Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00750 (PLA)
 16,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

This essay reviews the discoveries, synthesis, and biological significance of prostaglandins (PGs) and other eicosanoids in insect biology. It presents the most current - and growing - understanding of the insect mechanism of PG biosynthesis, provides an updated treatment of known insect phospholipase A2 (PLA2), and details contemporary findings on the biological roles of PGs and other eicosanoids in insect physiology, including reproduction, fluid secretion, hormone actions in fat body, immunity and eicosanoid signaling and cross-talk in immunity. It completes the essay with a prospectus meant to illuminate research opportunities for interested readers. In more detail, cellular and secretory types of PLA2, similar to those known on the biomedical background, have been identified in insects and their roles in eicosanoid biosynthesis documented. It highlights recent findings showing that eicosanoid biosynthetic pathway in insects is not identical to the solidly established biomedical picture. The relatively low concentrations of arachidonic acid (AA) present in insect phospholipids (PLs) (< 0.1% in some species) indicate that PLA2 may hydrolyze linoleic acid (LA) as a precursor of eicosanoid biosynthesis. The free LA is desaturated and elongated into AA. Unlike vertebrates, AA is not oxidized by cyclooxygenase, but by a specific peroxidase called peroxinectin to produce PGH2, which is then isomerized into cell-specific PGs. In particular, PGE2 synthase recently identified converts PGH2 into PGE2. In the cross-talks with other immune mediators, eicosanoids act as downstream signals because any inhibition of eicosanoid signaling leads to significant immunosuppression. Because host immunosuppression favors pathogens and parasitoids, some entomopathogens evolved a PLA2 inhibitory strategy activity to express their virulence.
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PMID:Prostaglandins and Other Eicosanoids in Insects: Biosynthesis and Biological Actions. 3079 67

The precise degradation of dysfunctional mitochondria by mitophagy is essential for maintaining neuronal homeostasis. HTT (huntingtin) can interact with numerous other proteins and thereby perform multiple biological functions within the cell. In this study, we investigated the role of HTT during mitophagy and analyzed the impact of the expansion of its polyglutamine (polyQ) tract. HTT is involved in different mitophagy steps, promoting the physical proximity of different protein complexes during the initiation of mitophagy and recruiting mitophagy receptors essential for promoting the interaction between damaged mitochondria and the nascent autophagosome. The presence of the polyQ tract in mutant HTT affects the formation of these protein complexes and determines the negative consequences of mutant HTT on mitophagy, leading to the accumulation of damaged mitochondria and an increase in oxidative stress. These outcomes contribute to general mitochondrial dysfunction and neurodegeneration in Huntington disease.Abbreviations: AMPK: AMP-activated protein kinase; ATG13: autophagy related 13; BECN1: beclin 1, autophagy related; BNIP3: BCL2/adenovirus E1B interacting protein 3; BNIP3L/Nix: BCL2/adenovirus E1B interacting protein 3-like; CCCP: carbonyl cyanide 3-chlorophenyl hydrazone; DMEM: Dulbecco's modified eagle medium; EDTA: ethylene-diamine-tetra-acetic acid; EGFP: enhanced green fluorescent protein; EGTA: ethylene glycol bis(2-aminoethyl ether)tetraacetic acid; FUNDC1: FUN14 domain containing 1; HD: Huntington disease; HRP: horseradish peroxidase; HTT: huntingtin; LC3-II: lipidated form of MAP1LC3/LC3; mtDNA: mitochondrial deoxyribonucleic acid; MTDR: MitoTracker Deep Red; MTOR: mechanistic target of rapamycin kinase; MTORC1: mechanistic target of rapamycin kinase complex 1; NBR1: NBR1, autophagy cargo receptor; CALCOCO2/NDP52: calcium binding and coiled-coil domain 2; OCR: oxygen consumption rate; OPTN: optineurin; OXPHOS: oxidative phosphorylation; PIK3C3/VPS34: phosphatidylinositol 3-kinase catalytic subunit type 3; PIK3R4/VPS15: phosphoinositide-3-kinase regulatory subunit 4; PINK1: PTEN induced putative kinase 1; PLA: proximity ligation assay; PMSF: phenylmethylsulfonyl fluoride; polyQ: polyglutamine; PtdIns3K: phosphatidylinositol 3-kinase; ROS: reactive oxygen species; Rot: rotenone; SDS-PAGE: sodium dodecyl sulfate-polyacrylamide gel electrophoresis; SEM: standard error of the mean; SQSTM1/p62: sequestosome 1; TMRM: tetramethylrhodamine methyl ester; UB: ubiquitin; ULK1: unc-51 like kinase 1.
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PMID:Mutant HTT (huntingtin) impairs mitophagy in a cellular model of Huntington disease. 3209 70


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