Platelet activating-factor acetylhydrolase II: A member of phospholipase A2 family that hydrolyzes oxidized phospholipids

Dong, Linyue; Li, Yiming; Wu, Huali

doi:10.1016/j.chemphyslip.2021.105103

Cited by 8 publications

(2 citation statements)

References 82 publications

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“…PAFAH2 is a hydrolase, which was described as being able to cleave a variety of acyl-chains from phospholipids, thus functioning as a phospholipase [47]. More recently, it was shown that PAFAH2 preferentially removes oxidized phospholipids, fulfilling a protective role under oxidative stress [48]. Since the numerous peroxisomal oxidases continuously produce H 2 O 2 , phospholipid oxidation of the inner leaflet of the peroxisome membrane may be a major threat to maintaining physiological membrane properties of the organelle.…”

Section: Discussionmentioning

confidence: 99%

Analysis of the Mouse Hepatic Peroxisome Proteome—Identification of Novel Protein Constituents Using a Semi-Quantitative SWATH-MS Approach

Singin,

Astapenka,

Costina

et al. 2024

Cells

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Ongoing technical and bioinformatics improvements in mass spectrometry (MS) allow for the identifying and quantifying of the enrichment of increasingly less-abundant proteins in individual fractions. Accordingly, this study reassessed the proteome of mouse liver peroxisomes by the parallel isolation of peroxisomes from a mitochondria- and a microsome-enriched prefraction, combining density-gradient centrifugation with a semi-quantitative SWATH-MS proteomics approach to unveil novel peroxisomal or peroxisome-associated proteins. In total, 1071 proteins were identified using MS and assessed in terms of their distribution in either high-density peroxisomal or low-density gradient fractions, containing the bulk of organelle material. Combining the data from both fractionation approaches allowed for the identification of specific protein profiles characteristic of mitochondria, the ER and peroxisomes. Among the proteins significantly enriched in the peroxisomal cluster were several novel peroxisomal candidates. Five of those were validated by colocalization in peroxisomes, using confocal microscopy. The peroxisomal import of HTATIP2 and PAFAH2, which contain a peroxisome-targeting sequence 1 (PTS1), could be confirmed by overexpression in HepG2 cells. The candidates SAR1B and PDCD6, which are known ER-exit-site proteins, did not directly colocalize with peroxisomes, but resided at ER sites, which frequently surrounded peroxisomes. Hence, both proteins might concentrate at presumably co-purified peroxisome-ER membrane contacts. Intriguingly, the fifth candidate, OCIA domain-containing protein 1, was previously described as decreasing mitochondrial network formation. In this work, we confirmed its peroxisomal localization and further observed a reduction in peroxisome numbers in response to OCIAD1 overexpression. Hence, OCIAD1 appears to be a novel protein, which has an impact on both mitochondrial and peroxisomal maintenance.

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Section: Discussionmentioning

confidence: 99%

Analysis of the Mouse Hepatic Peroxisome Proteome—Identification of Novel Protein Constituents Using a Semi-Quantitative SWATH-MS Approach

Singin,

Astapenka,

Costina

et al. 2024

Cells

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“…Indeed, there is a wide consensus that atherosclerosis and low-grade inflammation are, although often subclinical, conditions associated with cognitive decline in the elderly [ 28 , 29 , 30 , 31 , 32 ]. High Lp-PLA2 reflects in enhanced phospholipid hydrolysis, high contents of oxidized non-esterified fatty acids and PLs are produced, which promote expression of adhesion molecules, stimulate cytokine production (TNF-α, IL-6), and attract macrophages to the arterial intima [ 33 , 34 , 35 ]. This exacerbates endothelial dysfunction and accelerates the growth of the plaque and, eventually, the formation of a necrotic core [ 14 ].…”

Section: Discussionmentioning

confidence: 99%

Lipoprotein-Associated Phospholipase A2 Activity as Potential Biomarker of Vascular Dementia

et al. 2023

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A wealth of evidence suggests that Lipoprotein-associated phospholipase A2 (Lp-PLA2) plays a relevant role in atherogenesis and inflammation, which in turn are associated with the risk of developing dementia. The aim of this study was to evaluate whether serum Lp-PLA2 activity might be an early and/or late biomarker for different forms of dementia. Serum Lp-PLA2 activity was assessed in older patients with mild cognitive impairment (MCI, n = 166; median clinical follow-up = 29 months), Late-Onset Alzheimer’s disease (LOAD, n = 176), vascular dementia (VAD, n = 43), dementia characterized by an overlap between LOAD and VAD (AD-VAD MIXED dementia) (n = 136), other dementia subtypes (n = 45), and cognitively normal controls (n = 151). We found a significant trend towards higher levels of Lp-PLA2 activity in VAD compared with the other groups (ANOVA, p = 0.028). Similarly, Lp-PLA2 activity was greater in MCI converting to VAD compared with those that did not or did convert to the other types of dementia (ANOVA, p = 0.011). After adjusting for potential confounders, high levels of Lp-PLA2 activity were associated with the diagnosis of VAD (O.R. = 2.38, 95% C.I. = 1.06–5.10), but not with other types of dementia. Our data suggest that increased serum Lp-PLA2 activity may represent a potential biomarker for the diagnosis of VAD.

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Signal transduction mechanisms of phospholipases and their roles in cancer signaling and progression

Finnerty,

Cummings

2023

Phospholipases in Physiology and Pathology

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Platelet activating-factor acetylhydrolase II: A member of phospholipase A2 family that hydrolyzes oxidized phospholipids

Cited by 8 publications

References 82 publications

Analysis of the Mouse Hepatic Peroxisome Proteome—Identification of Novel Protein Constituents Using a Semi-Quantitative SWATH-MS Approach

Analysis of the Mouse Hepatic Peroxisome Proteome—Identification of Novel Protein Constituents Using a Semi-Quantitative SWATH-MS Approach

Lipoprotein-Associated Phospholipase A2 Activity as Potential Biomarker of Vascular Dementia

Signal transduction mechanisms of phospholipases and their roles in cancer signaling and progression

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