Sickle cell anemia

From The School of Biomedical Sciences Wiki
(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
&nbsp;Sickle cell is an inherited disease and it is caused by a mutation that occurs in the beta sub units of the [[Haemoglobin|haemoglobin]]. Haemoglobin is a tetrameric protein made up of &nbsp;2 alpha subunits and 2 beta subunits and it is the essential part of the blood responsible for oxygen transportation. Sickle cell is a &nbsp;disease that results from a substitution of a polar amino acid known as glutamate with a non polar one valine at &nbsp;position six of the beta poly peptide unit of haemoglobin. The substitution happens as a result of a change in one of the bases in the beta globin gene from adenine to thymine. <br>As a result of this mutation, the beta polypeptide chains become sticky in low oxygen conditions because the valine sticks out of the chain and interacts with neighbouring non polar amino acids. The molecules stick together and finally develop into a massive fibrous polymer that causes the distortion of the red blood cells into a “c” or sickle. The normal red blood cell is dough- nut shaped and soft so it has a larger surface area to carry oxygen efficiently and can squeeze through blood vessels. As opposed to the normal cell, the sickle cell carries less oxygen and it is stiff so it cannot squeeze through blood vessels easily and therefore has a high tendency of blocking arteries that supply oxygen to the cells. This could lead to organ failure and damage for example stroke, heart attack or kidney failure.&nbsp;
+
Sickle cell is an inherited disease and it is caused by a mutation that occurs in the beta sub units of the [[Haemoglobin|haemoglobin]]. Haemoglobin is a tetrameric [[protein|protein]] made up of &nbsp;2 alpha subunits and 2 beta subunits and it is the essential part of the [[blood|blood]] responsible for [[oxygen|oxygen]] transportation. Sickle cell is a &nbsp;disease that results from a substitution of a [[polar|polar ]][[amino acid|amino acid]] known as [[glutamate|glutamate]] with a non polar one [[valine|valine]] at &nbsp;position six of the beta [[polypeptide|polypeptide]] unit of haemoglobin. The substitution happens as a result of a change in one of the bases in the beta globin [[gene|gene]] from [[adenine|adenine]] to [[thymine|thymine]].  
  
References
+
As a result of this mutation, the beta polypeptide chains become sticky in low oxygen conditions because the valine sticks out of the chain and interacts with neighbouring non-polar amino acids. The molecules stick together and finally develop into a massive fibrous polymer that causes the distortion of the red blood cells into a “c” or sickle. The normal red blood cell is dough- nut shaped and soft so it has a larger surface area to carry oxygen efficiently and can squeeze through blood vessels. As opposed to the normal cell, the sickle cell carries less oxygen and it is stiff so it cannot squeeze through blood vessels easily and therefore has a high tendency of blocking arteries that supply oxygen to the cells. This could lead to organ failure and damage for example stroke, heart attack or kidney failure <ref>Understanding Sickle Cell Disease by Mariam Bloom, Ph.D 1995</ref><ref>http://sickle.bwh.harvard.edu/msh.html</ref><ref>http://www.nejm.org/doi/full/10.1056/NEJM199008093230602</ref>.&nbsp;
  
1. Understanding Sickle Cell Disease by Mariam Bloom, Ph.D 1995
+
=== References  ===
  
2&nbsp;http://sickle.bwh.harvard.edu/msh.html <br>  
+
<references /><br>
 
+
3.&nbsp;http://www.nejm.org/doi/full/10.1056/NEJM199008093230602 <br>
+

Revision as of 05:49, 25 October 2012

Sickle cell is an inherited disease and it is caused by a mutation that occurs in the beta sub units of the haemoglobin. Haemoglobin is a tetrameric protein made up of  2 alpha subunits and 2 beta subunits and it is the essential part of the blood responsible for oxygen transportation. Sickle cell is a  disease that results from a substitution of a polar amino acid known as glutamate with a non polar one valine at  position six of the beta polypeptide unit of haemoglobin. The substitution happens as a result of a change in one of the bases in the beta globin gene from adenine to thymine.

As a result of this mutation, the beta polypeptide chains become sticky in low oxygen conditions because the valine sticks out of the chain and interacts with neighbouring non-polar amino acids. The molecules stick together and finally develop into a massive fibrous polymer that causes the distortion of the red blood cells into a “c” or sickle. The normal red blood cell is dough- nut shaped and soft so it has a larger surface area to carry oxygen efficiently and can squeeze through blood vessels. As opposed to the normal cell, the sickle cell carries less oxygen and it is stiff so it cannot squeeze through blood vessels easily and therefore has a high tendency of blocking arteries that supply oxygen to the cells. This could lead to organ failure and damage for example stroke, heart attack or kidney failure [1][2][3]

References

  1. Understanding Sickle Cell Disease by Mariam Bloom, Ph.D 1995
  2. http://sickle.bwh.harvard.edu/msh.html
  3. http://www.nejm.org/doi/full/10.1056/NEJM199008093230602

Personal tools
Namespaces
Variants
Actions
Navigation
Toolbox