FAQ - Glucosephosphate Dehydrogenase Deficiency
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Pyruvate dehydrogenase complex deficiency?

My nephew was diagnosed with Pyruvate dehydrogenase complex deficiency 2 years ago. I have never been able to understand it. Can anyone give me some information on it? Or point me in the right direction for good information please?

Pyruvate dehydrogenase complex deficiency (PDCD) is one of the most common neurodegenerative disorders associated with abnormal mitochondrial metabolism. The citric acid cycle is a major biochemical process that derives energy from carbohydrates. Malfunction of this cycle deprives the body of energy.

PDCD is a rare disorder. Several hundred cases of PDCD have been reported. Most mutations are sporadic, and the recurrence rate is very low. The true occurrence of this disorder is unknown because mild mutations of the E1 alpha enzyme subunit gene on the X chromosome may be asymptomatic, especially in females.

Individuals with neonatal- and infantile-onset types of PDCD usually die during the first years of life. Later childhood onset of the disease is usually, but not always, associated with survival into adulthood.

Some therapies may extend the lives of individuals who are severely affected with PDCD; however, the progressive nature of the neurological deterioration results in significant morbidity.

-Evaluation by an expert in metabolic and genetic disease is necessary to confirm the diagnosis, guide the appropriate treatment, and determine the prognosis.
-Genetic counseling for the parents of the individual with PDCD is important in order to estimate the recurrence risk for future pregnancies.
-Progressive renal failure is common in PDCD. A nephrologist should be consulted if signs of renal failure are evident.
-Anesthesia can be complicated by PDCD. An anesthesiologist should be consulted prior to procedures that require anesthesia.  (+ info)

What are the causes and effects of Glucose-6-Phosphate Dehydrogenase Deficiency?

Glucose-6-phosphatase dehydrogenase (G-6-PD) deficiency is the most common disease-producing enzymopathy in humans. Inherited as an X-linked disorder, G-6-PD deficiency affects 400 million people worldwide. The disease is highly polymorphic, with more than 300 reported variants. It confers protection against malaria, which probably accounts for its high gene frequency.

The G6PD enzyme catalyzes the oxidation of glucose-6-phosphate to 6-phosphogluconate while concomitantly reducing the oxidized form of nicotinamide adenine dinucleotide phosphate (NADP+) to nicotinamide adenine dinucleotide phosphate (NADPH). NADPH, a required cofactor in many biosynthetic reactions, maintains glutathione in its reduced form.

Reduced glutathione acts as a scavenger for dangerous oxidative metabolites in the cell. With the help of the enzyme glutathione peroxidase, reduced glutathione also converts harmful hydrogen peroxide to water. Red blood cells rely heavily upon G-6-PD activity because it is the only source of NADPH that protects the cells against oxidative stresses; therefore, people deficient in G-6-PD are not prescribed oxidative drugs because their red blood cells undergo rapid hemolysis under this stress.

The five classes of G-6-PD deficiency include low, normal, or increased levels of the enzyme.

Internationally: The highest prevalence rates (with gene frequencies from 5-25%) are found in tropical Africa, the Middle East, tropical and subtropical Asia, some areas of the Mediterranean, and Papua New Guinea.
Mortality/Morbidity: The most common clinical feature is a lack of symptoms. Symptomatic patients present with neonatal jaundice and acute hemolytic anemia.

Neonatal jaundice: Jaundice usually appears by age 1-4 days, at the same time as or slightly earlier than so-called physiological jaundice and later than in-blood group alloimmunization. Kernicterus is a rare complication.
Acute hemolytic anemia: Clinical expression results from stress factors such as oxidative drugs or chemicals, infection, or ingestion of fava beans.
Race: G-6-PD deficiency affects all races. The highest prevalence is among persons of African, Asian, or Mediterranean descent. Severity varies significantly between racial groups because of different variants of the enzyme. Severe deficiency variants primarily occur in the Mediterranean population. The enzymatic variants in the African population have more activity and produce a milder form of the disease.

G-6-PD deficiency is an X-linked inherited disease that primarily affects men.
Homozygous women are found in populations in which the frequency of G-6-PD deficiency is quite high.
Heterozygous (carrier) women can develop hemolytic attacks.  (+ info)

I had G6DP Deficiency (Glucose-6 Phosphate Dehydrogenase Deficiency), please advise me what kind of medicine?

please advise me what kind of medicine I can take when I have an headache or catch a flu, catch a cold... since I can not take aspirin, acetaminophen, Vitamin C.
Thank you very much for your help.

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does the prune juice cause harm to a Glucose-6-phosphate dehydrogenase deficiency(g6pd) positive?

i have a neighbor whose baby is g6pd positive and when the baby drank prune juice his face turn black and is coughing badly...

No, drinking prune juice will hyper ventilate the circular quadrants of the upper depository receptacle, and if not closely watched, could cause a person to become hypo glycemic, a diabetic quadro placegic, over and over again.
It happened to a friend of mine and now he is a she.  (+ info)

Why can't alcohol dehydrogenase enzymes be injected into yourself to lower your tolerance to alcohol?

I read that alcohol dehydrogenase enzymes are what help you process alcohol and after years of drinking you develop a deficiency in these enzymes, therefore making your tolerance higher (you need to drink more to get the same "drunk" feeling).

My question is: Why can't we just medically raise our levels of these enzymes back up to where they used to be, or even higher, so that we get drunk faster and therefore drink less?

Likewise, why isn't there a treatment for alcoholism that tries to balance this enzyme to a "normal" level in order to more normalize someone's drinking habits?
to answer the first reply, acetaldehyde dehydrogenase will detoxify acetaldehyde to acetic acid. Is that still as fatal?

It might be LETHAL to drink alcohol in such a case . The enzyme breaks alcohol down to toxic compounds , acetaldhyde being the main one .
Acetaldehyde and other preliminary toxic results are FURTHER processed by OTHER enzyme systems to give an energy rich molecule called "acetyl coenzyme-A " .

So if the enzyme on the first limb of that process (dehydrogenase) was injected WITHOUT the enzymes of the second limb , the toxic metabolites (like acetaldhyde) will accumulate FASTER than the normal levels of the enzymes of the second limb CAN ACCOMODATE .
That will result in a spike in acetaldhyde level with even little alcohol intake , potentially leading to death or blindness etc

You mean inject BOTH enzymes ?
Well that might work except that I doubt those reactions actually take place in serum . The enzyme conversion , at least the final steps (beginning with acetaldhyde) takes place EXCLUSIVELY in HEPATOCYTES (liver cells) , inside the cell environment .
An injected enzyme might work for reactions in the blood stream , but not for intracellular reactions , unless it is also modified to cross the cell wall and enter the hepatocyte .

Acetic acid = acetyl coenzymeA (acetic acid BOUND to a carrier ) , it is not toxic , it is an energy storage molecule that is produced during cell respiration and metabolism of fat .

I have a problem understanding this . It ultimately depends on what EXACTLY causes drunkenness : free alcohol or its metabolites .

The explanation of tolerance by a deficiency in metabolizing enzymes is contradictory .
It means that chronic drinkers will have higher blood alcohol levels than normal people with for the same amount of ingested alcohol , since it will not be metabolized .

That also means that drunkenness is NOT caused by alcohol itself , but rather by it's metabolites .

Even in such a state , the amount of drunkenness cannot be increased by increasing the enzyme concentration simply because thats how enzymes work . The enzymatic reaction is limited by the amount of the precursor . So while decreasing the enzyme WILL decrease the resulting products , INCREASING the enzyme will only increase the production point to a certain level which is the optimal enzyme concentration , after that , the rate of production depends ONLY on the precursor concentration , no matter how much enzyme you add .

Hypothetically , IF the enzyme concentration CAN be manipulated , whether by injection or otherwise , it might bring the tolerance of CHRONIC drinkers to the normal level before the years of alcohol abuse , however I doubt it would decrease the normal tolerance of a normal person (so that the alcohol intake of such a person might become low)  (+ info)


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to whom should i consult for my niece's glucose 6 phosphate dehydrogenase deficiency?

she was diagnosed thru newborn screening program

her doctor  (+ info)

What is the physiological basis of elevated serum lactate and lactate dehydrogenase?

What is the physiological basis of elevated serum lactate and lactate dehydrogenase during or post myocardial infarction?

Following a myocardial infarction, levels of LDH peak at 3-4 days and remain elevated for up to 10 days. In this way, elevated levels of LDH (where the level of LDH1 is higher than that of LDH2) can be useful for determining if a patient has had a myocardial infarction if they come to doctors several days after an episode of chest pain.
Other conditions under which the test may be done:
* Anemia of vitamin B-12 deficiency
* Megaloblastic anemia
* Pernicious anemia
A typical range of lactate dehydrogenase is 105 - 333 IU/L (international units per liter).  (+ info)

What vitamin deficiency causes bumps and sores at the corners of your mouth?

My 16 month old daughter has small bumps on the inside corner of her mouth and a sore on the outside corner of one lip. Is that a sign of vitamin deficiency. She does not seem bothered by them.

Could be vitamin B12, but I am not certain.

Top Ten foods highest in vitamin B12:
http://www.healthaliciousness.com/articles/foods-high-in-vitamin-B12.php  (+ info)

What is the deficiency of food causes weight loss due to thyroid disorder?

I am taking methimozole along with multivitimins tablets for thyroid disorder for the last 10 days. I have been prescribed these medicines for two months. In addition to it, what food I should take more to meet the deficiency. I have no other health problem. I am regularly doing physical exercises for the last 10 years. I wonder how it happened? can any expert please explain?

Hyperthyroidism is characterized by hypermetabolism and elevated serum levels of free thyroid hormones. Symptoms are many but include tachycardia, fatigue, weight loss, and tremor. Diagnosis is clinical and with thyroid function tests. Treatment depends on cause.(Merck)
Major clinical signs of Hyperthyroidism include weight loss (often accompanied by a ravenous appetite), anxiety, intolerance to heat, fatigue, hair loss, weakness, hyperactivity, irritability, apathy, depression, polyuria, polydipsia, and sweating.(Wikipedia)
Methimazole is used to treat hyperthyroidism, a condition that occurs when the thyroid gland produces too much thyroid hormone. It is also taken before thyroid surgery or radioactive iodine therapy.(MedlinePlus)
Methimazole and propylthiouracil are used to treat conditions in which the thyroid gland produces too much thyroid hormone.
These medicines work by making it harder for the body to use iodine to make thyroid hormone. They do not block the effects of thyroid hormone that was made by the body before their use was begun.(MayoClinic).  (+ info)

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