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Hypoxia Alters miRNAs Levels Involved in Non-Mendelian Inheritance of Autism Spectrum Disorder in Mice

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Genetic differences in hemoglobin function between highland and lowland deer mice.

Jay F Storz¹, Amy M Runck, Hideaki Moriyama

¹School of Biological Sciences, University of Nebraska, Lincoln, NE 68588, USA. jstorz2@unl.edu

The Journal of Experimental Biology

|July 20, 2010

Summary

Highland deer mice exhibit hemoglobin adaptations for better oxygen transport at altitude. Genetic diversity in hemoglobin isoforms influences oxygen affinity and allosteric regulation in these adaptable mammals.

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Area of Science:

Physiology
Genetics
Biochemistry

Background:

High-altitude vertebrates often adapt by modifying hemoglobin (Hb) structure for improved oxygen transport.
These adaptations can involve intrinsic Hb oxygen affinity or responsiveness to allosteric effectors.

Purpose of the Study:

To investigate genetically based differences in Hb-O(2) affinity between highland and lowland deer mouse populations.
To understand the role of Hb isoform diversity in adaptation to varying altitudes.

Main Methods:

Combined genetic and proteomic analysis of deer mouse hemoglobin.
Oxygen equilibrium experiments to assess Hb-O(2) affinity and effector sensitivity.

Main Results:

Deer mice possess high Hb isoform diversity due to polymorphic globin genes.
Highland mice Hbs show higher intrinsic O(2) affinity and lower chloride sensitivity than lowland mice.
Distinct biochemical properties of deer mouse Hb related to anion-dependent allosteric regulation were identified.

Conclusions:

Modifications in Hb structure, particularly altered allosteric anion sensitivity, are crucial for fine-tuning blood-O(2) affinity in deer mice.
Hb structural modifications play a significant role in the adaptation of deer mice to high-altitude environments.