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Neuroglobin
Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging. 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 photosynthetic acoel as well as radiata such as jellyfish. In addition to neurons, neuroglobin is present in astrocytes in certain pathologies of the rodent brain and in the physiological seal brain. This is thought to be due to convergent evolution. It is of ancient evolutionary origin, and is homologous to nerve globin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Globin
The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group. They are widely distributed in many organisms. Structure Globin superfamily members share a common three-dimensional fold. This 'globin fold' typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini. Since the globin fold contains only helices, it is classified as an all-alpha protein fold. The globin fold is found in its namesake globin families as well as in phycocyanins. The globin fold was thus the first protein fold discovered (myoglobin was the first protein whose structure was solved). Helix packaging The eight helices of the globin fold core share significant nonlocal st ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytoglobin
Cytoglobin is the protein product of CYGB, a human and mammalian gene. Cytoglobin is a globin molecule ubiquitously expressed in all tissues and most notably utilized in marine mammals. It was discovered in 2001 and named cytoglobin in 2002. It is thought to protect against hypoxia. The predicted function of cytoglobin is the transfer of oxygen from arterial blood to the brain. Function Cytoglobin is a ubiquitously expressed hexacoordinate hemoglobin that may facilitate diffusion of oxygen through tissues, scavenge nitric oxide or reactive oxygen species, or serve a protective function during oxidative stress. Applications CYGB expression can be used as a specific marker with which hepatic stellate cells can be distinguished from portal myofibroblast A myofibroblast is a cell phenotype that was first described as being in a state between a fibroblast and a smooth muscle cell. Structure Myofibroblasts are contractile web-like fusiform cells that are identifiable by th ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemoprotein
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both. The heme consists of iron cation bound at the center of the conjugate base of the porphyrin, as well as other ligands attached to the "axial sites" of the iron. The porphyrin ring is a planar dianionic, tetradentate ligand. The iron is typically Fe2+ or Fe3+. One or two ligands are attached at the axial sites. The porphyrin ring has 4 nitrogen atoms that bind to the iron, leaving two other coordination positions of the iron available for bonding to the histidine of the protein and a divalent atom. Hemeproteins probably evolved to incorporate the iron atom contained within the protoporphyrin IX rin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemoprotein
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both. The heme consists of iron cation bound at the center of the conjugate base of the porphyrin, as well as other ligands attached to the "axial sites" of the iron. The porphyrin ring is a planar dianionic, tetradentate ligand. The iron is typically Fe2+ or Fe3+. One or two ligands are attached at the axial sites. The porphyrin ring has 4 nitrogen atoms that bind to the iron, leaving two other coordination positions of the iron available for bonding to the histidine of the protein and a divalent atom. Hemeproteins probably evolved to incorporate the iron atom contained within the protoporphyrin IX rin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Jellyfish
Jellyfish and sea jellies are the informal common names given to the medusa-phase of certain gelatinous members of the subphylum Medusozoa, a major part of the phylum Cnidaria. Jellyfish are mainly free-swimming marine animals with umbrella-shaped bells and trailing tentacles, although a few are anchored to the seabed by stalks rather than being mobile. The bell can pulsate to provide propulsion for highly efficient animal locomotion, locomotion. The tentacles are armed with Cnidocyte, stinging cells and may be used to capture prey and defend against predators. Jellyfish have a complex Biological life cycle, life cycle; the medusa is normally the sexual phase, which produces planula larvae that disperse widely and enter a sedentary polyp (zoology), polyp phase before reaching sexual maturity. Jellyfish are found all over the world, from surface waters to the deep sea. Scyphozoans (the "true jellyfish") are exclusively marine habitats, marine, but some hydrozoans with a simila ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Myoglobin
Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. In humans, myoglobin is only found in the bloodstream after muscle injury. (Google books link is the 2008 edition) High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many texts consider myoglobin not to be found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells. Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Leghemoglobin
3rd Leghemoglobin (also leghaemoglobin or legoglobin) is an oxygen-carrying phytoglobin found in the nitrogen-fixing root nodules of leguminous plants. It is produced by these plants in response to the roots being colonized by nitrogen-fixing bacteria, termed rhizobia, as part of the symbiotic interaction between plant and bacterium: roots not colonized by ''Rhizobium'' do not synthesise leghemoglobin. Leghemoglobin has close chemical and structural similarities to hemoglobin, and, like hemoglobin, is red in colour. It was originally thought that the heme prosthetic group for plant leghemoglobin was provided by the bacterial symbiont within symbiotic root nodules. However, subsequent work shows that the plant host strongly expresses heme biosynthesis genes within nodules, and that activation of those genes correlates with leghemoglobin gene expression in developing nodules. In plants colonised by ''Rhizobium'', such as alfalfa or soybeans, the presence of oxygen in the root nodu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hemoglobin
Hemoglobin (haemoglobin BrE) (from the Greek word αἷμα, ''haîma'' 'blood' + Latin ''globus'' 'ball, sphere' + ''-in'') (), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein present in red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the respiratory organs (''e.g.'' lungs or gills) to the rest of the body (''i.e.'' tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power functions of an organism in the process called metabolism. A healthy individual human has 12to 20grams of hemoglobin in every 100mL of blood. In mammals, the chromoprotein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL O2 per gram, which increases the total blood oxygen ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carbon Monoxide
Carbon monoxide (chemical formula CO) is a colorless, poisonous, odorless, tasteless, flammable gas that is slightly less dense than air. Carbon monoxide consists of one carbon atom and one oxygen atom connected by a triple bond. It is the simplest molecule of the oxocarbon family. In coordination complexes the carbon monoxide ligand is called carbonyl. It is a key ingredient in many processes in industrial chemistry. The most common source of carbon monoxide is the partial combustion of carbon-containing compounds, when insufficient oxygen or heat is present to produce carbon dioxide. There are also numerous environmental and biological sources that generate and emit a significant amount of carbon monoxide. It is important in the production of many compounds, including drugs, fragrances, and fuels. Upon emission into the atmosphere, carbon monoxide affects several processes that contribute to climate change. Carbon monoxide has important biological roles across phylogenetic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Murine
The Old World rats and mice, part of the subfamily Murinae in the family Muridae, comprise at least 519 species. Members of this subfamily are called murines. In terms of species richness, this subfamily is larger than all mammal families except the Cricetidae and Muridae, and is larger than all mammal orders except the bats and the remainder of the rodents. Description The Murinae are native to Africa, Europe, Asia, and Australia. They are terrestrial placental mammals. They have also been introduced to all continents except Antarctica, and are serious pest animals. This is particularly true in island communities where they have contributed to the endangerment and extinction of many native animals. Two prominent murine species have become vital laboratory animals: the brown rat and house mouse are both used as medical subjects. The murines have a distinctive molar pattern that involves three rows of cusps instead of two, the primitive pattern seen most frequently in mur ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Convergent Evolution
Convergent evolution is the independent evolution of similar features in species of different periods or epochs in time. Convergent evolution creates analogous structures that have similar form or function but were not present in the last common ancestor of those groups. The cladistic term for the same phenomenon is homoplasy. The recurrent evolution of flight is a classic example, as flying insects, birds, pterosaurs, and bats have independently evolved the useful capacity of flight. Functionally similar features that have arisen through convergent evolution are ''analogous'', whereas '' homologous'' structures or traits have a common origin but can have dissimilar functions. Bird, bat, and pterosaur wings are analogous structures, but their forelimbs are homologous, sharing an ancestral state despite serving different functions. The opposite of convergence is divergent evolution, where related species evolve different traits. Convergent evolution is similar to parallel evo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pinniped
Pinnipeds (pronounced ), commonly known as seals, are a widely distributed and diverse clade of carnivorous, fin-footed, semiaquatic, mostly marine mammals. They comprise the extant families Odobenidae (whose only living member is the walrus), Otariidae (the eared seals: sea lions and fur seals), and Phocidae (the earless seals, or true seals). There are 34 extant species of pinnipeds, and more than 50 extinct species have been described from fossils. While seals were historically thought to have descended from two ancestral lines, molecular evidence supports them as a monophyletic lineage (descended from one ancestral line). Pinnipeds belong to the order Carnivora; their closest living relatives are musteloids (weasels, raccoons, skunks, and red pandas), having diverged about 50 million years ago. Seals range in size from the and Baikal seal to the and southern elephant seal male, which is also the largest member of the order Carnivora. Several species exh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
