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Published on: January 19, 2013
Cytoglobin is a stress-responsive hemoprotein expressed in the developing and adult brain
Pradeep P A Mammen1, John M Shelton, Qiu Ye
1Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX 75390-8573, USA. pradeep.mammen@utsouthwestern.edu
Insights
Cytoglobin (Cygb) is a novel tissue hemoprotein. This study reveals Cygb is oxygen-responsive, expressed in specific brain regions, and may aid the brain's response to hypoxia.
Area of Science:
- Biochemistry
- Neuroscience
- Developmental Biology
Background:
- Cytoglobin (Cygb) is a novel tissue hemoprotein with structural similarities to myoglobin (Mb).
- Its precise physiological functions, particularly in oxygen and nitric oxide metabolism or free radical scavenging, remain under investigation.
- Understanding Cygb's role requires examining its expression patterns during development and in response to physiological stimuli.
Purpose of the Study:
- To investigate the spatial and temporal expression patterns of Cytoglobin (Cygb) during murine embryogenesis.
- To compare Cygb expression with myoglobin (Mb) and neuroglobin (Ngb) in the developing and adult brain.
- To determine if Cygb expression is modulated by hypoxic conditions.
Main Methods:
- In situ hybridization
- RT-PCR
- Northern blot analyses
Main Results:
- Limited Cygb expression was observed during embryogenesis, primarily in the central nervous system and neural crest derivatives.
- In adult mice, Cygb expression was detected in distinct brain regions (hippocampus, thalamus, hypothalamus) compared to Ngb.
- Chronic hypoxia induced Cygb expression in the brain, unlike Ngb.
Conclusions:
- Cytoglobin (Cygb) is an oxygen-responsive tissue hemoprotein.
- It is expressed in specific regions of the normoxic and hypoxic brain.
- Cygb may play a crucial role in the brain's response to hypoxic insults.
Abstract:
Cytoglobin (Cygb) is a novel tissue hemoprotein relatively similar to myoglobin (Mb). Because Cygb shares several structural features with Mb, we hypothesized that Cygb functions in the modulation of oxygen and nitric oxide metabolism or in scavenging free radicals within a cell. In the present study we examined the spatial and temporal expression pattern of Cygb during murine embryogenesis. Using in situ hybridization, RT-PCR, and Northern blot analyses, limited Cygb expression was observed during embryogenesis compared with Mb expression. Cygb expression was primarily restricted to the central nervous system and neural crest derivatives during the latter stages of development. In the adult mouse, Cygb is expressed in distinct regions of the brain as compared with neuroglobin (Ngb), another globin protein, and these regions are responsive to oxidative stress (i.e., hippocampus, thalamus, and hypothalamus). In contrast to Ngb, Cygb expression in the brain is induced in response to chronic hypoxia (10% oxygen). These results support the hypothesis that Cygb is an oxygen-responsive tissue hemoglobin expressed in distinct regions of thenormoxic and hypoxic brain and may play a key role in the response of the brain to ahypoxic insult.
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