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Disorders of blood and immune function
Published in Angus Clarke, Alex Murray, Julian Sampson, Harper's Practical Genetic Counselling, 2019
Other red cell enzyme defects are mostly autosomal recessive, with the exception of phosphoglycerate kinase deficiency, which is X-linked. Some are confined to the red cell, others have generalised clinical effects (e.g. triose phosphate isomerase deficiency). Prenatal diagnosis from fetal blood is a possibility for this group but, as the genes have been cloned and sequenced, DNA analysis is generally preferable, being available much earlier in pregnancy.
Carbon Dioxide Sequestration by Microalgae
Published in Gokare A. Ravishankar, Ranga Rao Ambati, Handbook of Algal Technologies and Phytochemicals, 2019
G.V. Swarnalatha, Ajam Shekh, P.V. Sijil, C.K. Madhubalaji, Vikas Singh Chauhan, Ravi Sarada
The supplementation of CO2 and its assimilation in microalgal cells are dependent on the photosynthetic CO2 fixation, known as the Calvin cycle. It has been observed that the CO2 supplementation up-regulated the genes encoding the major enzymes in the Calvin cycle. Phosphoglycerate kinase (PGK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are up-regulated. It catalyzes the phosphorylation and reduction of 3-carbon intermediates, respectively, in the presence of ATP and NADPH to generate glyceraldehyde-3-phosphate. This up-regulation of the Calvin cycle by CO2 supplementation shows higher CO2 fixation by microalgae resulting in increased biomass production. Even so, it is reported that the higher CO2 concentration inhibited the photosynthetic efficiency of microalgae. According to Winck et al. (2016), at 10% CO2 supplementation sucrose was reduced, and the xylose was accumulated, which is a clear indication of inhibition of photosynthesis. These results also suggest that photorespiration or an alternative pathway with similar substrates and products may be modulated in cells at a high CO2 concentration. It has been observed that the gene encoding the ferredoxin was up-regulated by CO2 supplementation which is suggested to enhance the Calvin cycle and carbohydrate synthesis (Peng et al. 2016; Zhu et al. 2017).
Human Erythroenzymopathies Of The Anaerobic Embden-Meyerhof Glycolytic And Associated Pathways
Published in Ronald L. Nagel, Genetically Abnormal Red Cells, 2019
Ernst R. Jaffé, William N. Valentine
Phosphoglycerate kinase catalyzes the reversible interconversion of 3-phosphoglycerate (3-PG) and 1,3-diphosphoglycerate (1, 3-DPG), the first ATP-generating step in glycolysis:
Effects of the Cobalt-60 gamma radiation on Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase
Published in International Journal of Radiation Biology, 2022
Abdelghani Iddar, Mohammed El Mzibri, Adnane Moutaouakkil
Due to the abundance of proteins in the cell, their reactivity with the products of water radiolysis is higher. The free radicals formed react with proteins, nucleic acids and lipids, which leads to their damage. Understanding the action of free radicals on proteins should provide a better understanding of the biological processes for cells adaptation to radiation (Headlam and Davies 2003; Kowalczyk et al. 2008). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key enzyme of the glycolytic pathway, found at high concentrations and with multitude of functions in the eukaryotic organisms (Punt et al. 1990). GAPDH has been studied virtually in all organisms and all glycolytic GAPDHs are homotetrameric, which have been remarkably conserved during evolution (Cerff 1995). The enzyme catalyzes the reversible phosphorylation and oxidation of glyceraldehyde-3-phosphate to generate 1,3-diphosphoglycerate, which is used by phosphoglycerate kinase to produce the adenosine triphosphate (ATP) (Forthergill-Gilmore and Michels 1993). In addition, GAPDH has been shown to play vital other roles in eukaryotic metabolism related to the cell cycle, cancer, apoptosis, proteins regulation, gene transcription, DNA replication, DNA repair, and nuclear ribonucleic acid (nRNA) export (Morgenegg et al. 1986; Meyer-Siegler et al. 1991; Singh and Green 1993; Zheng et al. 2003; Tarze et al. 2007; Kornberg et al. 2010; Das et al. 2016). On the other hand, it has been indicated that GAPDH expression is modified by various cell stress and it is involved in regulation of ROS in cells (Hara et al. 2005; Fourrat et al. 2007; Henry et al. 2015).
Glycometabolic rearrangements–aerobic glycolysis in pancreatic ductal adenocarcinoma (PDAC): roles, regulatory networks, and therapeutic potential
Published in Expert Opinion on Therapeutic Targets, 2021
In addition, other glycolytic enzymes are also involved in regulating aerobic glycolysis in PDAC and further influence the biological functions of PDAC cells. Aldolase A (ALDOA) is found to be overexpressed in PDAC patients with poor prognosis, and when it is knocked down, it not only leads to reduced glycolytic flux but also suppresses the expression of HIF-1α and even promotes the proliferation and metastasis of PDAC cells [64,65]. By analysing data based on clinical specimens, GAPDH is overexpressed in PDAC tumors compared to normal tissues [41]. The further study reveals that increased GAPDH mRNA and protein expression is associated with enhanced glycolysis in PDAC [13]. And phosphoglycerate kinase 1 (PGK1) is significantly elevated in both serum and tumor tissues of PDAC patients [66]. In particular, upregulation of PGK1 is observed in SMAD4-negative PDAC, enhancing glycolysis and tumor aggressiveness and affecting the overall survival of patients [67]. Microarray data from human PDAC tissues and cell lines shows differences in ENO1 mRNA and protein expression levels between tumors and normal pancreas tissues [68], which also occurs in LDHA mRNA and protein expression [69,70]. LDHA knockdown inhibits aerobic glycolysis and growth of PDAC cells and promotes cell migration [70,71].
Screening tools for hereditary hemolytic anemia: new concepts and strategies
Published in Expert Review of Hematology, 2021
Elisa Fermo, Cristina Vercellati, Paola Bianchi
Hereditary hemolytic anemias may also be caused by deficiencies of enzymes of the erythrocyte metabolism, that is composed by three main pathways: glycolysis, the main source of metabolic energy in the erythrocytes, pentose phosphate pathway, and nucleotide metabolism. G6PD deficiency is the most widespread erythroenzymopathy, and is usually associated with acute hemolysis caused by oxidative stress, with the exception of the class-I variants, that result in chronic hemolytic anemia. Pyruvate kinase (PK) deficiency is the most frequent enzymopathy affecting glycolysis, followed by glucose ephosphate isomerase (GPI), whereas pyrimidine 5′-nucleotidase (P5′N) and adenylate kinase (AK) deficiency involve the nucleotide metabolism. Some enzymes, such as triose phosphate isomerase (TPI), phosphoglycerate kinase (PGK) and phosphofructokinase (PFK), are not confined to the red cells but also expressed in other tissues; in such cases, hemolytic anemia may be accompanied to non-hematological symptoms such as myopathy, neuromuscular impairment and mental retardation [5–7].