Oh, the allure of a misleading headline. When I saw this story on BBC news, “Mammoths had ‘anti-freeze blood’, gene study finds,” I thought for a moment that scientists had discovered those Ice Age behemoths had secreted some glycerol-like compound into their tissues to prevent freezing. Such a finding would have been genuinely astounding because, as far as I know, that trick is seen only among certain polar fish and overwintering insects; it would have been a first among mammals.
In reality, the surprise is not that the mammoths’ blood resisted freezing but rather that it cleverly continued to do what blood vitally must do: transport oxygen to needy tissues, even at low temperatures. Kevin L. Campbell of the University of Manitoba and his colleagues reached this conclusion through a nifty piece of paleogenomic molecular biology, as they reported in Nature Genetics. Their technique’s fascinating potential to help biologists learn about the physiologies of extinct creatures has already drawn considerable attention, but the mechanism of the hardiness of the mammoths’ blood also helps to highlight a common way in which evolution innovates.
Mammoths display obvious features that must have helped them stay warm in the brutal subzero temperatures of the Pleistocene ice ages, such as long, shaggy coats and small ears. They may well also have had less obvious ones, too, like the arrangement of blood vessels in the legs of caribou that allows countercurrent exchange to minimize the loss of body heat from their legs while they stand in snow. Nevertheless, Campbell had wondered about whether the mammoths’ blood might have been adapted, too, because of hemoglobin releases oxygen into tissues only sluggishly at low temperatures.
Human hemoglobin. By Richard Wheeler (Zephyris) 2007.
By extracting the hemoglobin gene from DNA in well-preserved mammoth remains and inserting it into bacteria, Campbell and Alan Cooper of the University of Adelaide were able to replicate samples of the mammoth’s hemoglobin. And sure enough, in subsequent tests, the resurrected hemoglobin proved to release oxygen much more consistently across a wide range of temperatures—even glacially low ones.
Perhaps it sounds surprising that something so fundamental to mammalian physiology as its hemoglobin chemistry would be subject to evolutionary revision. Surely the mammoths might have survived the cold just as well by evolving more hair or thicker insulation. Yet hemoglobin chemistry is actually a feature particularly well suited to modification—and that has been modified many times throughout evolutionary history. The key is that the genes making the globin proteins have leant themselves to frequent duplication throughout evolutionary history, which opens up the opportunity of variation among the copies and specialization in their activities. Read Full Article