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Hemoglobin, or haemoglobin, abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the lungs or gills to the rest of the body. There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism. A healthy individual has 12 to 20 grams of hemoglobin in every 100 mL of blood.
Red blood cells (RBCs), also referred to as red cells, red blood corpuscles (in humans or other animals not having nucleus in red blood cells), haematids, erythroid cells or erythrocytes (from Greek erythros for "red" and kytos for "hollow vessel", with -cyte translated as "cell" in modern usage), are the most common type of blood cell and the vertebrate's principal means of delivering oxygen (O2) to the body tissues—via blood flow through the circulatory system. RBCs take up oxygen in the lungs, or in fish the gills, and release it into tissues while squeezing through the body's capillaries.
Myoglobin is an iron- and oxygen-binding protein found in the 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. But at the core, it is an oxygen-binding protein in red blood cells. In humans, myoglobin is only found in the bloodstream after muscle injury.
Leghemoglobin 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.
Heme, or haem is a substance precursive to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver.
Molecular binding is an interaction between molecules that results in a stable physical association between those molecules. Cooperative binding occurs in binding systems containing more than one type, or species, of molecule and in which one of the partners is not mono-valent and can bind more than one molecule of the other species.
The swim bladder, gas bladder, fish maw, or air bladder is an internal gas-filled organ that contributes to the ability of many bony fish to control their buoyancy, and thus to stay at their current water depth without having to waste energy in swimming. Also, the dorsal position of the swim bladder means the center of mass is below the center of volume, allowing it to act as a stabilizing agent. Additionally, the swim bladder functions as a resonating chamber, to produce or receive sound.
A rete mirabile is a complex of arteries and veins lying very close to each other, found in some vertebrates, mainly warm-blooded ones. The rete mirabile utilizes countercurrent blood flow within the net to act as a countercurrent exchanger. It exchanges heat, ions, or gases between vessel walls so that the two bloodstreams within the rete maintain a gradient with respect to temperature, or concentration of gases or solutes. This term was coined by Galen.
Fetal hemoglobin, or foetal haemoglobin is the main oxygen carrier protein in the human fetus. Hemoglobin F is found in fetal red blood cells, and is involved in transporting oxygen from the mother's bloodstream to organs and tissues in the fetus. It is produced at around 6 weeks of pregnancy and the levels remain high after birth until the baby is roughly 2–4 months old. Hemoglobin F has a different composition from the adult forms of hemoglobin, which allows it to bind oxygen more strongly. This way, the developing fetus is able to retrieve oxygen from the mother's bloodstream, which occurs through the placenta found in the mother's uterus.
The Bohr effect is a phenomenon first described in 1904 by the Danish physiologist Christian Bohr. Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment. Since carbon dioxide reacts with water to form carbonic acid, an increase in CO2 results in a decrease in blood pH, resulting in hemoglobin proteins releasing their load of oxygen. Conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen.
The crocodile icefish or white-blooded fish comprise a family (Channichthyidae) of notothenioid fishes found in the Southern Ocean around Antarctica. They are the only known vertebrates to lack hemoglobin in their blood as adults. Icefish populations are known to reside in the Atlantic and Indian sectors of the Southern Ocean, as well as the continental shelf waters surrounding Antarctica. Water temperatures in these regions remain relatively stable, generally ranging from −1.8 to 2 °C. One icefish, Champsocephalus esox, is distributed north of the Antarctic Polar Frontal Zone. At least 16 species of crocodile icefish are currently recognized, although eight additional species have been proposed for the icefish genus Channichthys.
Carboxyhemoglobin, or carboxyhaemoglobin, is a stable complex of carbon monoxide and hemoglobin (Hb) that forms in red blood cells upon contact with carbon monoxide. Carboxyhemoglobin is often mistaken for the compound formed by the combination of carbon dioxide (carboxyl) and hemoglobin, which is actually carbaminohemoglobin. Carboxyhemoglobin terminology emerged when carbon monoxide was known by its ancient name carbonic oxide; the preferred IUPAC nomenclature is carbonylhemoglobin.
A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O2 transport. Other functions performed include O2 storage, CO2 transport, and transportation of substances other than respiratory gases. There are four major classifications of respiratory pigment: hemoglobin, hemocyanin, erythrocruorin–chlorocruorin, and hemerythrin. The heme-containing globin is the most commonly-occurring respiratory pigment, occurring in at least 9 different phyla of animals.
The oxygen–hemoglobin dissociation curve, also called the oxyhemoglobin dissociation curve or oxygen dissociation curve (ODC), is a curve that plots the proportion of hemoglobin in its saturated (oxygen-laden) form on the vertical axis against the prevailing oxygen tension on the horizontal axis. This curve is an important tool for understanding how our blood carries and releases oxygen. Specifically, the oxyhemoglobin dissociation curve relates oxygen saturation (SO2) and partial pressure of oxygen in the blood (PO2), and is determined by what is called "hemoglobin affinity for oxygen"; that is, how readily hemoglobin acquires and releases oxygen molecules into the fluid that surrounds it.
Notothenioidei is one of 19 suborders from the order Perciformes and that primarily includes Antarctic fish and Subantarctic fish, but also a few species ranging north to southern Australia and southern South America. These species, which are referred to collectively as the notothenioids, account for approximately 90% of the fish fauna biomass in the continental shelf waters surrounding Antarctica.
The Haldane effect is a property of hemoglobin first described by John Scott Haldane, within which oxygenation of blood in the lungs displaces carbon dioxide from hemoglobin, increasing the removal of carbon dioxide. Consequently, oxygenated blood has a reduced affinity for carbon dioxide. Thus, the Haldane effect describes the ability of hemoglobin to carry increased amounts of carbon dioxide (CO2) in the deoxygenated state as opposed to the oxygenated state. A high concentration of CO2 facilitates dissociation of oxyhemoglobin.
2,3-Bisphosphoglyceric acid (2,3-BPG), also known as 2,3-diphosphoglyceric acid (2,3-DPG), is a three-carbon isomer of the glycolytic intermediate 1,3-bisphosphoglyceric acid (1,3-BPG). 2,3-BPG is present in human red blood cells at approximately 5 mmol/L. It binds with greater affinity to deoxygenated hemoglobin than it does to oxygenated hemoglobin due to conformational differences: 2,3-BPG fits in the deoxygenated hemoglobin conformation, but not as well in the oxygenated conformation. It interacts with deoxygenated hemoglobin beta subunits and so it decreases the affinity for oxygen and allosterically promotes the release of the remaining oxygen molecules bound to the hemoglobin; therefore it enhances the ability of RBCs to release oxygen near tissues that need it most. 2,3-BPG is thus an allosteric effector.
Organisms can live at high altitude, either on land, in water, or while flying. Decreased oxygen availability and decreased temperature make life at such altitudes challenging, though many species have been successfully adapted via considerable physiological changes. As opposed to short-term acclimatisation, high-altitude adaptation means irreversible, evolved physiological responses to high-altitude environments, associated with heritable behavioural and genetic changes. Among animals, only few mammals and certain birds are known to have completely adapted to high-altitude environments.
Fish are exposed to large oxygen fluctuations in their aquatic environment since the inherent properties of water can result in marked spatial and temporal differences in the concentration of oxygen (see oxygenation and underwater). Fish respond to hypoxia with varied behavioral, physiological, and cellular responses in order to maintain homeostasis and organism function in an oxygen-depleted environment. The biggest challenge fish face when exposed to low oxygen conditions is maintaining metabolic energy balance, as 95% of the oxygen consumed by fish is used for ATP production releasing the chemical energy of O2 through the mitochondrial electron transport chain. Therefore, hypoxia survival requires a coordinated response to secure more oxygen from the depleted environment and counteract the metabolic consequences of decreased ATP production at the mitochondria. This article is a review of the effects of hypoxia on all aspects of fish, ranging from behavior down to genes.
Chaenocephalus aceratus, commonly known as the blackfin icefish or the Scotia Sea icefish, is a species of crocodile icefish belonging to the family Channichthyidae. The blackfin icefish belongs to Notothenioidei, a suborder of fishes that accounts for 90% of the fish fauna on the Antarctic continental shelf. Icefishes, also called white-blooded fishes, are a unique family in that they are the only known vertebrates to lack haemoglobin, making their blood oxygen carrying capacity just 10% that of other teleosts. Icefishes have translucent blood and creamy white gills.
References
- ↑ Ito N.; Komiyama N. H.; Fermi G. (1995). "Structure of Deoxyhaemoglobin of the Antarctic Fish Pagothenia bernachii with an Analysis of the Structural Basis of the Root Effect by Comparison of the Liganded and Unliganded Haemoglobin Structures". Journal of Molecular Biology. 250 (5): 648–658. doi:10.1006/jmbi.1995.0405. PMID 7623382.
- 1 2 Pelster B (December 2001). "The generation of hyperbaric oxygen tensions in fish". News Physiol. Sci. 16 (6): 287–91. doi:10.1152/physiologyonline.2001.16.6.287. PMID 11719607.
- 1 2 Verde, C., A. Vergara, D. Giordano, L. Mazzarella, and G. di Prisco. 2007. The Root effect - a structural and evolutionary perspective. Antarctic Science 19:271-278.
- ↑ Berenbrink M, Koldkjaer P, Kepp O, Cossins AR (March 2005). "Evolution of oxygen secretion in fishes and the emergence of a complex physiological system". Science. 307 (5716): 1752–7. doi:10.1126/science.1107793. PMID 15774753. S2CID 36391252.
- ↑ Rummer JL, McKenzie DJ, Innocenti A, Supuran CT, Brauner CJ (June 2013). "Root Effect Hemoglobin May Have Evolved to Enhance General Tissue Oxygen Delivery" (PDF). Science. 340 (6138): 1327–9. doi:10.1126/science.1233692. hdl: 2158/1022682 . PMID 23766325. S2CID 43241955.
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