Respiration and Hemoglobin

Oxygen transport physiology The cells of the human body use oxygen molecules (two oxygen atoms forming an O2) as a vital component of their basic metabolism Most can survive briefly without oxygen but not for long and not well Delivering oxygen to the cells is a process that starts in the lungs Oxygen in the ambient air is inhaled into the thin-walled sacs called aveoli where they easily

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HUMAN PHYSIOLOGY

IV The affinity of hemoglobin for oxygen is also decreased by an organic molecule in the red blood cells called 2 3-diphosphoglyceric acid (2 3-DPG) A Since oxyhemoglobin inhibits 2 3-DPG production 2 3-DPG concentrations will be higher when anemia or low PO2 (as in high altitude) causes a decrease in oxyhemoglobin B If a person is anemic

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Blttern nach Institutionen der Universitt

Baumann Rosemarie Gtz Robert und Dragon Stefanie (2003) Nucleoside triphosphate pattern of avian embryonic red cells: role of RNA degradation and AMP deaminase/5'-nucleotidase activity American journal of physiology Regulatory integrative and comparative physiology 284 (3) R771-R779 Volltext nicht vorhanden

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Acide 2 3

L'acide 2 3-bisphosphoglycrique — ou 2 3-bisphosphoglycrate sous forme dprotone abrge en 2 3-BPG — est un compos organique isomre de l'acide 1 3-bisphosphoglycrique un important intermdiaire mtabolique de la glycolyse Il intervient chez l'espce humaine dans la rgulation du transport de l'oxygne dans le sang en stabilisant la forme dsoxy de l'hmoglobine

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Effects of High Altitude (Low Arterial [equation]) and of

Accordingly the main role of the 2 3-DPG change at high altitude (and also in acid-base disorders) is to maintain the oxygen dissociation curve of human blood at (or near) its original position This conclusion seems to be valid for man resting at altitudes up to 7000 m The changes occurring at higher altitudes and during a rapid climb to a

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Oxygen dissociation curve

What is the role of 2-3What is the role of 2-3 DPG ??DPG ?? In the deoxygenated T conformer a cavityIn the deoxygenated T conformer a cavity capable of binding 2 3-BPG forms in the centercapable of binding 2 3-BPG forms in the center of the molecule 2 3-BPG can occupy this cavityof the molecule 2 3-BPG can occupy this cavity stabilizing the T state Conversely when 2 3-stabilizing the T

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Brain Blood Flow in Andean and Himalayan High

The affinity of oxygen for hemoglobin is however influenced by temperature CO 2 H + and within the red cell by 2 3-diphosphoglycerate (2 3-DPG) In residents at high altitude a small hyperventilation alkalosis is observed that produces a left shift of the oxygen dissociation curve and an increase of the affinity of oxygen for hemoglobin This leftward shift is compensated for by an

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Sodium cyanate: from a promising therapeutic agent to a

an important role in oxygen transport both at sea level and at high altitude It is usually represented by an ODC relating P0 2 and 0 2 saturation (S0 2) (Fig 1) The position of the ODC may vary the change being usually a shift to the right or to the left with all P0 2s increasing or decreasing in the same propor tion as in a Bohr shift For example the blood ODC is strongly influenced

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Universitt Regensburg

Oxygen pressure-dependent control of carbonic anhydrase synthesis in chick embryonic erythrocytes Am J Physiol 1991 Nov 261(5 Pt 2):R1188-96 1986 Baumann R Haller EA Schning U Weber M Hypoxic incubation leads to concerted changes of carbonic anhydrase activity and 2 3 DPG concentration of chick embryo red cells

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Oxygen hemoglobin dissociation curve

2 3-DPG: 2 3-Diphosphoglycerate is an organophosphate which is created in erythrocyte during glycolysis In the presence of 2 3-DPG the curve shift to the right causes low hemoglobin affinity for oxygen Temperature: Increases in temperature weaken and denature the bond between oxygen and hemoglobin and shift the oxygen hemoglobin dissociation curve to the right Leftward shift: The

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AltitudeOmics: Red Blood Cell Metabolic Adaptation to

Red blood cells (RBCs) are key players in systemic oxygen transport RBCs respond to in vitro hypoxia through the so-called oxygen-dependent metabolic regulation which involves the competitive binding of deoxyhemoglobin and glycolytic enzymes to the N-terminal cytosolic domain of band 3 This mechanism promotes the accumulation of 2 3-DPG stabilizing the deoxygenated state of hemoglobin and

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Oxygen Transport to Tissue

Oxygen Transport to Tissue 1 OXYGEN TRANSPORT TO TISSUE Pharmacology Mathematical Studies and Neonatology 2 ADV ANCES IN EXPERIMENTAL MEDICINE AND BIOLOGY Editorial Board: Nathan Back N R Di Luzio Alfred Gellhorn Bernard Halpern Ephraim Katchalski David Kritchevsky Abel Lajtha Rodolfo Paoletti Volume 1 Chairman Department 0/ Biochemical

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Effects of the "live high

tion of 2 3-diphosphoglycerate (2 3-DPG) causing a rightward shift of the oxyhemoglobin dissociation curve development of capillary density an increase in mito-chondrial capacity an increase in oxidative enzyme activ-ity and an increase in muscle myoglobin content (Fig 1)2-8) Consequently both the oxygen transporting ability

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High Altitude

Role of EPAS1 Genetic Evidence for High-Altitude Adaptation in Tibet 2010 Tibetans have lived at very high altitudes for thousands of years and they have a distinctive suite of physiological traits that enable them to tolerate environmental hypoxia These phenotypes are clearly the result of adaptation to this environment but their genetic basis remains unknown We report genome-wide

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Erythropoiesis

Erythropoiesis-stimulating agents and other methods to enhance oxygen transport S Elliott Department of Hematology One Amgen Center Amgen Inc Thousand Oaks CA USA Oxygen is essential for life and the body has developed an exquisite method to collect oxygen in the lungs and transport it to the tissues Hb contained within red blood cells (RBCs) is the key oxygen-carrying

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Oxyhemoglobin Dissociation Curve

The standard curve is shifted to the right by an increase in temperature 2 3-DPG or PCO 2 or a decrease in pH The curve is shifted to the left by the opposite of these conditions A rightward shift by definition causes a decrease in the affinity of hemoglobin for oxygen This makes it harder for the hemoglobin to bind to oxygen (requiring a higher partial pressure to achieve the same

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AltitudeOmics: Red Blood Cell metabolic adaptation to high

This mechanism promotes the accumulation of 2 3-DPG stabilizing the deoxygenated state of hemoglobin and cytosol acidification triggering oxygen off-loading through the Bohr effect Despite in vitro studies in vivo adaptations to hypoxia have not yet been completely elucidated Within the framework of the AltitudeOmics study erythrocytes were collected from 21 healthy volunteers at sea

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