Neuronal regulation of expression of hydrogen sulfide-producing enzyme cystathionine β-synthase in rat spinal cord astrocytes. (August 2015)
- Record Type:
- Journal Article
- Title:
- Neuronal regulation of expression of hydrogen sulfide-producing enzyme cystathionine β-synthase in rat spinal cord astrocytes. (August 2015)
- Main Title:
- Neuronal regulation of expression of hydrogen sulfide-producing enzyme cystathionine β-synthase in rat spinal cord astrocytes
- Authors:
- Miyamoto, Ryo
Otsuguro, Ken-ichi
Yamaguchi, Soichiro
Ito, Shigeo - Abstract:
- Highlights: In the rat spinal cord, an H2 S-producing enzyme, CBS is localized to astrocytes. Neuronal loss is accompanied by reduction of astrocytic CBS expression. Reduced astrocytic CBS expression is restored by co-culture with neuron. Abstract: Cystathionine β-synthase (CBS), expressed in astrocytes, generates a gaseous neuromodulator, hydrogen sulfide (H2 S) in the central nervous system (CNS). However, little is known about the regulatory mechanisms of astrocytic CBS expression and activity. This study evaluated the influence of neurons on astrocytic CBS expression by employing multiple culture systems. Substantial CBS expression was observed in the intact neonatal rat spinal cord, while CBS content was markedly reduced in an astrocyte-enriched culture prepared from the neonatal spinal cord. Immunofluorescence analysis confirmed the localization of spinal cord CBS in astrocytes, but not in neurons. Although CBS expression was weak in the embryonic rat spinal cord, enzyme levels were time-dependently increased in a neuron/astrocyte mixed culture originating from embryonic spinal cord. The reduced CBS expression in isolated neonatal astrocytes was restored by co-culture with embryonic neurons. Together with the observed CBS expression levels, H2 S production was relatively low in astrocytes cultured alone, but was considerably higher in astrocytes cultured with neurons. These results indicate that neurons are essential for maintaining the expression and H2 S-producingHighlights: In the rat spinal cord, an H2 S-producing enzyme, CBS is localized to astrocytes. Neuronal loss is accompanied by reduction of astrocytic CBS expression. Reduced astrocytic CBS expression is restored by co-culture with neuron. Abstract: Cystathionine β-synthase (CBS), expressed in astrocytes, generates a gaseous neuromodulator, hydrogen sulfide (H2 S) in the central nervous system (CNS). However, little is known about the regulatory mechanisms of astrocytic CBS expression and activity. This study evaluated the influence of neurons on astrocytic CBS expression by employing multiple culture systems. Substantial CBS expression was observed in the intact neonatal rat spinal cord, while CBS content was markedly reduced in an astrocyte-enriched culture prepared from the neonatal spinal cord. Immunofluorescence analysis confirmed the localization of spinal cord CBS in astrocytes, but not in neurons. Although CBS expression was weak in the embryonic rat spinal cord, enzyme levels were time-dependently increased in a neuron/astrocyte mixed culture originating from embryonic spinal cord. The reduced CBS expression in isolated neonatal astrocytes was restored by co-culture with embryonic neurons. Together with the observed CBS expression levels, H2 S production was relatively low in astrocytes cultured alone, but was considerably higher in astrocytes cultured with neurons. These results indicate that neurons are essential for maintaining the expression and H2 S-producing activity of astrocytic CBS in the rat spinal cord. … (more)
- Is Part Of:
- Neuroscience research. Volume 97(2015:Aug.)
- Journal:
- Neuroscience research
- Issue:
- Volume 97(2015:Aug.)
- Issue Display:
- Volume 97 (2015)
- Year:
- 2015
- Volume:
- 97
- Issue Sort Value:
- 2015-0097-0000-0000
- Page Start:
- 52
- Page End:
- 59
- Publication Date:
- 2015-08
- Subjects:
- AraC cytosine arabinoside -- CAT cysteine aminotransferase -- CBS cystathionine β-synthase -- CSE cystathionine γ-lyase -- GFAP glial fibrillary acidic protein -- H2S hydrogen sulfide -- MAP-2 microtubule-associated protein 2 -- MPST mercaptopyruvate sulfurtransferase -- PGP 9.5 protein gene product 9.5 -- Tuj-1 β-III-tubulin
Astrocyte -- Cystathionine β-synthase -- Homocysteine -- Hydrogen sulfide -- Neuron
Neurosciences -- Research -- Periodicals
Neurosciences -- Research -- Japan -- Periodicals
Neurology -- Periodicals
Neurosciences -- Periodicals
Neurosciences -- Recherche -- Périodiques
Neurosciences -- Recherche -- Japon -- Périodiques
Neurosciences -- Research
Japan
Periodicals
612.8 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01680102 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.neures.2015.03.003 ↗
- Languages:
- English
- ISSNs:
- 0168-0102
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6081.563600
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