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Zoology and wildlife conservation

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Abstracts » Zoology and wildlife conservation

Endothelial nitric oxide synthase and LTP

Article Abstract:

Long-term potentiation (LTP) is defective in hippocampal slices from mice lacking functional endothelial nitric oxide synthase (eNOS) and from wild-type mice treated with a NOS inhibitor. The maintenance of LTP in the hippocampus also appears to require the endothelial isoform of NOS. This was gleaned from an examination of LTP induction in the hippocampal CA1 region, where NO synthesized in the dendrites of pyramidal cells may transport retrograde signals from the post-synaptic to the presynaptic terminals. Results support the hypothesis that NO synthesized by eNOS in post-synaptic CA1 pyramidal cells acts as a retrograde messenger necessary for the long-term maintenance of potentiation induced by weak stimuli.

Author: Wilson, Rachel I., Stevens, David R., Yanovsky, Jevgenij, Godecke, Axel, Schrader, Jurgen, Haas, Helmut L.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
Endothelium, Cytology, Hippocampus (Brain)

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The haemoglobin enzyme

Article Abstract:

It has been established that haemoglobin from a parasitic nematode, Ascaris suum, is a true enzyme, acting as a nitric oxide (NO)-activated deoxygenase. It is suggested that Ascaris haemoglobin is an NO-dependent deoxygenase which uses endogenously produced NO as a substrate to detoxify oxygen. It seems that the physiological function of Ascaris haemoglobin is to eliminate oxygen, rather than supply it. The deoxygenase activity eliminates oxygen toxicity by keeping tissues extremely anaerobic.

Author: Imai, Kiyohiro
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
Research, Oxidases, Hemoglobin synthesis

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Dynamics of haemoglobin

Article Abstract:

Normal levels of haemoglobin with haem-bound nitric oxide (NO) in vivo may be detected in venous blood of animals exposed to oxidative stress. These levels are too low in vivo to be detected by direct measurements. Two NO molecules interact with haem in deoxygenated haemmoglobin in venous blood in vivo to form haem-bound NO. The haems that participate in this interaction are those in the alpha-chains.

Author: Day, Billy W., Kagan, Valerian E., Elsayed, Nabil M., Gorbunov, Nikolai V.
Publisher: Macmillan Publishing Ltd.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
Hemoglobin, Hemoglobins, Animals, Heme, Veins

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Subjects list: Analysis, Physiological aspects, Nitric oxide
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