Tuesday, September 27, 2011
But, what made these mammoths so different from elephants (which are successors of the mammoth) or even humans? After all, all living forms were derived from one common ancestor, but later diversified on the path of evolution. So, would humans have anything in common with the mammoths? Could we try to establish a relationship between the physiology of humans and mammoths? Now, physically, it is quite evident, that Homo sapiens are not at all similar to Mammuthus primigenius. But, there are many similarities in the cellular components of both. All living forms belonging to a common Kingdom share certain common characteristics, be it the presence of blood in all of them or the way the proteins in their bodies react to temperature extremes. Then what is it that determines which species survives better and wins the struggle for existence? It is the genetic components which vary and keep changing in response to changing environments, to produce metabolic products which render the particular organism capable of surviving a particularly odd condition.
When the Ice Age came to an end and it became difficult for life forms to deal with rising temperatures, it is not surprising that the Mammoths were the first to disappear. Their biochemical make-up was designed to counteract the cold temperatures and the perils that came with it. The greatest and most dangerous peril is the disability to breathe, caused due to the lack of oxygen reaching out to all organs of the body. This is because the protein haemoglobin, that carries oxygen and transports it throughout the body by circulation, freezes at low temperatures and loses it's ability to circulate. The Mammoths were hale and hearty in the Plesitocene Ice Age, which means their haemoglobin was different from ours.
According to a study published in the journal Biochemistry by Yue Yuan et al., the haemoglobin of Mammoths had a higher affinity for oxygen, while having less temperature sensitivity. More simplistically, it just means that the mammoth blood was better equipped to handle wider temperature changes. Added to this study, when the nucleic acids of some mammoth specimens were studied by researchers in North America, Australia and the U.K, they were able to isolate the genetic sequences responsible for producing the haemoglobin molecule. These sequences were used to recreate the mammoth haemoglobin and when compared with human haemoglobin, it was shown to be a much more effective oxygen carrier.
Imagine what this study could mean for people living in extreme climates and facing the ill-effects of hypothermia! If the research on haemoglobin molecules translates into the engineering of blood products and its large scale production, it could act as the wonder molecule for Alpine mountaineers. The biggest advantage would be its use in medical treatments where induced hypothermia is used as a form of treatment, specifically in cases of spinal cord injury or stroke. When hypothermia is used to prevent tissue damage, blood products with increased ability to deliver oxygen at freezing temperatures would keep the patient's body oxygenated. We still cannot foresee what other greater applications this research might find for itself, but studies like these prove that it is only the tip of the iceberg that is visible to us, and what goes on beyond that, is left to be challenged by researchers and scientists.