichet Adstamongkonkul Paul G DeCaen David E Clapham

TRPM7 (transient receptor potential cation channel subfamily M member 7) regulates gene expression and stress-induced cytotoxicity and is required in early embryogenesis through organ development. Here, we show that the majority of TRPM7 is localized in abundant intracellular vesicles. These vesicles (M7Vs) are distinct from endosomes, lysosomes, and other familiar vesicles or organelles. M7Vs ...

Journal: :The Journal of General Physiology 1998
Tsung-Yu Chen

Extracellular Zn2+ was found to reversibly inhibit the ClC-0 Cl- channel. The apparent on and off rates of the inhibition were highly temperature sensitive, suggesting an effect of Zn2+ on the slow gating (or inactivation) of ClC-0. In the absence of Zn2+, the rate of the slow-gating relaxation increased with temperature, with a Q10 of approximately 37. Extracellular Zn2+ facilitated the slow-g...

2014
Susumu Koyama Munechika Enjoji Mark S. Brodie Sarah B. Appel

Ventral tegmental area dopamine (DA VTA) neurons are important for the reinforcing effects of drugs of abuse such as ethanol and nicotine. We have previously shown that M-current (IM) regulates the excitability of DA VTA neurons. Zinc (Zn2+) contributes to the regulation of neuronal excitation as a neuromodulator. In the present study, we investigated zinc effect on the properties of IM and the...

Journal: :Biotechnology and bioengineering 2009
Tyler S Radniecki Lewis Semprini Mark E Dolan

The effects of ZnCl2 additions on a mercuric reductase, merA, ammonia monooxygenase, amoA, and hydroxylamine (NH2OH) oxidoreductase, hao, gene expression were examined in continuously cultured Nitrosomonas europaea cells. The reactor was operated for 85 days with a 6.9 d hydraulic retention time and with four successive additions of ZnCl2 achieving maximum concentrations from 3 to 90 microM Zn2...

2017
Li Li Shi Bai Christian T. Sheline

Zinc (Zn2+) is involved in both type 1 diabetes (T1DM) and type 2 diabetes (T2DM). The wild-type (WT) form of the β-cell-specific Zn2+ transporter, ZNT8, is linked to T2DM susceptibility. ZnT8 null mice have a mild phenotype with a slight decrease in glucose tolerance, whereas patients with the ZnT8 R325W polymorphism (rs13266634) have decreased proinsulin staining and susceptibility to T2DM. W...

Journal: :Molecular pharmacology 1998
R J Vandenberg A D Mitrovic G A Johnston

Zinc ions (Zn2+) are stored in synaptic vesicles with glutamate in a number of regions of the brain. When released into the synapse, Zn2+ modulates the activity of various receptors and ion channels. Excitatory amino acid transporters (EAATs) maintain extracellular glutamate concentrations below toxic levels and regulate the kinetics of glutamate receptor activation. We have investigated the ac...

2005
F. PARRISH R. FAIR

The relative binding affinity of Zn2+ to several glycosaminoglycans was determined by gel-filtration chromatography. Binding was observed only between Zn2+ and heparin. No binding was observed between Zn2+ and chondroitin 4-sulphate, chondroitin 6-sulphate, dermatan sulphate or hyaluronic acid. All of the glycosaminoglycans contained carboxy groups, but only heparin bound Zn2+. This observation...

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