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Platelet-activating factor acetylhydrolase 1b, catalytic subunit 2

Platelet-activating factor acetylhydrolase (PAFAH) inactivates platelet-activating factor (PAF) into acetate and LYSO-PAF. This gene encodes the beta subunit of PAFAH, the other subunits are alpha and gamma. Multiple alternatively spliced transcript variants that encode different protein isoforms have been described for this gene. [providedby RefSeq, May 2010] (from NCBI)
Top mentioned proteins: PAFAH1B3, PAF, CAN, 1-Alkyl-2-acetylglycerophosphocholine Esterase, ACID
Papers on Pafah1b2
Multiple Susceptibility Loci at Chromosome 11q23.3 are Associated with Plasma Triglyceride in East Asians.
Sung et al., Seoul, South Korea. In J Lipid Res, Jan 2016
ApoA5 [rs651821; rs2075291]; ZNF259 [rs964184; rs603446]; BUD13 [rs11216126]; Apoa4 [rs7396851]; SIK3 [rs12292858]; PCSK7 [rs199890178]; PAFAH1B2 [rs12420127] and SIDT2 [rs2269399].
Activity-Based Protein Profiling of Oncogene-Driven Changes in Metabolism Reveals Broad Dysregulation of PAFAH1B2 and 1B3 in Cancer.
Nomura et al., Berkeley, United States. In Acs Chem Biol, Aug 2015
Through this profiling effort, we found oncogenic regulatory mechanisms for several cancer-relevant serine hydrolases and discovered that platelet activating factor acetylhydrolase 1B2 and 1B3 (PAFAH1B2 and PAFAH1B3) activities were consistently upregulated by several oncogenes, alongside previously discovered cancer-relevant hydrolases fatty acid synthase and monoacylglycerol lipase.
Selective inhibitor of platelet-activating factor acetylhydrolases 1b2 and 1b3 that impairs cancer cell survival.
Cravatt et al., Berkeley, United States. In Acs Chem Biol, May 2015
Here, we report a class of tetrahydropyridine reversible inhibitors of PAFAH1b2/3 discovered using a fluorescence polarization-activity-based protein profiling (fluopol-ABPP) screen of the NIH 300,000+ compound library.
A recurrent 11q aberration pattern characterizes a subset of MYC-negative high-grade B-cell lymphomas resembling Burkitt lymphoma.
Berlin-Frankfurt-Münster Non-Hodgkin Lymphoma Group et al., Kiel, Germany. In Blood, 2014
The minimal region of gain was defined by high-level amplifications in 11q23.3 and associated with overexpression of genes including PAFAH1B2 on a transcriptional and protein level.
Association of low-frequency and rare coding-sequence variants with blood lipids and coronary heart disease in 56,000 whites and blacks.
Cupples et al., Boston, United States. In Am J Hum Genet, 2014
Although we did not identify new genes associated with LDL-C, we did identify four low-frequency (frequencies between 0.1% and 2%) variants (ANGPTL8 rs145464906 [c.361C>T; p.Gln121*], PAFAH1B2 rs186808413 [c.482C>T; p.Ser161Leu], COL18A1 rs114139997 [c.331G>A; p.Gly111Arg], and PCSK7 rs142953140 [c.1511G>A; p.Arg504His]) with large effects on HDL-C and/or triglycerides.
Aspirin hydrolysis in plasma is a variable function of butyrylcholinesterase and platelet-activating factor acetylhydrolase 1b2 (PAFAH1b2).
McIntyre et al., Cleveland, United States. In J Biol Chem, 2013
Aspirin is rapidly hydrolyzed within erythrocytes by a heterodimer of PAFAH1b2/PAFAH1b3 but also in plasma by an unidentified activity.
Loss of PAFAH1B2 reduces amyloid-β generation by promoting the degradation of amyloid precursor protein C-terminal fragments.
Haass et al., München, Germany. In J Neurosci, 2013
After the γ-secretase complex components, the most potent effect was observed for platelet activating factor acetylhydrolase α (Paf-AHα), and, in mammalian cells, the effect was replicated for its ortholog PAFAH1B2.
Developmental dynamics of PAFAH1B subunits during mouse brain development.
Echevarria et al., San Juan de Alicante, Spain. In J Comp Neurol, 2013
The intracellular enzyme that deacetylates the PAF (PAFAH1B) is composed of a tetramer of two catalytic subunits, ALPHA1 (PAFAH1B3) and ALPHA2 (PAFAH1B2), and a regulatory dimer of LIS1 (PAFAH1B1).
Oncogenic activation of FOXR1 by 11q23 intrachromosomal deletion-fusions in neuroblastoma.
Molenaar et al., Amsterdam, Netherlands. In Oncogene, 2012
Genes at the proximal side of the deletion were fused to FOXR1, resulting in fusion transcripts of MLL-FOXR1 and PAFAH1B2-FOXR1.
Plasma platelet-activating factor-acetyl hydrolase activity and the levels of free forms of biomarker of lipid peroxidation in cerebrospinal fluid of patients with aneurysmal subarachnoid hemorrhage.
Yoshida et al., Sagamihara, Japan. In Neurosurgery, 2012
Plasma PAF-AH can hydrolyze oxidized phospholipids, and may attenuate the spreading of lipid peroxidation and participate in defense mechanisms against vasospasm after aneurysmal subarachnoid hemorrhage.
Identification of thalidomide-specific transcriptomics and proteomics signatures during differentiation of human embryonic stem cells.
Sachinidis et al., Köln, Germany. In Plos One, 2011
Proteome analysis showed loss of POU5F1 regulatory proteins PKM2 and RBM14 and an over expression of proteins involved in neuronal development (such as PAK2, PAFAH1B2 and PAFAH1B3) after 14 days of differentiation.
Intracellular erythrocyte platelet-activating factor acetylhydrolase I inactivates aspirin in blood.
McIntyre et al., Cleveland, United States. In J Biol Chem, 2011
intracellular type I PAF acetylhydrolase (PAFAH1B2 and PAFAH1B3) is the major aspirin hydrolase of human blood
Opposing effects of Ndel1 and alpha1 or alpha2 on cytoplasmic dynein through competitive binding to Lis1.
Zhu et al., Shanghai, China. In J Cell Sci, 2009
These results indicate an antagonistic effect of alpha1, alpha2 and Ndel1 for Lis1 binding, probably to modulate dynein functions in vivo.
Differential interaction of the Pafah1b alpha subunits with the Reelin transducer Dab1.
D'Arcangelo et al., Houston, United States. In Brain Res, 2009
study examined biochemical interactions of Pafah1b Alpha1 & Alpha2 subunits with the Reelin signaling machinery & demonstrated that Alpha2, but not Alpha1, binds Dab1 in a phosphorylation-independent manner
Novel isoforms of intracellular platelet activating factor acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs.
Bovill et al., Burlington, United States. In Prostaglandins Other Lipid Mediat, 2008
splice variants of the Pafah1b2 gene transcript retain exons 1-5 and replace exon 6 with alternative exons derived from genomic sequence 3' to exon 6. Splice variants encode two proteins with different novel carboxy termini
Exclusion of the alpha2 subunit of platelet-activating factor acetylhydrolase 1b (PAFAH1B2) as a prothrombotic gene in a protein C-deficient kindred and population-based case-control sample.
Bovill et al., Salt Lake City, United States. In Thromb Haemost, 2007
PAFAH1B2 is not the gene responsible for the linkage evidence on chromosome 11q23 in protein C deficiency.
Lissencephaly associated mutations suggest a requirement for the PAFAH1B heterotrimeric complex in brain development.
Eichele et al., Hannover, Germany. In Mech Dev, 2000
Lis1 is a subunit of a brain platelet-activating factor acetylhydrolase (PAFAH1B) where it forms a heterotrimeric complex with two hydrolase subunits, referred to as 29 kDa (PAFAH1B3) and 30 kDa (PAFAH1B2).
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