Hemoglobin And White Blood Cell Count Low – Hematocrit (HCT) refers to the proportion of red blood cells (RBC) in an individual’s blood. Adults with XY chromosomes usually have an HCT ranging from 40% to 54%, and adults with XX chromosomes have an HCT ranging from 36% to 48%. In addition to red blood cells, blood has three other major components: white blood cells, platelets, and plasma.

Hematocrit measures the percentage of red blood cells in the total volume of blood. A hematocrit test can be performed with a capillary tube and a centrifugal machine (that is, a machine that uses centrifugal force to separate blood substances due to their different densities). Usually, hematocrit levels are identified as part of a complete blood count (CBC), but they can also be tested alone. However, a CBC is the most common blood test that measures HCT while also measuring red blood cell count, white blood cell count, hemoglobin levels, and platelets.

Hemoglobin And White Blood Cell Count Low

The hematocrit is a very useful laboratory finding that having too few or too many RBCs can be a clinical indication of various medical conditions, such as anemia or polycythemia, respectively. It can also be used to monitor individuals post-operatively to prevent or screen for complications, such as internal bleeding.

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A low hematocrit level, also known as anemia, can be the result of decreased RBC production, increased blood loss, increased RBC destruction, or a combination of these.

The most common cause of low hematocrit levels is chronic (eg, ulcers, colon cancer) or acute (eg, trauma, internal bleeding) bleeding, which leads to significant blood loss. In particular, individuals of reproductive age who are assigned female at birth may have a low hematocrit due to menstruation. However, hematocrit can also decrease due to peripheral destruction of RBCs, as seen in conditions such as sickle cell anemia, where RBCs have a shorter lifespan; and splenomegaly (ie, enlargement of the spleen), where large numbers of healthy RBCs are destroyed in the spleen. Another cause of low hematocrit is decreased RBC production, as seen in chronic inflammatory diseases, or bone marrow suppression caused by radiation therapy, malignancy, or medications such as chemotherapy. Finally, malnutrition (for example, iron deficiency, B12 and folate) and hyperhydration can also lead to decreased hematocrit levels.

Dehydration, due to fluid loss from repetitive vomiting, overheating, or limited access to fluids, can cause hemoconcentration. In addition, the low availability of oxygen activates the production of new blood cells to transport oxygen in the body and can be caused by smoking; high altitude; congenital heart disease; or certain lung disorders, such as pulmonary fibrosis or chronic obstructive pulmonary disease (COPD). In addition, polycythemia vera, which is characterized by overproduction of RBC as a result of increased bone marrow stimulation (ie, myeloproliferation), can cause high hematocrit levels. Similarly, increased erythropoietin production, whether due to androgen use or erythropoietin production by renal, liver, and ovarian tumors, may also increase the hematocrit. Finally, various pathologies of the endocrine system, such as Cushing’s syndrome, can also result in high hematocrit levels.

Hematocrit measures the percentage of red blood cells in the total volume of blood. A wide variety of medical conditions and especially blood disorders can be detected by a hematocrit test. A low hematocrit level, also known as anemia, can be the result of decreased RBC production, increased blood loss, increased RBC destruction, or a combination of the above. On the other hand, high levels of hematocrit can be the result of hemoconcentration, or the overproduction of RBC, which can be triggered by many factors.

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Dixon, L.R. (1997). Complete blood: physiological basis and clinical use. The Journal of Perinatal & Neonatal Nursing, 11 (3), 1-18. DOI: 10.1097/00005237-199712000-00003

Kragh-Hansen, U. (2018). Possible mechanisms by which enzymatic degradation of human serum albumin may lead to bioactive peptides and biomarkers. Frontiers in molecular biosciences, 5: 63. DOI: 10.3389/fmolb.2018.00063 Hemoglobin disorders are a group of inherited conditions that affect a person’s red blood cells. Red blood cells pick up oxygen from the lungs and deliver it to all the body’s tissues. In people with hemoglobin disorders, the red blood cells are less in number, less able to do their job, or both.

The most common hemoglobin disorders are sickle cell disease and thalassemia. Some versions of the genes that cause these diseases also protect against malaria – a deadly parasite carried by mosquitoes. Due to natural selection, these gene variations have become very common in some parts of the world.

The Hbb gene codes for the beta-globin protein. Two molecules of beta-globin combine with two molecules of alpha-globin to form hemoglobin. If there is a problem with the beta-globin protein, the hemoglobin doesn’t work properly, and the red blood cells can’t do their job either.

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The HBB gene, on chromosome 11, codes for the beta-globin protein. Two molecules of beta-globin combine with two molecules of alpha-globin to form hemoglobin.

Hemoglobin protein is a major part of red blood cells. It gives the blood its color and allows it to carry oxygen. The red comes from hemes – iron-containing molecules found in each globin protein. Heme is necessary for hemoglobin to carry oxygen.

There are several different versions (alleles) of the HBB gene, each coding for a slightly different beta-globin protein. Some HBB alleles can cause genetic disorders. Each type of beta-globin disorder has a unique set of symptoms, which can range from very mild to life-threatening. In all of these disorders, the symptoms are traced back to hemoglobin that works poorly, which prevents the red blood cells from doing their job.

Too little protein. Some alleles of the HBB gene produce little or no beta-globin protein. They cause some forms of beta-thalassemia, a genetic disorder in which people have too few red blood cells.

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Altered proteins. Some alleles of the HBB gene code for unusual forms of the beta-globin protein. Depending on how the beta-globin protein is altered, alleles of this type can cause several genetic disorders.

From the perspective of the protein being made, a person’s two HBB alleles are co-dominant. Beta-globin proteins are made from both alleles, and they combine randomly to make hemoglobin.

Usually, people with a healthy HBB allele make enough healthy beta-globin protein, and their red blood cells can do their job. Thus, hemoglobin disorders usually follow an autosomal recessive inheritance pattern: it takes two malfunctioning alleles to cause the disorder, one from each parent. Sickle cell disease and most forms of beta-thalassemia work this way.

However, in some cases, hemoglobin disorders follow an autosomal dominant inheritance pattern: it only takes one non-functioning HBB allele to cause the disorder. A child can inherit the disorder directly from an affected parent. Oxygen transport disorders and some forms of beta-thalassemia work this way.

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With certain allele combinations, such as the oxygen transport allele plus sickle cell, or the sickle cell allele plus beta-thalassemia, the symptoms of the disorder also follow a co-dominant pattern. The symptoms a person experiences are the result of the combined effects of both alleles.

Each person inherits two copies (or alleles) of the Hbb gene – one from each parent. Our red blood cells make the protein from both alleles and assemble it into hemoglobin. Hemoglobin molecules can include beta-globin from any allele in any combination.

Stem cells in the red bone marrow divide rapidly, giving rise to all types of blood cells. The Hbb gene is activated in what will become red blood cells. Once mature, they move into the bloodstream.

Almost all beta-globin in the body is found in red blood cells. A few other types of cells make the protein beta-globin (and hemoglobin), including cells in the lungs, eyes, and lining of the female reproductive tract. But in these cells, beta-globin is not so central to its function.

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Red blood cells are made by stem cells in the bone marrow – more specifically, in the red bone marrow. As the cells mature, the genes that code for the globin proteins are turned on. The cells fill with hemoglobin, the nucleus is pushed out of the cell, and mature red blood cells enter the bloodstream.

Red blood cells live about 3-4 months, then they are recycled. A healthy adult produces 2-3 million red blood cells every second!

People with beta-globin disorders are born healthy. This is because before we are born, we make a different type of hemoglobin – called fetal hemoglobin – which uses different globin proteins instead of beta-globin. Shortly before birth, we switch to making beta-globin. These new beta-globin red blood cells gradually replace the fetal hemoglobin. Even in the most severe cases, it takes several months to develop symptoms of a beta-globin disorder.

Red blood cells are the largest component of blood tissue, and are the most abundant cell type in the body. They carry out one of the most important tasks of the blood: providing oxygen to all the tissues of the body.

Hematocrit Vs. Hemoglobin: Normal Range For Cbc Panel

The protein beta-globin is essential for the function of red blood cells. It combines with alpha-globin to make hemoglobin – the molecule in red blood cells that carries oxygen. Without healthy beta-globin protein, red blood cells have problems, and blood tissue does not function properly.

Depending on the genetic disorder and the specific HBB alleles involved, people may experience anemia (too few red blood cells), episodes of pain, organ damage and/or low oxygen levels in the body. The next section offers more details.

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