Root effect

Last updated

The Root effect is a physiological phenomenon that occurs in fish hemoglobin, named after its discoverer R. W. Root. It is the phenomenon where an increased proton or carbon dioxide concentration (lower pH) lowers hemoglobin's affinity and carrying capacity for oxygen. [1] [2] The Root effect is to be distinguished from the Bohr effect where only the affinity to oxygen is reduced. Hemoglobins showing the Root effect show a loss of cooperativity at low pH. This results in the Hb-O2 dissociation curve being shifted downward and not just to the right. At low pH, hemoglobins showing the Root effect don't become fully oxygenated even at oxygen tensions up to 20kPa. [2] This effect allows hemoglobin in fish with swim bladders to unload oxygen into the swim bladder against a high oxygen gradient. [3] The effect is also noted in the choroid rete, the network of blood vessels which carries oxygen to the retina. [3] In the absence of the Root effect, retia will result in the diffusion of some oxygen directly from the arterial blood to the venous blood, making such systems less effective for the concentration of oxygen. [4] It has also been hypothesized that the loss of affinity is used to provide more oxygen to red muscle during acidotic stress. [5]

Related Research Articles

<span class="mw-page-title-main">Hypoxia (medicine)</span> Medical condition of lack of oxygen in the tissues

Hypoxia is a condition in which the body or a region of the body is deprived of adequate oxygen supply at the tissue level. Hypoxia may be classified as either generalized, affecting the whole body, or local, affecting a region of the body. Although hypoxia is often a pathological condition, variations in arterial oxygen concentrations can be part of the normal physiology, for example, during strenuous physical exercise.

<span class="mw-page-title-main">Hemoglobin</span> Metalloprotein that binds with oxygen

Hemoglobin is a protein containing iron that facilitates the transport of oxygen in red blood cells. Almost all vertebrates contain hemoglobin, with the exception of the fish family Channichthyidae. Hemoglobin in the blood carries oxygen from the respiratory organs to the other tissues of the body, where it releases the oxygen to enable aerobic respiration which powers the animal's metabolism. A healthy human has 12 to 20 grams of hemoglobin in every 100 mL of blood. Hemoglobin is a metalloprotein, a chromoprotein, and globulin.

<span class="mw-page-title-main">Red blood cell</span> Oxygen-delivering blood cell and the most common type of blood cell

Red blood cells (RBCs), referred to as erythrocytes in academia and medical publishing, also known as red cells, erythroid cells, and rarely haematids, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen to the body tissues—via blood flow through the circulatory system. Erythrocytes take up oxygen in the lungs, or in fish the gills, and release it into tissues while squeezing through the body's capillaries.

<span class="mw-page-title-main">Myoglobin</span> Iron and oxygen-binding protein

Myoglobin 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. Myoglobin consists of non-polar amino acids at the core of the globulin, where the heme group is non-covalently bounded with the surrounding polypeptide of myoglobin. In humans, myoglobin is found in the bloodstream only after muscle injury.

<span class="mw-page-title-main">Leghemoglobin</span> Oxygen-carrying phytoglobin found in rhizome of leguminous plants

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.

<span class="mw-page-title-main">Hemocyanin</span> Proteins that transport oxygen throughout the bodies of some invertebrate animals

Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O2). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not confined in blood cells, but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form.

<span class="mw-page-title-main">Swim bladder</span> Gas-filled organ that contributes to the ability of a fish to control its buoyancy

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 expend energy in swimming. Also, the dorsal position of the swim bladder means that the expansion of the bladder moves the center of mass downwards, allowing it to act as a stabilizing agent in some species. Additionally, the swim bladder functions as a resonating chamber, to produce or receive sound.

<span class="mw-page-title-main">Rete mirabile</span> Complex of arteries and veins lying very close to each other

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.

<span class="mw-page-title-main">Fetal hemoglobin</span> Oxygen carrier protein in the human fetus

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 than adult forms of hemoglobin, allowing it to bind oxygen more strongly; this in turn enables the developing fetus to retrieve oxygen from the mother's bloodstream, which occurs through the placenta found in the mother's uterus.

<span class="mw-page-title-main">Bohr effect</span> Concept in physiology

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.

<span class="mw-page-title-main">Channichthyidae</span> Family of fishes

The crocodile icefish or white-blooded fish comprise a family (Channichthyidae) of notothenioid fish 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 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 historic name, "carbonic oxide", and evolved through Germanic and British English etymological influences; the preferred IUPAC nomenclature is carbonylhemoglobin.

<span class="mw-page-title-main">Oxygen–hemoglobin dissociation curve</span> Visual tool used to understand how human blood carries and releases oxygen

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.

<span class="mw-page-title-main">Notothenioidei</span> Suborder of fishes

Notothenioidei is one of 19 suborders of the order Perciformes. The group is found mainly in Antarctic and Subantarctic waters, with some species ranging north to southern Australia and southern South America. Notothenioids constitute approximately 90% of the fish biomass in the continental shelf waters surrounding Antarctica.

Carbaminohemoglobin (carbaminohaemoglobin BrE) (CO2Hb, also known as carbhemoglobin and carbohemoglobin) is a compound of hemoglobin and carbon dioxide, and is one of the forms in which carbon dioxide exists in the blood. Twenty-three percent of carbon dioxide is carried in blood this way (70% is converted into bicarbonate by carbonic anhydrase and then carried in plasma, 7% carried as free CO2, dissolved in plasma).

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. Vice versa, it is true that a high concentration of CO2 facilitates dissociation of oxyhemoglobin, though this is the result of two distinct processes (Bohr effect and Margaria-Green effect) and should be distinguished from Haldane effect.

<span class="mw-page-title-main">2,3-Bisphosphoglyceric acid</span> Chemical compound

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).

<span class="mw-page-title-main">Chloride shift</span> Transfer of ions into red blood cells

Chloride shift (also known as the Hamburger phenomenon or lineas phenomenon, named after Hartog Jakob Hamburger) is a process which occurs in a cardiovascular system and refers to the exchange of bicarbonate (HCO3) and chloride (Cl) across the membrane of red blood cells (RBCs).

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. Fish respond to hypoxia with varied behavioral, physiological, and cellular responses 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 nutrients 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.

<span class="mw-page-title-main">Blackfin icefish</span> Species of fish

The blackfin icefish, also known as 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

  1. 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.
  2. 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. Archived from the original on 2016-03-03. Retrieved 2011-03-06.
  3. 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.
  4. 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.
  5. 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.