High Altitude Respiration Research Articles

A high altitude respiration and SpO2 dataset for assessing the human response to hypoxia

This report presents the Harespod dataset, an open dataset for high altitude hypoxia research, which includes respiration and SpO2 data. The dataset was collected from 15 college students aged 23–31 in a hypobaric oxygen chamber, during simulated altitude changes and induced hypoxia. Real-time physiological data, such as oxygen saturation waveforms, oxygen saturation, respiratory waveforms, heart rate, and pulse rate, were obtained at 100 Hz. Approximately 12 hours of valid data were collected from all participants. Researchers can easily identify the altitude corresponding to physiological signals based on their inherent patterns. Time markers were also recorded during altitude changes to facilitate realistic annotation of physiological signals and analysis of time-difference-of-arrival between various physiological signals for the same altitude change event. In high altitude scenarios, this dataset can be used to enhance the detection of human hypoxia states, predict respiratory waveforms, and develop related hardware devices. It will serve as a valuable and standardized resource for researchers in the field of high altitude hypoxia research, enabling comprehensive analysis and comparison.

Molecular mechanism of high altitude respiration: primary structure of a minor hemoglobin component from Tufted duck ( Aythya fuligula, Anseriformes)

Avian hemoglobins have attracted much attention in view of the unique oxygen transport characteristics. The present study describes the primary structure of minor hemoglobin component HbD from Tufted duck ( Aythya fuligula), a migratory bird seen in Pakistan during the winter season. Separation of the polypeptide subunits was achieved by ion exchange chromatography in the presence of 8 M urea. Molecular masses of the intact protein as well as peptides obtained from chemical and enzymatic cleavages were determined by electrospray ionization mass spectrometry. The sequence was studied by automatic Edman degradation of the native chains and their tryptic/hydrolytic fragments in a gas-phase sequencer. Comparison of the hemoglobin sequence with the corresponding sequences of Anseriform representatives and other avian species shows residues like α D23 Asp, α D120 Asp as being specific to Tufted duck. The three-dimensional structure analyzed with the protein structure modeling package, WHAT IF, using the crystal structure coordinates of chicken hemoglobin (PDB code = 1hbr) shows α D34 Val, α D38 Gln, and α D94 Asp as possible mediators offering alternate pathway for oxygen uptake and release thereby leading to distinct hypoxia tolerance in the Tufted ducks. Results are discussed with reference to function and evolution in the Anseriform representatives.

Mutant hemoglobins (alpha 119-Ala and beta 55-Ser): functions related to high-altitude respiration in geese.

The unusually high blood-O2 affinity in the bar-headed and Andean geese is a necessary adaptation for migration across high mountain ranges. The amino acid residues alpha-119 and beta-55, which form an alpha 1 beta 1 contact in human hemoglobin (Hb), are altered in bar-headed and Andean geese, respectively, which suggests that loss of this contact increases O2 affinity. Two mutant human Hbs with equivalent mutations at these sites prepared by site-directed mutagenesis show the same increase in O2 affinity compared with Hb A, which indicates that these mutations are responsible for the changes in the protein. The intrinsic affinity difference compared with native Hb A is amplified by organic phosphates. Whereas the recombinant and native Hbs displayed similar sensitivities to pH, chloride, and 2,3-diphosphoglycerate, the oxygenation heat of the alpha-chain mutant decreased in the presence of 2,3-diphosphoglycerate. O2 association constants for the deoxygenated state of the alpha-mutant were about three times those for Hb A. The mutant Hb analogously exhibited higher affinity constants for binding the first three O2 molecules. Calculated heme-heme interaction energies indicated that loss of a single contact, resulting in destabilization of the deoxy (tense) structure, underlies the increased O2 affinity. Adaptations securing Hb-O2 binding at extreme altitude are discussed.

High-altitude respiration of birds. Structural adaptations in the major and minor hemoglobin components of adult Rüppell's Griffon (Gyps rueppellii, Aegypiinae): a new molecular pattern for hypoxic tolerance.

The primary structures of the hemoglobins Hb A, Hb A', Hb D and Hb D' of Rüppell's Griffon (Gyps rueppellii), which can fly as high as 11,300 m, are presented. The globin chains were separated on CM-Cellulose in 8M urea buffers, the four hemoglobin components by FPLC in phosphate buffers. The amino-acid sequences of five globin chains were established by automatic Edman degradation of the globin chains and of the tryptic peptides in liquid-phase and gas-phase sequenators. The sequences are compared with those of other Falconiformes. A new molecular pattern for survival at extreme altitudes is presented. For the first time four hemoglobins are found in blood of a bird; they show identical beta-chains and differ in the alpha A- and alpha D-chains by only one replacement. These four hemoglobins cause a gradient in oxygen affinities. The two main components Hb A and Hb A' differ at position alpha 34 Thr/Ile. In case of Ile as found in Hb A' an alpha 1 beta 1-interface is interrupted raising oxygen affinity compared to Hb A. In addition the hemoglobins of the A- and D-groups differ at position alpha 38 Pro or Gln/Thr (alpha 1 beta 2-interface). Expression of Gln in Hb D/D' raises the oxygen affinity of these components compared to Hb A/A' by destabilization of the deoxy-structure. The physiological advantage lies in the functional interplay of four hemoglobin components. Three levels of affinity are predicted: low affinity Hb A, Hb A' of intermediate affinity, and high affinity Hb D/D'. This cascade tallies exactly with oxygen affinities measured in the isolated components and predicts oxygen transport by the composite hemoglobins over an extended range of oxygen affinities. It is contended that the mechanisms of duplication of the alpha-genome (creating four hemoglobins) and of nucleotide replacements (creating different functional properties) are responsible for this remarkable hypoxic tolerance to 11,300 m. Based on this pattern the hypoxic tolerances of other vultures are predicted.

High Altitude and Hemoglobin Function in the Vultures Gyps rueppellii and Aegypius monachus

Functional characteristics of the stripped composite hemoglobins (Hbs) of the vultures Gyps rueppellii and Aegypius monachus that can fly at extremely high altitudes, and of component Hbs of G. rueppellii are reported, in relation to influences of pH, temperature and inositol hexaphosphate. G. rueppellii Hbs A, A' and D represent a sequence of increasing oxygen affinity, which is opposite to earlier results on avian Hb components, but correlates with two alpha-chain substitutions that predictably affect oxygen affinity. The homo- and heterotropic interactions in oxygen binding are related to primary structures of the constituent polypeptide chains to trace molecular adaptations to high-altitude respiration, and to physiological factors (pulmonary hypoxia and hypocapnia, body temperature shifts, and lung and nasal gas and heat exchange) to discern their possible survival value at altitudes of 11,300 m.

The primary structures of the major and minor hemoglobin-components of adult Andean goose (Chloephaga melanoptera, Anatidae): the mutation Leu----Ser in position 55 of the beta-chains.

The primary structures of the hemoglobin components Hb A and Hb D of the adult Andean Goose (Chloephaga melanoptera) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the globin chains and of the tryptic peptides in liquid- and gas-phase sequenators. The sequences are aligned with those of Greylag Goose (Anser anser) as a biological reference and other sequences of birds. A detailed evaluation of all residues of Andean Goose hemoglobins on the basis of the 12000 known avian globin sequences leads to a molecular pattern for high-altitude respiration of geese. The replacement of functional and structural importance is the unique occurrence of the residue beta 55 Leu----Ser (all other exchanges are functionally neutral), interrupting the same alpha 1 beta 1-interface contact (alpha 119-beta 55) that accounts for high-altitude respiration of the Barheaded Goose (Anser indicus); there the mutation is found on alpha A 119. Loosening the constraints of this interface must be interpreted as a destabilization of the low-affinity T-structure in favour of the high-affinity R-structure. The structural and functional significance of this interface for the molecular biology of high-altitude respiration of the Andean Goose and Barheaded Goose is discussed. Since Hb A consists of alpha A2 beta 2 and Hb D consists of alpha D2 beta 2 the mutation occurring in blood of the Andean Goose affects both hemoglobins whereas in the case of the Barheaded Goose only Hb A is affected. These results show that Hb D can be considered a biological reserve to enlarge situatively the normal hemoglobin function. A general molecular pattern for permanent (selective advantage of high intrinsic oxygen affinity) and transitory (selective advantage of graded oxygen affinities) adaptation to hypoxia is discussed. A survey on the sequence homology of the globin chains of geese (Anserinae) and ducks (Anatinae) is given.