Transferrin-measures iron carrier levels; Total iron binding capacity (TIBC) is a measurement of transferrin's ability to bind iron. Serum ferritin is a protein that evaluates the body's ability to store iron. TIBC is usually measured by adding transferrin to the sample and measuring the change in color which indicates how much free iron is present. Serum ferritin is also measured using an enzyme-linked immunosorbent assay (ELISA). Blood samples are placed on special paper and sent to a laboratory for analysis.
TIBC is useful in evaluating the status of iron metabolism while serum ferritin can help identify people with IDA. Although these tests can be useful in identifying certain conditions, their results should always be interpreted with other clinical information so they can not be used in isolation for making such decisions.
IDA is anemia caused by lack of absorption of iron or its excessive loss from the body. The two main types of IDA are non-IDANon-IDANon-absorption anemia occurs when the body does not absorb enough iron from the food we eat. This can happen if we have inflammation or ulcers in the gastrointestinal tract that block the uptake of iron or if we have autoimmune disorders that damage normal cells where iron is stored in our bodies. Some medications can also cause IDA by blocking iron from being absorbed by the intestine.
Ferritin is an iron-containing blood protein. A ferritin test tells your doctor how much iron your body has stored. A ferritin test reveals that your blood ferritin level is lower than normal, indicating that your body's iron reserves are depleted and you have an iron deficit. Conversely, a high-normal or high ferritin level may indicate that you have excess iron.
Iron is a metal that can occur in three forms: iron, ferrous (or ferric) ions, and ferritin. Iron is an essential element for human survival. It plays a key role in many processes within our bodies including DNA synthesis, muscle contraction, brain function, and the production of red blood cells. Excess iron can be toxic; however, too little iron can also be harmful. The amount of iron needed by humans is not enough to cause harm even if it were all absorbed into the body. However, because the body cannot absorb all of the iron that is ingested, some is always left in waste products. This leads to iron recycling back into the bloodstream which is called "iron metabolism".
Since iron is important for healthy blood but can also be dangerous if not used properly by the body, doctors often order blood tests to determine your body's total iron status. These tests can show whether you have too much iron, too little iron, or just the right amount. Your doctor may also use these tests to diagnose other diseases or problems.
The ferritin test is a straightforward blood test. Ferritin levels that are too high may suggest an iron storage issue, such as hemochromatosis, or a chronic disease process. Low ferritin levels indicate iron deficiency, which causes anemia (a reduction in the number of oxygen-carrying red blood cells). Anemic patients are at risk for cognitive impairment and other problems related to low blood counts.
High levels of ferritin can be a sign of inflammation or cancer. Patients with these conditions may require additional testing to determine the cause of their elevated ferritin levels.
Patients should not be alarmed by abnormal results on their ferritin test; however, physicians need to consider the possibility of an underlying health problem when interpreting these results.
Titin's principal purpose is to provide elastic stability to the relative locations of myosin and actin filaments. It has areas that mimic the distinct elements of the sacromere and have mechanical, catalytic, and binding abilities to many other sacromere proteins. These include nebulin, myopalladin, zaspanins, telethons, and others.
Titin is one of the largest human proteins (3.4 million Daltons). It is composed of an N-terminal headpiece and a rod section that extends for about 400 amino acids before terminating in a globular C-terminus. The N-terminal region is responsible for most of the protein's elasticity while the C-terminal region interacts with membrane proteins such as sodium channels and ion transporters.
In skeletal muscle, the thick filament consists of three types of proteins: actin, myosin, and nebulin/skeletal muscle protein 70. Actin is the major component of thin filaments while myosin is the major component of thick filaments. Nebulins are present in very small amounts in comparison with actin or myosin but play an important role in regulating the activity of actomyosin interactions. Loss of nebulins from the sarcomere results in familial hypertrophic cardiomyopathy (FHC) due to decreased cardiac stiffness and impaired relaxation time.