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AMPD3 encodes a member of the AMP deaminase gene family. Additionally we are shipping AMPD3 Antibodies (69) and many more products for this protein.
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mtDNA deletion coordinately induces AMP (show APRT Proteins) deaminase to contribute to the loss of atrial adenine nucleotides through degrading AMP (show APRT Proteins) excessively.
The primary underlying mechanism for increased catabolic flow through the AMP (show APRT Proteins) deaminase reaction in circulating erythrocytes of individuals with familial phosphofructokinase deficiency is Ca2 (show CA2 Proteins)+-calmodulin (show CALM1 Proteins) activation of AMP deaminase isoform E.
may control the systemic metabolic status by changing AMPK (show PRKAA1 Proteins) activity through the AMP (show APRT Proteins) level.
This is a first report evidencing the pattern of AMPD (show AMPD1 Proteins) genes expression in neoplastic human liver.
Data show that AMP deaminase 3 (Ampd3)-/-/5'-nucleotidase (CD73)-/- knockout mice are more sensitive to AMP (show TMPRSS5 Proteins)-induced hypometabolism than mice with a single enzyme deficiency, which are more sensitive than wild type.
depletion of the epigenome modifier histone deacetylase 3 (HDAC3 (show HDAC3 Proteins)) specifically in skeletal muscle causes severe systemic insulin (show INS Proteins) resistance in mice but markedly enhances endurance and resistance to muscle fatigue, despite reducing muscle force. This is due to lower glucose utilization and greater lipid oxidation in HDAC3 (show HDAC3 Proteins)-depleted muscles, a fuel switch caused by the activation of anaplerotic reactions driven by Ampd3.
Mice carrying the mutation exhibit rapid RBC (show CACNA1C Proteins) turnover, with increased erythropoiesis, dramatically shortened RBC (show CACNA1C Proteins) lifespan, and signs of increased RBC (show CACNA1C Proteins) senescence/eryptosis, suggesting a key role for AMPD3 in determining RBC (show CACNA1C Proteins) half-life. Mice were also found to be resistant to infection with the rodent malaria Plasmodium chabaudi.
Erythrocytes from Ampd3(-/-) mice exhibited higher half-saturation pressure of oxygen.
effect of AMP-deaminase 3 knock-out in mice on enzyme activity in heart and other organs
AMP (show TMPRSS5 Proteins) deaminase-deficient models demonstrate for the first time that AMPD3 plays a critical role in remote reperfusion lung injury via generation of inosine monophosphate (IMP (show BRAP Proteins)).
AMPD3 deficiency increases the level of ATP in erythrocytes, but does not improve anemia due to pyruvate kinase deficiency and leads to erythrocyte dysfunction.
Along with the activation of AMPD3, ischemia-reperfusion-induced lung inflammation is associated with increased MPO (show MPO Proteins) activity and TNF-alpha (show TNF Proteins) level.
This gene encodes a member of the AMP deaminase gene family. The encoded protein is a highly regulated enzyme that catalyzes the hydrolytic deamination of adenosine monophosphate to inosine monophosphate, a branch point in the adenylate catabolic pathway. This gene encodes the erythrocyte (E) isoforms, whereas other family members encode isoforms that predominate in muscle (M) and liver (L) cells. Mutations in this gene lead to the clinically asymptomatic, autosomal recessive condition erythrocyte AMP deaminase deficiency. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.
adenosine monophosphate deaminase (isoform E)
, AMP deaminase 3
, adenosine monophosphate deaminase 3
, erythrocyte adenosine monophosphate deaminase
, AMP deaminase 3-like
, AMP aminohydrolase
, erythrocyte AMP deaminase
, erythrocyte type AMP deaminase
, erythrocyte-specific AMP deaminase
, myoadenylate deaminase
, AMP deaminase H-type
, heart-type AMPD