Disease relevance of PISD

• Unexpectedly, the PISD fibres behave like paranodally demyelinated ones, since the myelin reduction increases slightly the effect of the paranodal demyelination on the nerve membrane properties [1].

High impact information on PISD

• We propose to employ structure similarity clustering of the ligand-sensing cores of protein domains (PSSC) in conjunction with natural product guided compound library development as a synergistic approach for the identification of biologically prevalidated ligands with high fidelity [2].
• These data provide compelling evidence that phosphatidylethanolamine synthesis via phosphatidylserine and phosphatidylserine decarboxylase contributes significantly to membrane biogenesis in mammalian cells [3].
• Protein structure similarity clustering (PSSC) and natural product structure as inspiration sources for drug development and chemical genomics [4].
• The donor cells were poisoned with hydroxylamine which irreversibly inactivates phosphatidylserine decarboxylase and will prevent the conversion of nascent phosphatidylserine to phosphatidylethanolamine [5].
• The inhibition of phosphatidylserine turnover could not be attributed to inhibition of either phosphatidylserine decarboxylase or phosphatidylserine exchange protein activity [6].

Biological context of PISD

• Towards developing a protein infrared spectra databank (PISD) for proteomics research [7].
• However, ageing lenses or lenses under oxidative stress show an extensively diminished size of GSH pool with some protein thiols being S-thiolated by oxidized non-protein thiols to form protein-thiol mixed disulfides, either as protein-S-S-glutathione (PSSG) or protein-S-S-cysteine (PSSC) or protein-S-S-gamma-glutamylcysteine [8].
• These results suggest that (i) there is a spatial difference in the patterns of fungal gene expression between ECM and EM, (ii) urea and polyamine transporters could facilitate the translocation of nitrogen compounds within the EM network, and (iii) fungal Psd may contribute to membrane remodeling during ectomycorrhiza formation [9].
• A phosphatidylserine decarboxylase activity in root cells of oat (Avena sativa) is involved in altering membrane phospholipid composition during drought stress acclimation [10].
• These results strongly suggest that sphingosine, sphingosylphosphorylcholine and sphingosine 1-phosphate can modulate cellular phospholipid homeostasis by stimulation of phosphatidylserine synthesis and an interference with phosphatidylserine decarboxylase [11].

Anatomical context of PISD

• We also review recent studies on phosphatidylethanolamine biosynthesis by two pathways: the CDP-ethanolamine pathway, which is active in the endoplasmic reticulum, and the phosphatidylserine decarboxylase pathway, which operates in mitochondria [12].

Associations of PISD with chemical compounds

• Polysaccharide O-antigen side chains (PSSC) of LPS from serum-resistant clones contained 12%-40% more of the longer carbohydrate molecules (L-PSSC) than did LPS from serum-sensitive parent strains; in contrast, 12%-27% more of the shorter PSSC (S-PSSC) were found in LPS from serum-sensitive strains [13].
• Protein S-thiolation is a process in which under oxidative stress, vulnerable sulfhydryl groups of proteins are conjugated to non-protein thiols such as glutathione (GSH) or cysteine resulting in the formation of protein-thiol mixed disulfides, protein-S-S-glutathione (PSSG) and protein-S-S-cysteine (PSSC) [14].
• This study focused on the comparison of the intensities of nuclear opacity and pigmentation (brunescence) with the changes in free glutathione (GSH) and the three species of protein-thiol mixed disulfides: protein-S-S-glutathione (PSSG), protein-S S-cysteine (PSSC) and protein-S-S-gamma-glutamylcysteine (PSSGC) [15].
• Recombinant human lens thioltransferase (RHLT), which was isolated and purified previously in this laboratory, reactivated these pure glycolytic enzymes inactivated by forming protein-S-S-gluthathione (PSSG), protein-S-S-cysteine (PSSC) or, protein-S-S-cysteamine after thiolating with oxidized glutathione, cystine or cystamine respectively [16].
• Plasma concentrations of D-penicillamine, PSSP and PSSC displayed similar characteristics in terms of times to maximum concentrations and biphasic elimination from plasma [17].

Other interactions of PISD

• Phosphatidylserine synthase is found predominantly in the microsomal fraction, and phosphatidylserine decarboxylase is found predominantly in the mitochondrial fraction of baby hamster kidney (BHK-21) cells [6].
• Labeled precursor incorporation experiments have shown that phosphatidylserine decarboxylase and phosphatidylethanolamine N-methyltransferase are more active in cells infected by E. cuniculi than in uninfected cells [18].

Analytical, diagnostic and therapeutic context of PISD

• Hence, if we want to build reliable pattern recognition based systems to support proteomics research, which are capable of making good predictions from spectral data of any unknown protein, one common goal should be to build a comprehensive protein infrared spectra databank (PISD) containing FTIR spectra of proteins of known structure [7].
• We have observed an elevation of protein S-S-glutathione (PSSG) and protein-S-S-cysteine (PSSC) in cataractous lenses from humans and from animal models subjected to oxidative stress [19].
• Activities of CTP:ethanolaminephosphate cytidyltransferase (EC 2.7.7.14), phosphatidylserine decarboxylase (EC 4.1.1.65) and phosphatidylserine synthase; CDP-DAG:L-serine o-phosphatidyltransferase (EC 2.7.8.8) were measured and additionally, the presence of a PS decarboxylase (PSD1) in oat was confirmed by immunoblotting [10].

References