Iron is an essential nutrient that is required by all organisms. Iron deficiency is the most common nutritional deficiency in the world and it continues to be a major public health problem, especially among women and children.Iron deficiency leads to anemia, neurological problems, and increased vulnerability to infection. Iron overload is also associated with a number of diseases, such as hereditary hemochromatosis and chronic inflammatory diseases of the liver. Impaired iron metabolism has been reported for diabetes, Alzheimer’s, and Parkinson’s diseases. Despite the importance of iron in human health and illnesses, our knowledge of how cells take up and use iron is limited. Our laboratory studies the genetics and cell biology of iron uptake and utilization. My research is focused on the biology of one of the forms of iron: heme.
Heme is a large organic molecular ring structure (called protoporphyrin) with an iron atom in it. In the body, heme forms complexes with proteins. One such complex, hemoglobin, is abundant in the red blood cells. It gives blood its red color and transports oxygen in the body. Complexes of heme with other proteins play vital roles in the cell. Free heme is chemically active and could be harmful to the cell. That is why the content and distribution of heme should be tightly regulated. In the blood, special heme-binding proteins get rid of “free” heme. Likewise, single cells should have mechanisms and pathways of safe heme distribution. However, this area is largely unexplored.
To understand how heme is transported within the cell, we use genetic methods to manipulate genes affecting iron/heme status in model organisms such as baker’s yeast and mice. Switching genes on and off helps to understand how the proteins, produced with the help of these genes, function, interact, and are regulated. Currently, we are studying yeast, mice, and human proteins important for keeping the balance of iron and heme in the cell.