Red Blood Cells

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Molecular model A shows the structure of hemoglobin, which is made up of four protein subunits, each of which is coiled into helices. Left right, bottom and top parts of the molecule are symmetrical. Four small heme groups are associated with hemoglobin. Oxygen is bound to the heme. Molecular model B shows the structure of hemocyanin, a protein made up of coiled helices and ribbon-like sheets. Two copper ions are associated with the protein. Molecular model C shows the structure of hemerythrin, a protein made of coiled helices with four iron ions associated with it.
In most vertebrates, (a) hemoglobin delivers oxygen to the body and removes some carbon dioxide. Hemoglobin is composed of four protein subunits, two alpha chains and two beta chains, and a heme group that has iron associated with it. The iron reversibly associates with oxygen, and in so doing is oxidized from Fe2+ to Fe3+. In most mollusks and some arthropods, (b) hemocyanin delivers oxygen. Unlike hemoglobin, hemolymph is not carried in blood cells, but floats free in the hemolymph. Copper instead of iron binds the oxygen, giving the hemolymph a blue-green color. In annelids, such as the earthworm, and some other invertebrates, (c) hemerythrin carries oxygen. Like hemoglobin, hemerythrin is carried in blood cells and has iron associated with it, but despite its name, hemerythrin does not contain heme. Source: OpenStax Biology 2e

OpenStax Biology 2e

Red blood cells, or erythrocytes (erythro- = “red”; -cyte = “cell”), are specialized cells that circulate through the body delivering oxygen to cells; they are formed from stem cells in the bone marrow. In mammals, red blood cells are small biconcave cells that at maturity do not contain a nucleus or mitochondria and are only 7–8 µm in size. In birds and non-avian reptiles, a nucleus is still maintained in red blood cells.

The red coloring of blood comes from the iron-containing protein hemoglobin. The principle job of this protein is to carry oxygen, but it also transports carbon dioxide as well. Hemoglobin is packed into red blood cells at a rate of about 250 million molecules of hemoglobin per cell. Each hemoglobin molecule binds four oxygen molecules so that each red blood cell carries one billion molecules of oxygen. There are approximately 25 trillion red blood cells in the five liters of blood in the human body, which could carry up to 25 sextillion (25 × 1021) molecules of oxygen in the body at any time. In mammals, the lack of organelles in erythrocytes leaves more room for the hemoglobin molecules, and the lack of mitochondria also prevents use of the oxygen for metabolic respiration. Only mammals have anucleated red blood cells, and some mammals (camels, for instance) even have nucleated red blood cells. The advantage of nucleated red blood cells is that these cells can undergo mitosis. Anucleated red blood cells metabolize anaerobically (without oxygen), making use of a primitive metabolic pathway to produce ATP and increase the efficiency of oxygen transport.

Not all organisms use hemoglobin as the method of oxygen transport. Invertebrates that utilize hemolymph rather than blood use different pigments to bind to the oxygen. These pigments use copper or iron to the oxygen. Invertebrates have a variety of other respiratory pigments. Hemocyanin, a blue-green, copper-containing protein is found in mollusks, crustaceans, and some of the arthropods. Chlorocruorin, a green-colored, iron-containing pigment is found in four families of polychaete tubeworms. Hemerythrin, a red, iron-containing protein is found in some polychaete worms and annelids. Despite the name, hemerythrin does not contain a heme group and its oxygen-carrying capacity is poor compared to hemoglobin.

The small size and large surface area of red blood cells allows for rapid diffusion of oxygen and carbon dioxide across the plasma membrane. In the lungs, carbon dioxide is released and oxygen is taken in by the blood. In the tissues, oxygen is released from the blood and carbon dioxide is bound for transport back to the lungs. Studies have found that hemoglobin also binds nitrous oxide (NO). NO is a vasodilator that relaxes the blood vessels and capillaries and may help with gas exchange and the passage of red blood cells through narrow vessels. Nitroglycerin, a heart medication for angina and heart attacks, is converted to NO to help relax the blood vessels and increase oxygen flow through the body.

A characteristic of red blood cells is their glycolipid and glycoprotein coating; these are lipids and proteins that have carbohydrate molecules attached. In humans, the surface glycoproteins and glycolipids on red blood cells vary between individuals, producing the different blood types, such as A, B, and O. Red blood cells have an average life span of 120 days, at which time they are broken down and recycled in the liver and spleen by phagocytic macrophages, a type of white blood cell.

Source:

Clark, M., Douglas, M., Choi, J. Biology 2e. Houston, Texas: OpenStax. Access for free at: https://openstax.org/details/books/biology-2e

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