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A novel PKLR gene mutation was identified in members of a Chinese family with hemolytic anemia.
Results show that different residues contribute to the two allosteric functions: regulation by the activator fructose-1,6-bisphosphate (Fru-1,6-BP) and alanine, the inhibitor. Only a small fraction of mutated residues perturbed inhibition by alanine. In contrast, a large percentage of mutated residues influenced activation by Fru-1,6-BP; inhibition by alanine is not simply the reverse of activation by Fru-1,6-BP.
PKLR gene sequencing in 15 Spanish patients affected by pyruvate kinase deficiency (PKD) was performed. Six out of the 18 alleles found were new mutations which had not been described previously, with the PKLR c.721G>T mutation being the most prevalent (26.67%), followed by the PKLR c.1456C>T mutation (13.33%).
Gene copy number variation (CNV) of the PKLR, FCGR2A, FCGR2C, and FCGR3 genes is associated with malaria severity, and our results provide evidence for a role of CNV in host responses to malaria.
Genotype-phenotype correlations for the novel missense mutations found in the PKLR gene in PK deficiency among Tunisian cases were investigated by three-dimensional structure analysis.
Data show that pyruvate kinase (PK) activity was decreased in the GATA1 hemizygous state and PKLR c.1284delA variant.
An update of PKLR gene mutation database has been presented. (Review)
Two Novel Missense Mutations and a 5bp Deletion in the Erythroid-Specific Promoter of the PKLR Gene in Two Unrelated Patients With Pyruvate Kinase Deficient Transfusion-Dependent Chronic Nonspherocytic Hemolytic Anemia.
PKLR promotes colorectal cancer liver colonization through induction of glutathione synthesis.
Pyruvate kinase variants modulate malaria phenotypes in a Thai population.
661G>A and 1528C>T mutations of PKLR gene are associated with pyruvate kinase deficiency.
Case Report: unknown mutation in the pyruvate kinase gene (PKLR) identified from a neonate with severe jaundice.
This study determined which interactions in the fructose 1,6-bisphosphate binding site of human liver pyruvate kinase contribute to allostery.
Partial pyruvate kinase deficiency aggravates the phenotypic expression of band 3 deficiency in a family with hereditary spherocytosis.
Hemolytic anemia associated with a novel heterozygous mutation 1183A in the pyruvate kinase gene has been found in two unrelated Jordanian patients.
11 patients from 10 unrelated pyruvate kinse deficiency families had 9 different disease-causing PKLR mutations, including 2 new ones: the point mutation c.878A>T (p.Asp293Val) and the frameshift deletion c.1553delG (p.(Arg518Leufs*12).
A new type of inherited PK hyperactivity having solely increased expression of a kinetically normal PK-R had no mutations or copy number variants. An upregulatory mutation at an unlinked site is proposed.
Herpes simplex virus type 1 virion-derived US11 inhibits type 1 interferon-induced protein kinase R phosphorylation.
A global geographical co-distribution between malaria and high frequency of PK deficiency seems to occur suggesting that malaria may be a selective force raising the frequency of this 277Lys variant.
investigation of structure-function relationship of the N-terminus of liver pyruvate kinase and its regulation by oxidation/oxidative coupling and post-translational phosphorylation
The existence of mitochondrial Pyruvate kinase was confirmed by immunological analysis in pig liver mitochondria.
AMPD3 deficiency increases the level of ATP in erythrocytes, but does not improve anemia due to pyruvate kinase deficiency and leads to erythrocyte dysfunction.
Pyruvate kinase deficiency in mice protects against malaria
the metabolic disturbance in PK deficiency alters not only the survival of red cells but also the maturation of erythroid progenitors, resulting in ineffective erythropoiesis.
The protein encoded by this gene is a pyruvate kinase that catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP, which is the rate-limiting step of glycolysis. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Multiple transcript variants encoding different isoforms have been found for this gene.
R-type/L-type pyruvate kinase
, pyruvate kinase 1
, pyruvate kinase PKLR
, pyruvate kinase isozyme R/L
, pyruvate kinase isozymes L/R
, pyruvate kinase isozymes R/L
, pyruvate kinase type L
, pyruvate kinase, liver and blood cell
, red cell/liver pyruvate kinase
, pyruvate kinase, liver and red blood cell
, pyruvate kinase, liver and RBC
, Pyruvate kinase isozyme R
, Pyruvate kinase isozymes R/L
, pyruvate kinase isozymes R/L-like
, secretory carrier-associated membrane protein 3-like