Neuroglobin and cytoglobin are new members of the heme-globin family. Both globins are primarily expressed in neurons of the brain and retina. Neuroglobin and cytoglobin have been suggested as novel therapeutic targets in various neurodegenerative diseases based on their oxygen binding and cell protecting properties. However, findings in Neuroglobin-deficient mice question the endogenous neuroprotective properties. The expression pattern of neuroglobin and cytoglobin in the rodent brain is also in contradiction to a major role of neuronal protection. In a recent study, neuroglobin was ubiquitously expressed and up-regulated following stroke in the human brain. The present study aimed at confirming our previous observations in rodents using two post-mortem human brains. The anatomical localization of neuroglobin and cytoglobin in the human brain is much like what has been described for the rodent brain. Neuroglobin is highly expressed in the hypothalamus, amygdale and in the pontine tegmental nuclei, but not in the hippocampus. Cytoglobin is highly expressed in the habenula, hypothalamus, thalamus, hippocampus and the pontine tegmental nuclei. We only detected a low expression of neuroglobin and cytoglobin in the cerebral cortex, while no expression in the cerebellar cortex was detectable. We provide a neuroanatomical indication for a different role of neuroglobin and cytoglobin in the human brain.
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http://dx.doi.org/10.1007/s00429-012-0480-8 | DOI Listing |
J Comput Chem
April 2024
Chemistry Department, Southern Methodist University, Dallas, Texas, USA.
We investigated the intrinsic strength of distal and proximal FeN bonds for both ferric and ferrous oxidation states of bishistidyl hemoproteins from bacteria, animals, human, and plants, including two cytoglobins, ten hemoglobins, two myoglobins, six neuroglobins, and six phytoglobins. As a qualified measure of bond strength, we used local vibrational force constants k (FeN) based on local mode theory developed in our group. All calculations were performed with a hybrid QM/MM ansatz.
View Article and Find Full Text PDFInt J Mol Sci
November 2023
Frontiers of Innovative Research in Science and Technology (FIRST), Konan University, Minatojima-Minamimachi, Chuo-ku, Kobe 605-0047, Japan.
Globins have been studied as model proteins to elucidate the principles of protein evolution. This was achieved by understanding the relationship between amino acid sequence, three-dimensional structure, physicochemical properties, and physiological function. Previous molecular phylogenies of chordate globin genes revealed the monophyletic evolution of urochordate globins and suggested convergent evolution.
View Article and Find Full Text PDFPLoS Biol
May 2023
Australian Research Council Centre of Excellence for Coral Reef Studies, James Cook University, Townsville, Australia.
Connectivity of coral reef fish populations relies on successful dispersal of a pelagic larval phase. Pelagic larvae must exhibit high swimming abilities to overcome ocean and reef currents, but once settling onto the reef, larvae transition to endure habitats that become hypoxic at night. Therefore, coral reef fish larvae must rapidly and dramatically shift their physiology over a short period of time.
View Article and Find Full Text PDFJ Chem Phys
March 2023
Department of Chemistry, University of Basel, Klingelbergstrasse 80, CH-4056 Basel, Switzerland.
The transport of ligands, such as NO or O, through internal cavities is essential for the function of globular proteins, including hemoglobin, myoglobin (Mb), neuroglobin, truncated hemoglobins, or cytoglobin. For Mb, several internal cavities (Xe1 through Xe4) were observed experimentally and they were linked to ligand storage. The present work determines barriers for xenon diffusion and relative stabilization energies for the ligand in the initial and final pocket, linking a transition depending on the occupancy state of the remaining pockets from both biased and unbiased molecular dynamics simulations.
View Article and Find Full Text PDFAdv Exp Med Biol
April 2023
Miami Valley Biotech, Lansing, NY, USA.
Nitric-oxide dioxygenases (NODs) activate and combine O with NO to form nitrate. A variety of oxygen-binding hemoglobins with associated partner reductases or electron donors function as enzymatic NODs. Kinetic and structural investigations of the archetypal two-domain microbial flavohemoglobin-NOD have illuminated an allosteric mechanism that employs selective tunnels for O and NO, gates for NO and nitrate, transient O association with ferric heme, and an O and NO-triggered, ferric heme spin crossover-driven, motion-controlled, and dipole-regulated electron-transfer switch.
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