High impact information on Tpi1

• Enhanced association of mutant triosephosphate isomerase to red cell membranes and to brain microtubules [1].
• The procedure was based on the reduction of a tetrazolium salt as final electron acceptor and a multistep reaction using the exogenous or endogenous auxiliary enzymes aldolase, triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase [2].
• The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function [3].
• Screening a rat heart cDNA library, we identified two potential interacting proteins to be the glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and triose-phosphate isomerase [3].
• This approach has also shown that triosephosphate isomerase, aconitate hydratase, M-protein, nucleoside diphosphate kinase B, and myoglobin are S-thiolated during post-ischemic reperfusion [4].

Biological context of Tpi1

• Under these conditions, regulation and posttranslational modification were observed for glyceraldehyde 3-phosphate dehydrogenase, triosephosphate isomerase, heterogeneous nuclear ribonucleoprotein A2/B1 and heterogeneous nuclear ribonucleoprotein A3, similar to the observed changes in vivo [5].
• Binding of these metal ions is observed in the active site of the catalytic TIM barrel and in the calcium binding region (CBR) of the C2 domain [6].
• Other features support decreases in cytosolic (triose-phosphate isomerase, enolase, glycerol-3-P dehydrogenase, creatine kinase) and mitochondrial (isocitrate dehydrogenase, cytochrome-c oxidase) energy metabolisms [7].

Anatomical context of Tpi1

• The GAPDH, but not TPI, activity of spermatozoa incubated with ACH and CHOP was highly correlated with kinematic parameters of spermatozoa incubated in pyruvate- and lactate-free medium [8].
• Identification of HNE modified proteins in two alternative model systems, human retinal pigment epithelial cells in culture (ARPE19) and human donor eyes, indicated that triosephosphate isomerase and alpha enolase are generally modified [9].
• The addition of incubation medium from thymus (TIM) to cultured pituitary cells further enhanced GnRH stimulated FSH and LH production, the effect was dose related [10].

Associations of Tpi1 with chemical compounds

• Glucose oxidation appeared to be inhibited at the triose phosphate isomerase or glyceraldehyde 3-phosphate dehydrogenase reaction [11].
• This indicates the operation of a substrate cycle between extracellular glycerol and liver triose phosphates, where 2H is lost in the reversible reactions catalyzed by alpha-glycerophosphate dehydrogenase, triose-phosphate isomerase, and glycolytic enzymes [12].
• These included the LDL receptor-related protein 2, ATP synthase alpha chain, heat shock protein 90 beta, hydroxyacid oxidase 3, serum albumin precursor, triose phosphate isomerase, and lamin [13].
• The enzymatic analysis of fructose-1,6-diphosphate by a coupled assay utilizing triose-phosphate isomerase, glycerol-3-phosphate dehydrogenase and aldolase was carried out in rat serum and human plasma after fructose-1,6-diphosphate administration [14].
• The results indicated that the escape from deuteration amounted to about 46% at the phosphoglucoisomerase level, 100% at the phosphomannoisomerase level, 65% in the reactions catalyzed by phosphofructoaldolase and triose phosphate isomerase, and 58% at the level of glutamate pyruvate transaminase [15].

Other interactions of Tpi1

• Glucose-6-phosphate isomerase, phosphoglycerate kinase, enolase, lactate dehydrogenase, and most of triosephosphate isomerase remained unbound [16].
• The incorporation would arise by rapid equilibration of hexose phosphates through phosphoglucose isomerase, transaldolase and triose phosphate isomerase [17].
• Another one was highly similar to rabbit dystrobrevin and the other two clones were identical to rat triose phosphate isomerase and calnexin [18].

References