Do adults with phenylketonuria need to eat special food?

Written by Zeng Hai Jiang
Pediatrics
Updated on December 10, 2024
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Phenylketonuria may not necessarily require a special diet in adulthood. It is the first genetic metabolic disorder that can be treated through dietary control. Natural foods all contain a certain amount of phenylalanine, so once children with phenylketonuria are diagnosed, they should stop their natural diet and instead be given a low-phenylalanine diet. Low-phenylalanine formula treatment should continue at least until the age of 12. When the concentration of phenylalanine in the blood is controlled at an ideal level, a gradual addition of natural foods can be made. Larger infants and children can add foods such as milk, porridge, noodles, and eggs. However, these added foods should still primarily be low in protein and low in phenylalanine.

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Written by Zeng Hai Jiang
Pediatrics
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Can phenylketonuria be detected before a newborn is born?

Phenylketonuria can be screened prenatally before the birth of a newborn. The procedure involves genetic screening using amniotic fluid drawn through amniocentesis between the 16th and 20th week of pregnancy. Phenylketonuria is an autosomal recessive hereditary disease, greatly associated with chromosomal abnormalities. If chromosomal abnormalities are detected through amniocentesis, indicating the presence of pathogenic genes, it confirms that the fetus will be born with phenylketonuria. If both parents carry the relevant genes, prenatal screening is still necessary to rule out the risk of the disease in the fetus.

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Written by Yan Xin Liang
Pediatrics
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The causes of phenylketonuria

Phenylketonuria is a common autosomal recessive genetic disorder, the most frequent primary clinical manifestation among congenital amino acid metabolic disorders. It is characterized by intellectual disability, pale skin and hair pigmentation, and a mouse urine-like odor. The main cause is that phenylalanine is an essential amino acid for the human body. The phenylalanine ingested is partly used for protein synthesis and partly converted to tyrosine by the action of phenylalanine hydroxylase, which is necessary for the synthesis of substances like adrenaline, melanin, and thyroxine. The disease is mainly due to a deficiency of phenylalanine hydroxylase, which inhibits the conversion of phenylalanine to tyrosine, resulting in increased concentrations of phenylalanine in the blood, cerebrospinal fluid, and various tissues. At the same time, due to the predominance of the main pathway, the enhancement of the secondary metabolic pathway leads to the deamination of phenylalanine by transaminase, producing a large amount of phenylpyruvic acid, which through oxidation produces a large amount of phenylacetic acid, phenyllactic acid, and p-hydroxyphenylpyruvic acid. These metabolic by-products are excreted in large quantities in the urine, and the high concentrations of phenylalanine and its by-products accumulate extensively in brain tissue, thereby causing damage to brain cells.

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Written by Zeng Hai Jiang
Pediatrics
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Does phenylketonuria require chromosome testing?

Phenylketonuria is usually screened during the neonatal period through routine blood testing, where the level of phenylalanine in the blood is measured to screen each newborn. This enables early diagnosis and treatment, hence reducing the occurrence of intellectual disabilities. Phenylketonuria can also be screened prenatally before the birth of the newborn. It is an autosomal recessive genetic disorder, closely related to chromosomal abnormalities. Therefore, prenatal screening can be conducted by amniocentesis between the 16th to 20th weeks of pregnancy. Chromosomal abnormalities detected through the amniocentesis indicate that the fetus carries the pathogenic gene, meaning the child will be born with phenylketonuria. If both parents carry related genes, it is crucial to undergo prenatal screening and chromosomal analysis to eliminate the risk of the fetus developing the condition.

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Written by Hu Qi Feng
Pediatrics
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Mechanism of phenylketonuria

Phenylketonuria is characterized by reduced activity of phenylalanine hydroxylase, which fails to convert phenylalanine to tyrosine, causing extremely elevated levels of phenylalanine in the blood, cerebrospinal fluid, and tissues. This leads to the production of large amounts of phenylpyruvic acid, phenylacetic acid, phenyllactic acid, and p-hydroxyphenylacetic acid via alternative pathways. High concentrations of phenylalanine and its metabolic products can cause brain damage, which manifests as developmental intellectual disabilities, changes in skin and hair pigmentation, and a mousy urine odor, all part of a clinical syndrome.

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Written by Yan Xin Liang
Pediatrics
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How is phenylketonuria cured?

Phenylketonuria is an autosomal recessive genetic disease, primarily due to a mutation in the phenylalanine hydroxylase gene which leads to reduced enzymatic activity, causing the accumulation of phenylalanine and its metabolites in the body, thereby leading to this disease. The main manifestations include developmental intellectual disabilities, light skin and hair pigmentation, and a musty urine odor. Once diagnosed, immediate treatment is necessary, mainly using a low-phenylalanine formula milk. Generally, when orally administering low-phenylalanine formula milk, it is essential to monitor the phenylalanine levels in the blood. Since each patient has a different tolerance level for phenylalanine, periodic determination of blood phenylalanine concentration is required in the dietary treatment. Such patients can only be treated long-term in this way; it is not curable nor can it be completely eradicated; treatment can only alleviate the symptoms and involves long-term administration of a low-phenylalanine diet.