Pathways

SGLT2 is a sodium/glucose co-transporter that exists almost exclusively in kidney tissue. It is responsible for approximately 90% of the kidney's reabsorption of glucose, and can be found in the S1 segment of the proximal convoluted tubule of the nephron. A defect in the SLC5A2 gene that codes for SGLT2 results in glucosuria, due to the inability of most of the glucose to be reabsorbed by the kidney. There are some drugs that inhibit SGLT2 and are used to decrease blood sugar in patients with type 2 diabetes mellitus.

SGLT2 is a sodium/glucose co-transporter that exists almost exclusively in kidney tissue. It is responsible for approximately 90% of the kidney's reabsorption of glucose, and can be found in the S1 segment of the proximal convoluted tubule of the nephron. A defect in the SLC5A2 gene that codes for SGLT2 results in glucosuria, due to the inability of most of the glucose to be reabsorbed by the kidney. There are some drugs that inhibit SGLT2 and are used to decrease blood sugar in patients with type 2 diabetes mellitus.

SGLT2 is a sodium/glucose co-transporter that exists almost exclusively in kidney tissue. It is responsible for approximately 90% of the kidney's reabsorption of glucose, and can be found in the S1 segment of the proximal convoluted tubule of the nephron. A defect in the SLC5A2 gene that codes for SGLT2 results in glucosuria, due to the inability of most of the glucose to be reabsorbed by the kidney. There are some drugs that inhibit SGLT2 and are used to decrease blood sugar in patients with type 2 diabetes mellitus.

glucose uptake

Glucose-6-phosphate dehydrogenase deficiency, also called G6PDD, is a very common inherited inborn error of metabolism (IEM) that is characterized by a defect in the glucose-6-phosphate dehydrogenase gene. Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway. G6PD converts glucose-6-phosphate into 6-phosphoglucono-delta-lactone. This reaction supplies reducing energy to cells by maintaining high levels of NADPH inside cells, especially red blood cells. NADPH helps maintain the supply of reduced glutathione that is used to eliminate free radicals that cause oxidative damage in red blood cells. G6PDD is an X-linked genetic disorder that primarily affects males and predisposes affected individuals to red blood cell breakdown, which is called hemolysis. About 400 million people (1 in 20) have G6PDD globally and it is particularly common in certain parts of Africa, Asia, the Mediterranean, and the Middle East. Carriers of the G6PDD allele may be partially protected against malaria, which explains the higher incidence of this genetic defect in people coming from countries that have or historically had malaria. While the vast majority of affected individuals are male, females can be clinically affected due to unfavourable lyonization, where random inactivation of an X-chromosome in certain cells creates a population of G6PD-deficient red blood cells coexisting with unaffected red blood cells. As noted above, G6PDD mainly affects the redox capacity of red blood cells, which carry oxygen from the lungs to tissues throughout the body. The most common medical problem associated with G6PDD is hemolytic anemia, which occurs when red blood cells are destroyed faster than the body can replace them. This type of anemia leads to paleness, yellowing of the skin and whites of the eyes (jaundice), dark urine, shortness of breath, fatigue, and a rapid heart rate. In individuals with G6PDD, hemolytic anemia is most often triggered by bacterial or viral infections or by certain drugs (such as some antibiotics, aspirin, quinine and other antimalarials derived from quinine). Hemolytic anemia can also occur after inhaling fava plant pollen or consuming fava beans (a reaction called favism). In newborns, G6PDD is also a significant cause of mild to severe jaundice. Many people with G6PDD, however, are asymptomatic.

Glucose-6-phosphate dehydrogenase deficiency, also called G6PDD, is a very common inherited inborn error of metabolism (IEM) that is characterized by a defect in the glucose-6-phosphate dehydrogenase gene. Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway. G6PD converts glucose-6-phosphate into 6-phosphoglucono-delta-lactone. This reaction supplies reducing energy to cells by maintaining high levels of NADPH inside cells, especially red blood cells. NADPH helps maintain the supply of reduced glutathione that is used to eliminate free radicals that cause oxidative damage in red blood cells. G6PDD is an X-linked genetic disorder that primarily affects males and predisposes affected individuals to red blood cell breakdown, which is called hemolysis. About 400 million people (1 in 20) have G6PDD globally and it is particularly common in certain parts of Africa, Asia, the Mediterranean, and the Middle East. Carriers of the G6PDD allele may be partially protected against malaria, which explains the higher incidence of this genetic defect in people coming from countries that have or historically had malaria. While the vast majority of affected individuals are male, females can be clinically affected due to unfavourable lyonization, where random inactivation of an X-chromosome in certain cells creates a population of G6PD-deficient red blood cells coexisting with unaffected red blood cells. As noted above, G6PDD mainly affects the redox capacity of red blood cells, which carry oxygen from the lungs to tissues throughout the body. The most common medical problem associated with G6PDD is hemolytic anemia, which occurs when red blood cells are destroyed faster than the body can replace them. This type of anemia leads to paleness, yellowing of the skin and whites of the eyes (jaundice), dark urine, shortness of breath, fatigue, and a rapid heart rate. In individuals with G6PDD, hemolytic anemia is most often triggered by bacterial or viral infections or by certain drugs (such as some antibiotics, aspirin, quinine and other antimalarials derived from quinine). Hemolytic anemia can also occur after inhaling fava plant pollen or consuming fava beans (a reaction called favism). In newborns, G6PDD is also a significant cause of mild to severe jaundice. Many people with G6PDD, however, are asymptomatic.

Glucose-6-phosphate dehydrogenase deficiency, also called G6PDD, is a very common inherited inborn error of metabolism (IEM) that is characterized by a defect in the glucose-6-phosphate dehydrogenase gene. Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway. G6PD converts glucose-6-phosphate into 6-phosphoglucono-delta-lactone. This reaction supplies reducing energy to cells by maintaining high levels of NADPH inside cells, especially red blood cells. NADPH helps maintain the supply of reduced glutathione that is used to eliminate free radicals that cause oxidative damage in red blood cells. G6PDD is an X-linked genetic disorder that primarily affects males and predisposes affected individuals to red blood cell breakdown, which is called hemolysis. About 400 million people (1 in 20) have G6PDD globally and it is particularly common in certain parts of Africa, Asia, the Mediterranean, and the Middle East. Carriers of the G6PDD allele may be partially protected against malaria, which explains the higher incidence of this genetic defect in people coming from countries that have or historically had malaria. While the vast majority of affected individuals are male, females can be clinically affected due to unfavourable lyonization, where random inactivation of an X-chromosome in certain cells creates a population of G6PD-deficient red blood cells coexisting with unaffected red blood cells. As noted above, G6PDD mainly affects the redox capacity of red blood cells, which carry oxygen from the lungs to tissues throughout the body. The most common medical problem associated with G6PDD is hemolytic anemia, which occurs when red blood cells are destroyed faster than the body can replace them. This type of anemia leads to paleness, yellowing of the skin and whites of the eyes (jaundice), dark urine, shortness of breath, fatigue, and a rapid heart rate. In individuals with G6PDD, hemolytic anemia is most often triggered by bacterial or viral infections or by certain drugs (such as some antibiotics, aspirin, quinine and other antimalarials derived from quinine). Hemolytic anemia can also occur after inhaling fava plant pollen or consuming fava beans (a reaction called favism). In newborns, G6PDD is also a significant cause of mild to severe jaundice. Many people with G6PDD, however, are asymptomatic.

Glucose-6-phosphate dehydrogenase deficiency, also called G6PDD, is a very common inherited inborn error of metabolism (IEM) that is characterized by a defect in the glucose-6-phosphate dehydrogenase gene. Glucose-6-phosphate dehydrogenase (G6PD) is an enzyme in the pentose phosphate pathway. G6PD converts glucose-6-phosphate into 6-phosphoglucono-delta-lactone. This reaction supplies reducing energy to cells by maintaining high levels of NADPH inside cells, especially red blood cells. NADPH helps maintain the supply of reduced glutathione that is used to eliminate free radicals that cause oxidative damage in red blood cells. G6PDD is an X-linked genetic disorder that primarily affects males and predisposes affected individuals to red blood cell breakdown, which is called hemolysis. About 400 million people (1 in 20) have G6PDD globally and it is particularly common in certain parts of Africa, Asia, the Mediterranean, and the Middle East. Carriers of the G6PDD allele may be partially protected against malaria, which explains the higher incidence of this genetic defect in people coming from countries that have or historically had malaria. While the vast majority of affected individuals are male, females can be clinically affected due to unfavourable lyonization, where random inactivation of an X-chromosome in certain cells creates a population of G6PD-deficient red blood cells coexisting with unaffected red blood cells. As noted above, G6PDD mainly affects the redox capacity of red blood cells, which carry oxygen from the lungs to tissues throughout the body. The most common medical problem associated with G6PDD is hemolytic anemia, which occurs when red blood cells are destroyed faster than the body can replace them. This type of anemia leads to paleness, yellowing of the skin and whites of the eyes (jaundice), dark urine, shortness of breath, fatigue, and a rapid heart rate. In individuals with G6PDD, hemolytic anemia is most often triggered by bacterial or viral infections or by certain drugs (such as some antibiotics, aspirin, quinine and other antimalarials derived from quinine). Hemolytic anemia can also occur after inhaling fava plant pollen or consuming fava beans (a reaction called favism). In newborns, G6PDD is also a significant cause of mild to severe jaundice. Many people with G6PDD, however, are asymptomatic.

The glucose-alanine cycle—also referred to in the literature as the Cahill cycle or the alanine cycle—involves muscle protein being degraded to provide more glucose to generate additional ATP for muscle contraction. It allows pyruvate and glutamate to be transported out of muscle tissue to the liver where gluconeogenesis takes place to supply the muscle tissue with more glucose as mentioned previously. To initiate the cycle, muscle and tissues that catabolize amino acids for fuel generate amino groups—most commonly in the form of glutamate—through the process of transamination. These amino groups are transferred via alanine aminotransferase to pyruvate (a product of glycolysis) to form alanine and alpha-ketoglutarate. Alanine subsequently moves through the circulatory system to the liver where the reaction previously catalyzed by alanine aminotransferase is reversed to produce pyruvate. This pyruvate is converted into glucose through the process of gluconeogenesis which subsequently is transported back to the muscle tissue. Meanwhile, glutamate dehydrogenase in the mitochondria catabolizes glutamate into ammonium. Ammonium moves on to form urea in the urea cycle.