Hemoglobinopathies

INTRODUCTION
Hemoglobinopathies are diseases caused by the production of faulty hemoglobin protein, which occurs due to anomalies in the formation of the globin moiety of the hemoglobin molecule or by a deficiency of its synthesis. The hemoglobin protein molecule present in each red blood cell is a metalloprotein complex responsible for binding and transport of oxygen and carbon dioxide from the lungs to the body organs and tissues throughout the body in vertebrates (Hunefeld, 1840). Hemoglobin constitutes 97% of RBC dry weight and is critical to their shape, integrity, and half-life. Mutation in the hemoglobin results in the alteration of biological functions that leads to a condition called as “hemoglobinopathy” (Rodwell, 2000).These mutations …show more content…
A very few of them produce life threatening serious diseases. In general hemoglobinopathies are the group of disorders that cause changes in the type or amount of the hemoglobin that is produced. These hemoglobinopathies may be due to alterations in certain globin chains that include absence of production, diminished production, and abnormal structure. The hemoglobinopathies consist of structural hemoglobin variants (the most important of which are the sickling disorders) and thalassemias (hereditary defects of the synthesis of either the a or β globin chains) (Weatherall, 1997). These are the genetic defects that results in abnormal structure of one of the globin chains (inherited single-gene disorder) of the hemoglobin molecule and in most of the cases they inherit as autosomal co-dominant traits (Weatherall and Clegg, 2001). Thus the structural defects in subunits or quantitative abnormalities (non-stoichiometric expression) of hemoglobin molecules may lead to intracellular toxicity and reduction of RBC differentiation and life-span, to trapping of deformed RBCs in peripheral blood vessels, followed by widespread …show more content…
Hemoglobin is a member of the important class of conjugated proteins called as heme proteins. This class of proteins carries out varied and diversified kinds of reactions in the living organism concerned with oxidation-reduction and oxygen transporting mechanisms. All of them possess a common structural feature of iron-porphyrin prosthetic groups united with protein. Variations in the nature of the heme occurs (cytochrome), but protoheme (ferroorferri-protoporphyrin IX) is common (hemoglobin, catalase, horse-radish peroxidase). The nature of the heme-protein and of the linkages to the prosthetic group is of great importance in determining the type of activity of these proteins. In all higher animals, hemoglobin is concerned principally with oxygen-transport, this property being determined largely by the coordination of ferrous iron in the protoporphyrin molecule, and the nature of the linkage of the four heme groups to the surface of the

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