Hemoglobin function and physiological adaptation to hypoxia in high-altitude mammals

Research output: Contribution to journalReview article

78 Scopus citations

Abstract

Understanding the biochemical mechanisms that enable high-altitude animals to survive and function under conditions of hypoxic stress can provide important insights into the nature of physiological adaptation. Evidence from a number of high-altitude vertebrates indicates that modifications of hemoglobin function typically play a key role in mediating an adaptive response to chronic hypoxia. Because much is known about structure-function relationships of mammalian hemoglobins and their physiological role in oxygen transport, the study of hemoglobin variation in high-altitude mammals holds much promise for understanding the nature of adaptation to hypoxia from the level of blood biochemistry to the level of whole-organism physiology. In this review I 1st discuss basic biochemical principles of hemoglobin function and the nature of physiological adaptation to high-altitude hypoxia in mammals. I then discuss a case study involving a complex hemoglobin polymorphism in North American deer mice (Peromyscus maniculatus) that illustrates how integrative studies of protein function and fitness-related physiological performance can be used to obtain evolutionary insights into genetic mechanisms of adaptation.

Original languageEnglish (US)
Pages (from-to)24-31
Number of pages8
JournalJournal of Mammalogy
Volume88
Issue number1
DOIs
StatePublished - Feb 2007

Keywords

  • Adaptation
  • Altitude
  • Deer mouse
  • Ecological physiology
  • Evolutionary physiology
  • Hemoglobin
  • Hypoxia
  • Natural selection
  • Oxygen transport
  • Peromyscus maniculatus

ASJC Scopus subject areas

  • Ecology, Evolution, Behavior and Systematics
  • Ecology
  • Animal Science and Zoology
  • Genetics
  • Nature and Landscape Conservation

Fingerprint Dive into the research topics of 'Hemoglobin function and physiological adaptation to hypoxia in high-altitude mammals'. Together they form a unique fingerprint.

  • Cite this