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'''Neuroglobin''' is a member of the vertebrate [[globin]] family involved in cellular oxygen [[homeostasis]]. It is an intracellular [[hemoprotein]] expressed in the central and peripheral nervous system, [[cerebrospinal fluid]], [[retina]] and [[endocrine system|endocrine]] tissues. Neuroglobin is a [[monomer]] that reversibly binds oxygen with an affinity higher than that of [[hemoglobin]]. It also increases oxygen availability to brain tissue and provides protection under [[hypoxia (medical)|hypoxic]] or [[ischemia|ischemic]] conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated [[protostome]]s, like [[photosynthesis]] [[acoel]] as well as [[radiata]] such as [[jelly fish]]. In addition to neurons, neuroglobin is present in [[astrocytes]] in certain pathologies of the rodent brain<ref>{{cite journal |vauthors=DellaValle B, Hempel C, Kurtzhals JA, Penkowa M |title=In vivo expression of neuroglobin in reactive astrocytes during neuropathology in murine models of traumatic brain injury, cerebral malaria, and autoimmune encephalitis |journal=Glia |volume=58 |issue=10 |pages=1220–7 | date=August  2010 |pmid=20544857 |doi=10.1002/glia.21002}}</ref><ref>{{cite journal  |vauthors=De Marinis E, Acaz-Fonseca E, Arevalo MA, etal |title=17β-Oestradiol anti-inflammatory effects in primary astrocytes require oestrogen receptor β-mediated neuroglobin up-regulation |journal=Journal of Neuroendocrinology |volume=25 |issue=3 |pages=260–70 | date=March  2013 |pmid=23190172 |doi=10.1111/jne.12007}}</ref> and in the physiological [[Pinniped|seal]] brain.<ref>{{cite journal  |vauthors=Mitz SA, Reuss S, Folkow LP, etal |title=When the brain goes diving: glial oxidative metabolism may confer hypoxia tolerance to the seal brain |journal=Neuroscience |volume=163 |issue=2 |pages=552–60 | date=October  2009 |pmid=19576963 |doi=10.1016/j.neuroscience.2009.06.058}}</ref> This is thought to be due to [[convergent evolution]].<ref>[http://www.science.gov/topicpages/c/clytia+hemisphaerica+cnidaria.html science.gov, Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity] by Lechauve, Christophe; Jager, Muriel; Laguerre, Laurent; Kiger, Laurent; Correc, Gaelle; Leroux, Cedric; Vinogradov, Serge; Czjzek, Mirjam; Marden, Michael C.; Bail</ref> It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Recent research on Neuroglobin presence confirmed that Human neuroglobin protein in [[cerebrospinal fluid]] (CSF).<ref>{{cite journal |vauthors=Casado B, Pannell LK, Whalen G, Clauw DJ, Baraniuk JN |title=Human neuroglobin protein in cerebrospinal fluid |journal=Proteome Science |volume=3 |issue=1 |pages=2 | date=February  2005 |pmid=15730566 |pmc=554085 |doi=10.1186/1477-5956-3-2}}</ref>
'''Neuroglobin''' is a member of the vertebrate [[globin]] family involved in cellular oxygen [[homeostasis]]. It is an intracellular [[hemoprotein]] expressed in the central and peripheral nervous system, [[cerebrospinal fluid]], [[retina]] and [[endocrine system|endocrine]] tissues. Neuroglobin is a [[monomer]] that reversibly binds oxygen with an affinity higher than that of [[hemoglobin]]. It also increases oxygen availability to brain tissue and provides protection under [[hypoxia (medical)|hypoxic]] or [[ischemia|ischemic]] conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated [[protostome]]s, like [[photosynthesis]] [[acoel]] as well as [[radiata]] such as [[jelly fish]]. In addition to neurons, neuroglobin is present in [[astrocytes]] in certain pathologies of the rodent brain<ref>{{cite journal |vauthors=DellaValle B, Hempel C, Kurtzhals JA, Penkowa M |title=In vivo expression of neuroglobin in reactive astrocytes during neuropathology in murine models of traumatic brain injury, cerebral malaria, and autoimmune encephalitis |journal=Glia |volume=58 |issue=10 |pages=1220–7 | date=August  2010 |pmid=20544857 |doi=10.1002/glia.21002}}</ref><ref>{{cite journal  |vauthors=De Marinis E, Acaz-Fonseca E, Arevalo MA, etal |title=17β-Oestradiol anti-inflammatory effects in primary astrocytes require oestrogen receptor β-mediated neuroglobin up-regulation |journal=Journal of Neuroendocrinology |volume=25 |issue=3 |pages=260–70 | date=March  2013 |pmid=23190172 |doi=10.1111/jne.12007|url=https://digital.csic.es/bitstream/10261/73308/1/accesoRestringido.pdf |format=Submitted manuscript }}</ref> and in the physiological [[Pinniped|seal]] brain.<ref>{{cite journal  |vauthors=Mitz SA, Reuss S, Folkow LP, etal |title=When the brain goes diving: glial oxidative metabolism may confer hypoxia tolerance to the seal brain |journal=Neuroscience |volume=163 |issue=2 |pages=552–60 | date=October  2009 |pmid=19576963 |doi=10.1016/j.neuroscience.2009.06.058}}</ref> This is thought to be due to [[convergent evolution]].<ref>[http://www.science.gov/topicpages/c/clytia+hemisphaerica+cnidaria.html science.gov, Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity] by Lechauve, Christophe; Jager, Muriel; Laguerre, Laurent; Kiger, Laurent; Correc, Gaelle; Leroux, Cedric; Vinogradov, Serge; Czjzek, Mirjam; Marden, Michael C.; Bail</ref> It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Recent research confirmed the presence of human neuroglobin protein in [[cerebrospinal fluid]] (CSF).<ref>{{cite journal |vauthors=Casado B, Pannell LK, Whalen G, Clauw DJ, Baraniuk JN |title=Human neuroglobin protein in cerebrospinal fluid |journal=Proteome Science |volume=3 |issue=1 |pages=2 | date=February  2005 |pmid=15730566 |pmc=554085 |doi=10.1186/1477-5956-3-2|url=https://deepblue.lib.umich.edu/bitstream/2027.42/112428/1/12953_2004_Article_18.pdf }}</ref>


Neuroglobin was first identified by Thorsten Burmester ''et al.'' in 2000.<ref>{{cite journal |vauthors=Burmester T, Weich B, Reinhardt S, Hankeln T |title=A vertebrate globin expressed in the brain |journal=Nature |volume=407 |issue=6803 |pages=520–3 | date=September  2000 |pmid=11029004 |doi=10.1038/35035093}}</ref>  
Neuroglobin was first identified by Thorsten Burmester ''et al.'' in 2000.<ref>{{cite journal |vauthors=Burmester T, Weich B, Reinhardt S, Hankeln T |title=A vertebrate globin expressed in the brain |journal=Nature |volume=407 |issue=6803 |pages=520–3 | date=September  2000 |pmid=11029004 |doi=10.1038/35035093}}</ref>


The 3D structure of human neuroglobin was determined in 2003.<ref>{{cite journal |title=Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity |author=Alessandra Pesce |author2=Sylvia Dewilde |author3=Marco Nardini |author4=Luc Moens |author5=Paolo Ascenzi |author6=Thomas Hankeln |author7=Thorsten Burmester |author8=Martino Bolognes |last-author-amp=yes |doi=10.1016/S0969-2126(03)00166-7 |journal=Structure |volume=11 |issue=9 |year=2003 |pages=1087–1095 |pmid=12962627}}</ref> The next year, [[murine]] neuroglobin was determined at a higher resolution.<ref>{{cite journal |journal=Proteins: Structure, Function, and Bioinformatics |volume=56 |issue=1 |pages=85–92 |year=2004 |doi=10.1002/prot.20113 |title=The structure of murine neuroglobin: Novel pathways for ligand migration and binding |author1=Beatrice Vallone |author2=Karin Nienhaus |author3=Maurizio Brunori |author4=G. Ulrich Nienhaus |pmid=15162488}}</ref>
The 3D structure of human neuroglobin was determined in 2003.<ref>{{cite journal |title=Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity |author=Alessandra Pesce |author2=Sylvia Dewilde |author3=Marco Nardini |author4=Luc Moens |author5=Paolo Ascenzi |author6=Thomas Hankeln |author7=Thorsten Burmester |author8=Martino Bolognes |last-author-amp=yes |doi=10.1016/S0969-2126(03)00166-7 |journal=Structure |volume=11 |issue=9 |year=2003 |pages=1087–1095 |pmid=12962627}}</ref> The next year, [[murine]] neuroglobin was determined at a higher resolution.<ref>{{cite journal |journal=Proteins: Structure, Function, and Bioinformatics |volume=56 |issue=1 |pages=85–92 |year=2004 |doi=10.1002/prot.20113 |title=The structure of murine neuroglobin: Novel pathways for ligand migration and binding |author1=Beatrice Vallone |author2=Karin Nienhaus |author3=Maurizio Brunori |author4=G. Ulrich Nienhaus |pmid=15162488}}</ref>
A practical treatment for [[carbon monoxide]] poisoning based on binding of CO by neuroglobin (Ngb) with a mutated distal histidine (H64Q) appears to be possible.<ref>{{cite journal |pmid=29566507 |doi=10.1063/1.5013659|year=2018|last1=Rydzewski|first1=J|title=Photoinduced transport in an H64Q neuroglobin antidote for carbon monoxide poisoning|journal=The Journal of Chemical Physics|volume=148|issue=11|pages=115101|last2=Nowak|first2=W}}</ref>


==See also==
==See also==

Revision as of 15:40, 30 October 2018

Neuroglobin
File:Neuroglobin.png
Model of murine neuroglobin from PDB: 1Q1F​
Identifiers
SymbolNGB
Entrez58157
HUGO6553
OMIM605304
UniProtQ9NPG2
Other data
LocusChr. 14 q24

Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues. Neuroglobin is a monomer that reversibly binds oxygen with an affinity higher than that of hemoglobin. It also increases oxygen availability to brain tissue and provides protection under hypoxic or ischemic conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated protostomes, like photosynthesis acoel as well as radiata such as jelly fish. In addition to neurons, neuroglobin is present in astrocytes in certain pathologies of the rodent brain[1][2] and in the physiological seal brain.[3] This is thought to be due to convergent evolution.[4] It is of ancient evolutionary origin, and is homologous to nerve globins of invertebrates. Recent research confirmed the presence of human neuroglobin protein in cerebrospinal fluid (CSF).[5]

Neuroglobin was first identified by Thorsten Burmester et al. in 2000.[6]

The 3D structure of human neuroglobin was determined in 2003.[7] The next year, murine neuroglobin was determined at a higher resolution.[8]

A practical treatment for carbon monoxide poisoning based on binding of CO by neuroglobin (Ngb) with a mutated distal histidine (H64Q) appears to be possible.[9]

See also

References

  1. ↑ DellaValle B, Hempel C, Kurtzhals JA, Penkowa M (August 2010). "In vivo expression of neuroglobin in reactive astrocytes during neuropathology in murine models of traumatic brain injury, cerebral malaria, and autoimmune encephalitis". Glia. 58 (10): 1220–7. doi:10.1002/glia.21002. PMID 20544857.
  2. ↑ De Marinis E, Acaz-Fonseca E, Arevalo MA, et al. (March 2013). "17β-Oestradiol anti-inflammatory effects in primary astrocytes require oestrogen receptor β-mediated neuroglobin up-regulation" (Submitted manuscript). Journal of Neuroendocrinology. 25 (3): 260–70. doi:10.1111/jne.12007. PMID 23190172.
  3. ↑ Mitz SA, Reuss S, Folkow LP, et al. (October 2009). "When the brain goes diving: glial oxidative metabolism may confer hypoxia tolerance to the seal brain". Neuroscience. 163 (2): 552–60. doi:10.1016/j.neuroscience.2009.06.058. PMID 19576963.
  4. ↑ science.gov, Neuroglobins, Pivotal Proteins Associated with Emerging Neural Systems and Precursors of Metazoan Globin Diversity by Lechauve, Christophe; Jager, Muriel; Laguerre, Laurent; Kiger, Laurent; Correc, Gaelle; Leroux, Cedric; Vinogradov, Serge; Czjzek, Mirjam; Marden, Michael C.; Bail
  5. ↑ Casado B, Pannell LK, Whalen G, Clauw DJ, Baraniuk JN (February 2005). "Human neuroglobin protein in cerebrospinal fluid" (PDF). Proteome Science. 3 (1): 2. doi:10.1186/1477-5956-3-2. PMC 554085. PMID 15730566.
  6. ↑ Burmester T, Weich B, Reinhardt S, Hankeln T (September 2000). "A vertebrate globin expressed in the brain". Nature. 407 (6803): 520–3. doi:10.1038/35035093. PMID 11029004.
  7. ↑ Alessandra Pesce; Sylvia Dewilde; Marco Nardini; Luc Moens; Paolo Ascenzi; Thomas Hankeln; Thorsten Burmester & Martino Bolognes (2003). "Human Brain Neuroglobin Structure Reveals a Distinct Mode of Controlling Oxygen Affinity". Structure. 11 (9): 1087–1095. doi:10.1016/S0969-2126(03)00166-7. PMID 12962627.
  8. ↑ Beatrice Vallone; Karin Nienhaus; Maurizio Brunori; G. Ulrich Nienhaus (2004). "The structure of murine neuroglobin: Novel pathways for ligand migration and binding". Proteins: Structure, Function, and Bioinformatics. 56 (1): 85–92. doi:10.1002/prot.20113. PMID 15162488.
  9. ↑ Rydzewski, J; Nowak, W (2018). "Photoinduced transport in an H64Q neuroglobin antidote for carbon monoxide poisoning". The Journal of Chemical Physics. 148 (11): 115101. doi:10.1063/1.5013659. PMID 29566507.

External links

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