STM Journals Peer-reviewed research from Consortium e-Learning Network

Research and Reviews : A Journal of Biotechnology Review Article

Hemoglobin is the Breath of Life within Our Cells: An Update

  1. Ajit Pal Singh Department of Medical Lab Technology, Sharda University, Gr. Noida
  2. Aakriti Acharya Department of Medical Lab Technology, Sharda University, Gr. Noida

Abstract

Hemoglobin is a fascinating protein found in human red blood cells. This specialist protein carries oxygen from your lungs to every cell in your body, functioning as a little delivery system. While hemoglobin’s stronghold on oxygen is necessary, releasing it at the right time is a delicate challenge. This adaptable protein masterfully balances holding on to its oxygen cargo or releasing it swiftly. This article explores how hemoglobin achieves this remarkable feat. The key lies in the changing conditions within your body! During exercise, your body creates a kind of "acid rain" that signals the need for oxygen, prompting hemoglobin to release its precious cargo. Similarly, the thinner air of high altitudes, such as the Alps, encourages hemoglobin to cling to oxygen molecules, ensuring adequate oxygen supply. This mesmerizing interplay between oxygen, hemoglobin, and your body's ever-changing needs fuels your energy to run, play, and explore. Hemoglobin is an iron-rich protein found in red blood cells. It plays a crucial role in transporting oxygen throughout the body, making it essential for life. The various processes governing hemoglobin’s affinity for binding oxygen are examined in this abstract, along with its physiological significance. Two molecules that bind to oxygen reversibly are found in each of the four globin chains that make up hemoglobin. Oxygen binding to hemoglobin causes structural alterations in the surrounding globin chains, which alters hemoglobin’s oxygen affinity. The S-shaped oxygen dissociation curve reveals how factors like carbon dioxide, pH, and 2,3-diphosphoglycerate (2,3-DPG) influence the cooperative binding of oxygen to hemoglobin. The erythrocyte can buffer hydrogen ions and combine carbon dioxide with carbamino compounds thanks to hemoglobin, which also carries carbon dioxide in the blood. Atypical hemoglobin may result from alterations to the iron atom, globin chains, or the attachment of non-oxygen ligands.

Keywords

References (18)

  1. Wagner PD. Blood Gas Transport: Carriage of Oxygen and Carbon Dioxide in Blood. Seminars in Respiratory and Critical Care Medicine. 2023;44(05):569-583. doi:10.1055/s-0043-1771160
  2. Kang Y. Liver transplantation: historical perspective. In: Anesthesia and Perioperative Care for Organ Transplantation. 2017. p. 319–31.
  3. Wang R. Physiological Implications of Hydrogen Sulfide: A Whiff Exploration That Blossomed. Physiological Reviews. 2012;92(2):791-896. doi:10.1152/physrev.00017.2011
  4. Hosseinzadeh R, Moosavi-Movahedi AA. Human hemoglobin structural and functional alterations and heme degradation upon interaction with benzene: A spectroscopic study. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2016;157:41-49. doi:10.1016/j.saa.2015.12.014
  5. Perutz MF. Mechanisms of cooperativity and allosteric regulation in proteins. Quarterly Reviews of Biophysics. 1989;22(2):139-237. doi:10.1017/s0033583500003826
  6. Dorn GW. Neurohormonal connections with mitochondria in cardiomyopathy and other diseases. American Journal of Physiology-Cell Physiology. 2022;323(2):C461-C477. doi:10.1152/ajpcell.00167.2022
  7. Abbaspour N, Hurrell R, Kelishadi R. Review on iron and its importance for human health. J Res Med Sci. 2014;19:164–74. PubMed: 24778671.
  8. Pittman RN. Oxygen transport. In: Regulation of Tissue Oxygenation. 2011. Morgan & Claypool Life Sciences.
  9. Wells RMG. Blood-gas transport and hemoglobin function. In: Fish Physiology. Vol. 27. Academic Press. 2009. p. 255–99.
  10. Nairz M, Theurl I, Swirski FK, Weiss G. “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels. Pflügers Archiv - European Journal of Physiology. 2017;469(3-4):397-418. doi:10.1007/s00424-017-1944-8
  11. Kumar S, Kaushik D, Sharma SK. Autoimmune Disorders: Types, Symptoms, and Risk Factors. Studies in Computational Intelligence. 2024:3-31. doi:10.1007/978-981-99-9029-0_1
  12. Rossaint R, Bouillon B, Cerny V, Coats TJ, Duranteau J, Fernández-Mondéjar E, et al. Management of bleeding following major trauma: an updated European guideline. Critical Care. 2010;14(2). doi:10.1186/cc8943
  13. Salvagno GL, Sanchis-Gomar F, Picanza A, Lippi G. Red blood cell distribution width: A simple parameter with multiple clinical applications. Critical Reviews in Clinical Laboratory Sciences. 2014;52(2):86-105. doi:10.3109/10408363.2014.992064
  14. Singh AP, Batra J, Saxena R, Saxena S, Kumar C. Alarming rise in professional Blood donors and its repercussions. CARDIOMETRY. 2023:1394-1396. doi:10.18137/cardiometry.2022.25.13941396
  15. Ajit P, Rahul S, Suyash S. Cytopathology: an important aspect of medical diagnosis. Res Rev. 2024;12:13–8.
  16. SINGH AP, SAXENA R, SAXENA S. HEMOGLOBIN ESTIMATION BY USING COPPER SULPHATE METHOD. Asian Journal of Current Research. 2022:13-15. doi:10.56557/ajocr/2022/v7i17760
  17. Yadav K, Kant S, Ramaswamy G, Ahamed F, Jacob OM, Vyas H, et al. Validation of Point of Care Hemoglobin Estimation Among Pregnant Women Using Digital Hemoglobinometers (HemoCue 301 and HemoCue 201+) as Compared with Auto-Analyzer. Indian Journal of Hematology and Blood Transfusion. 2019;36(2):342-348. doi:10.1007/s12288-019-01196-5
  18. Nardini S, Corbanese U, Visconti A, Dalle Mule J, Sanguinetti CM, De Benedetto F. Improving the management of patients with chronic cardiac and respiratory diseases by extending pulse-oximeter uses: the dynamic pulse-oximetry. Multidisciplinary Respiratory Medicine. 2023;18. doi:10.4081/mrm.2023.922
Support