Alpha-1-antitrypsin deficiency *Gene map locus 14q32.1 [Clinical features: emphysema, liver disease] [Inheritance: autosomal recessive] </ < td> </< td> </ < td> Brain haemorrhage in five infants with coagulopathy A comparative ultrastructural and molecular biological study on Chlamydia psittaciinfection in alpha-1 antitrypsin deficiency and non-alpha-1 antitrypsin deficiency emphysema versus lung tissue of patients with hamartochondroma A comparative ultrastructural and molecular biological study on Chlamydia psittaciinfection in alpha-1 antitrypsin deficiency and non-alpha-1 antitrypsin deficiency emphysema versus lung tissue of patients with hamartochondroma Archives of Disease in Childhood BMC Infectious Diseases BMC Infectious Diseases </< td> </< td> </< td> Normal Diffusing Capacity in Patients With PiZ {alpha}1- Antitrypsin Deficiency, Severe Airflow Obstruction, and Significant Radiographic Emphysema Normal Diffusing Capacity in Patients With PiZ {alpha}1- Antitrypsin Deficiency, Severe Airflow Obstruction, and Significant Radiographic Emphysema Normal Diffusing Capacity in Patients With PiZ {alpha}1- Antitrypsin Deficiency, Severe Airflow Obstruction, and Significant Radiographic Emphysema Chest Chest Chest
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Alpha-1-antitrypsin deficiency*Gene map locus 14q32.1
Alkaptonuria (blacked urine) is caused by a defective-deficiency of enzyme homogentisate 1,2 dioxygenase which results in an increase of homogentisic acid in urine.
Phenylketonuria is another genetic diseases resulting from defect in an enzyme (phenylalanine monooxygenase) involves in converting of phenylalanine to tyrosine.
Many human genetic diseases are metabolic defects that are due to the inability of the affected individual to dispose of specific dietary components.
Consequence
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HomocystinuriaThis condition occurs when an enzyme called "cystathionine beta-synthase" (CBS) is either missing or not working properly. This enzyme's job is to break down methionine. When the CBS enzyme is not working correctly, methionine and another amino acid, homocystine, build up in the blood and cause problems.
Homocystinuria, also known as Cystathionine beta synthase deficiency, is an inherited disorder of the metabolism of the amino acid methionine. It is an inherited autosomal recessive trait, which means a child needs to inherit the defective gene from both parents to be affected. This defect leads to a multisystemic disorder of the connective tissue, muscles, CNS, and cardiovascular system. Homocystinuria represents a group of hereditary metabolic disorders characterized by an accumulation of homocysteine in the serum and an increased excretion of homocysteine in the urine. Infants appear to be normal and early symptoms, if any are present, are vague.
Symptoms A family history of homocystinuria Nearsightedness Flush across the cheeks Tall, thin build Long limbs High-arched feet (pes cavus) Knock-knees (genu valgum) Pectus excavatum Pectus carinatum Mental retardation Psychiatric disease Eye anomalies:
-90% have ectopia lentis -Myopia -Glaucoma -Optic atrophy
Seizure extensive atheroma formation at young age which affects many arteries but not
the coronary arteries
PhenylketonuriaClassical PKU is caused by a defective gene for the enzyme phenylalanine hydroxylase (PAH). A rarer form of the disease occurs when PAH is normal but there is a defect in the biosynthesis or recycling of the cofactor tetrahydrobiopterin (BH4) by the patient.[6] This cofactor is necessary for proper activity of the enzyme.
The enzyme normally converts the amino acid phenylalanine to tyrosine. If, due to a faulty or missing enzyme, this reaction does not take place, levels of phenylalanine in the body can be far higher than normal, and levels of tyrosine lower than normal.
Untreated children with classic phenylketonuria are normal at birth, but fail to attain early developmental milestones, develop microcephaly, and demonstrate progressive impairment of cerebral function. Hyperactivity, seizures, and severe mental retardation are major clinical problems later in life. Electroencephalographic abnormalities; “mousy” odor of skin, hair, and urine (due to phenylacetate accumulation); and a tendency to hypopigmentation and eczema complete the devastating clinical picture. In contrast, affected children who are detected and treated at birth are less likely to develop neurological problems and have seizures and mental retardation, though such clinical disorders are still possible.
Gene therapy is the introduction of genetic material into cells for therapeutic purposes.
Recent scientific breakthroughs in the genomics field and our understanding of the important role of genes in disease has made gene therapy one of the most rapidly advancing fields of biotechnology with great promise for treating inherited and
acquired diseases.
Many human diseases are caused by the absence or inappropriate presence of a protein. The protein could then be administered to patients in order to compensate for its absence. Today, gene therapy is the ultimate method of protein delivery, in which the delivered gene enters the body's cells and turns them into small "factories" that produce a therapeutic protein for a specific disease over a prolonged period.
As gene therapy has moved from the laboratory into the clinic, several issues have emerged as central to the development of this technology: gene identification, gene expression and gene delivery. A number of disease-related genes with direct clinical have already been identified, and this number is growing as the field rapidly advances. Genes with broader clinical application are also being utilized to make cells express immune activating agents locally at the disease site or to become susceptible to further drug treatment or to immune response recognition.
