Phenylketonuria Disorder

Metabolic alkalosis is a condition in which the body fluids have excess base. The kidneys and lungs maintain the proper balance of chemicals, called acids and bases, in the body. Decreased carbon dioxide or increased bicarbonate level makes the body too alkaline. There are different types of alkalosis such as: respiratory alkalosis, which is caused by a low carbon dioxide level in the blood. This can be due to: fever, lack of oxygen, lung disease, or liver disease; hypochloermic alkalosis is caused by an extreme lack or loss of chloride, from prolonged vomiting; hypokalemic alkalosis is caused by the kidneys’ response to an extreme lack of potassium, this can occur from taking certain water pills. Compensated alkalosis occurs when the body returns to the acid-base balance to normal in cases of alkalosis, but bicarbonate and carbon dioxide levels remain abnormal. Symptoms of alkalosis can include: confusion, hand tremor, light-headedness, muscle twitching, vomiting, and numbness or tingling in the face, hands, or feet. Treatment for alkalosis depends on

According to research, PKU is “an autosomal recessive genetic disorder characterized by mental retardation due to a deficiency in phenylalanine hydroxylase, an enzyme necessary to metabolize the essential amino acid phenylalanine to tyrosine. Without phenylalanine hydroxylase, phenylalanine is converted to neurotoxic phenyl pyruvic acid” (Gonzalez, 2009). For those who have PKU, the phenyl pyruvic acid would become quite toxic and lead to damage within the brain causing mental retardation. PKU was first discovered in 1938 by a man named Asbjorn Fölling, and throughout the early 1960s phenyl pyruvic acid was found in urine using a reaction with ferric chloride. However, it was in 1958, that Dr. Guthrie transferred to the Buffalo Children’s Hospital and was able to develop a new approach to measure and monitor

In people with PKU Phenylalanine’s most apparent and benifical side affect is itrs function as a necessary building block for protein; It may also help create chemicals that work to regulate appetite and mood.

Polycystic kidney disorder is a genetic disorder. If one parent has the gene and passes it on to their child, this is called Dominant inheritance and the child has 50% chance of getting the disease. If both parents have the gene and pass it on to their child, this is called Recessive inheritance and the child has 25% chance of getting the disease. There are three types of PKD. Autosomal Dominant PKD is the first form. This form is passed from parent to child by dominant inheritance. Symptoms usually begin between the ages of 30 or 40 and can be earlier than that. Autosomal Dominant PKD is the most common form of PKD, 90% of PKD are this form. Infantile or Autosomal Recessive PKD is another form. This is passed from parent to child by recessive inheritance.

The specific metabolic disorder that I picked for this discussion is Krabbe Disease or globoid cell leukodystrophy. The disease destroys the protective coating of nerve cells in the brain and throughout the body causing the nerve cells to stop responding or react unpredictably. The disease is caused by a person receiving two copies of a mutated gene that results in severely curtailed production of an enzyme called galactocerebrosidase (GALC) (Krabbe disease, n.d.). This enzyme is responsible for breaking down certain substances in a cell's recycling center. Unfortunately, in Krabbe disease, not enough GALC was produced so the cells begin accumulating fats called galactolipids which normally are responsible for maintaining the protective coating

Phenylketonuria, or PKU, is an autosomal recessive, heritable disease that decreases levels of the enzyme phenylalanine hydroxylase, which is responsible for the metabolism of the amino acid phenylalanine, resulting in an unhealthy buildup that can lead to brain damage, seizures, and intellectual disability. While not curable, PKU, if detected early on, can be treated to allow sufferers to lead full and healthy lives. The symptoms of PKU appear almost immediately after birth, requiring parents and hospitals to make the necessary preparations, including feeding infants with special formula. Lack of such care can result in

Low phenylalanine containing diet is the first treatment of PKU, and this is applied for all of PKU patients. It has been demonstrated that low phenylalanine concentration in daily meals can effectively prevent mental retardation in PKU patients, especially in newborns (Knox, 1960). The major point of this treatment is to offer PKU patients with very low phenylalanine diets, and all of protein-rich and aspartame containing foods and drinks should be avoided. Aspartame is an artificial sweetener that can be converted into phenylalanine following ingestion, so it must be avoided from the diet of PKU patients (Williams, Mamotte & Burnett, 2008). Since PKU develops very early after birth, this treatment is applied immediately after conformation of the disease in an infant. For older kids, the amount of daily ingested protein is calculated each day regarding how severe PKU of the patient. Although this method can

Untreated PKU can lead to brain damage, intellectual disabilities, behavioral symptoms, or seizures. The defective gene does not produce the enzyme necessary to break down and rid the body of phenylalanine. The symptoms of phenylketonuria result from a buildup of (Global Genes, 2012) I eat differently. My friends understand PKU is very difficult, but-non PKU people think I am VERY different. I’ve had to adjust to other’s perceptions and learn to cope with what other people expect is the norm.”(Global Genes, 2012) this researcher would describe this disorder as A birth defect that causes an amino acid called phenylalanine to build up in the body. Phenylketonuria is an internal disorder. delayed development, failure to thrive, short stature, or slow growth

Black has stated that genetic causes often involve the mutation of multiple genes and have identified at least five chromosomes: 1, 12, 14, 19, and 21 (Black, 2009, p. 1894). Four genetic loci have also been identified as contributing to AD, including the amyloid precursor gene, the presenilin 1 gene, the presenilin 2 gene, and the apolipoprotein E gene on chromosome 19. Though there is not enough conclusive research to directly link AD to environmental factors (such as toxins or head trauma) or personal health (diabetes, vascular disease, heart and stroke), these issues are known to contribute to the destruction of brain cells. Understanding the etiology of brain cell loss is relevant to understanding how to effectively prevent the loss of function in the brain. For example, preventing the formation of chemicals called free radicals with antioxidants can indirectly prevent AD. Other causes of brain cell loss include a neurotransmitter called glutamate and an accumulation of beta amyloid proteins. Therefore, although the cause of AD has been unidentifiable, many contributing factors have been observed.

According to the CDC, autism spectrum disorder (ASD) is an umbrella term that includes a group of developmental disabilities that can cause significant social, communication and behavioral challenges. It affects a significant number of individuals in the United States, with the prevalence continuing to grow (Frye, 2014). A significant proportion of individuals with ASD also experience medical conditions such as epilepsy. In fact, treatment resistant epilepsy appears to have a higher prevalence in children with ASD than in children without ASD (Frye 2014). Many children with ASD also appear to have underlying metabolic conditions, including disorders of vitamin metabolism. Biotin, a vitamin of the B complex, is composed of ureido ring fused with a tetrahydrothiophene ring and is involved in the regulation of metabolism amongst many other vital life functions. Biotinidase deficiency is caused by mutations in BTD gene (located on the short p arm of chromosome 3 at position 25), which results in a deficiency of the biotinidase enzyme, an enzyme that is needed to recycle biotin, an essential cofactor for several carboxylase enzymes (Frye, 2014). Symptoms include seizures, developmental delays, skin rash, alopecia, seborrheic dermatitis, feeding difficulties, vomiting, diarrhea, brain atrophy and ataxia. (Frye, 2014). The identification and treatment of biotin disorders could improve the underlying metabolic derangements and potentially improve behavior and seizure frequency

Large neutral amino acid supplements can be consumed; they block phenylalanine from entering the brain. They can also lower the plasma phenylalanine levels. However, it has been suggested that taking large neutral amino acid supplements has no effect on those who maintain a phenylalanine restricted diet. Sapropterin is another supplement that can be used to lower phenylalanine levels. A study found that those taking 10mg/kg/day of sapropterin had a 30% reduction of plasma phenylalanine levels; of those 30%, 10% of the people had phenylalanine levels higher than 1200 µmol/L. There is also an alternative enzyme therapy under investigation for patients with PKU. This enzyme is an injectable form of phenylalanine ammonium lyase, also known as PegPAL, which is supposed to substitute phenylalanine hydroxylase. This pharmacologic treatment is being investigated for those who do not respond to the treatment of

In the United States, Phenylketonuria (PKU) affects about 1 in 10,000 to 15,000 newborn babies, making it a very uncommon genetic disorder (U.S National Library of Medicine, 2016). Phenylketonuria stems from an abundant buildup of an essential amino acid called phenylalanine that can become very dangerous when it reaches excessive levels (U.S.National Library of Medicine, 2016). The excessive buildup of phenylalanine is caused by an alteration in the gene which codes for the enzyme known as phenylalanine hydroxylase (PAH), which functions in breaking down the aforementioned essential amino acid phenylalanine (U.S National Library of Medicine, 2016). This genetic mutation is caused by an autosomal, recessive genetic mutation in chromosome 12 (Genetic Science Learning Center, 2016).

As previously stated, hyperammonemia is metabolic condition that expresses symptoms of high levels of ammonia within the blood stream. As a result, there are increased levels of nitrogen, which are toxic for the patient’s brain (1). However, nitrogen can be removed from the body by a less toxic substance known as urea. Urea plays a significant role in nitrogen metabolism. The target enzyme for treatment for people with hyperammonemia will be from the urea cycle. The urea cycle occurs partially in the mitochondria and mostly in the cytosol.

One of the world’s most rare inherited genetic disorders, Phenylketonuria is an autosomal recessive condition that affects 1 out of every 15,000 people in the U.S. It’s well known for causing brain damage and mental disabilities, and central nervous system damage amongst other irreversible symptoms. Although it can now be tested for and is treatable today, it limits what foods the body can eat without serious harm. Phenylketonuria is a metabolic disorder involved with chemical imbalances of proteins and paves the way for harsh symptoms, developmental disabilities, and an incredibly strict diet.

Phenylketonuria (PKU) is an error of the metabolism discovered in 1934 by Ivar Asbjørn Følling. Phenylketonuria leads to a decreased metabolism of the amino acid phenylalanine. Phenylketonuria is a genetic disorder inherited from the parents, and both parents must have this enzyme deficiency in order for the child to be affected. Mutations in the PAH gene result in PKU, this results in low levels of the enzyme phenylalanine hydroxylase. If low levels of phenylalanine hydroxylase are produced then there is a buildup of dietary phenylalanine, which are toxic and harmful if not broken down. A rise in phenylalanine can lead to many intellectual disabilities as well as other health problems. There are two main types, the basic one is PKU(which