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Platelet-activating factor acetylhydrolase 1b, catalytic subunit 3

PAFAH1B3
This gene encodes an acetylhydrolase that catalyzes the removal of an acetyl group from the glycerol backbone of platelet-activating factor. The encoded enzyme is a subunit of the platelet-activating factor acetylhydrolase isoform 1B complex, which consists of the catalytic beta and gamma subunits and the regulatory alpha subunit. This complex functions in brain development. A translocation between this gene on chromosome 19 and the CDC-like kinase 2 gene on chromosome 1 has been observed, and was associated with mental retardation, ataxia, and atrophy of the brain. Alternatively spliced transcript variants have been described. [provided by RefSeq, Mar 2009] (from NCBI)
Top mentioned proteins: Pafah1b2, 1-Alkyl-2-acetylglycerophosphocholine Esterase, PAF, CAN, Alpha-1
Papers on PAFAH1B3
Activity-Based Protein Profiling of Oncogene-Driven Changes in Metabolism Reveals Broad Dysregulation of PAFAH1B2 and 1B3 in Cancer.
New
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.
Molecular signatures of mood stabilisers highlight the role of the transcription factor REST/NRSF.
Quinn et al., Liverpool, United Kingdom. In J Affect Disord, 2014
RESULTS: Global Pattern Recognition (GPR) analysis identified a total of 9 genes (DRD3(⁎), FOS(†), JUN(⁎), GAD1(⁎†), NRG1(⁎), PAFAH1B3(⁎), PER3(⁎), RELN(⁎) and RGS4(⁎)) to be significantly regulated in response to cellular challenge with the mood stabilisers sodium valproate ((⁎)) and lithium ((†)).
Metabolic profiling reveals PAFAH1B3 as a critical driver of breast cancer pathogenicity.
Nomura et al., Berkeley, United States. In Chem Biol, 2014
In this study, we used metabolic mapping platforms to identify biochemical drivers of cellular transformation and malignant progression driven through RAS and the Hippo pathway in breast cancer and identified platelet-activating factor acetylhydrolase 1B3 (PAFAH1B3) as a key metabolic driver of breast cancer pathogenicity that is upregulated in primary human breast tumors and correlated with poor prognosis.
Global proteomic characterization of uterine histotroph recovered from beef heifers yielding good quality and degenerate day 7 embryos.
Crowe et al., Dublin, Ireland. In Domest Anim Endocrinol, 2014
Of interest, PAFAH1B3, detected only in histotroph from the group yielding viable embryos, belongs to the group of platelet-activating factors that are known to be important for the development of the pre-implantation embryo in other species.
Identification of FOXM1-induced epigenetic markers for head and neck squamous cell carcinomas.
Teh et al., London, United Kingdom. In Cancer, 2014
RESULTS: Here, we investigated 8 FOXM1-induced differentially methylated genes, SPCS1, FLNA, CHPF, GLT8D1, C6orf136, MGAT1, NDUFA10, and PAFAH1B3, using human head and neck tissue specimens donated by 2 geographically independent patient cohorts from Norway and the United Kingdom.
Whole genome sequencing of Ethiopian highlanders reveals conserved hypoxia tolerance genes.
Haddad et al., In Genome Biol, 2013
Three genes significantly impact survival rates in low oxygen: cic, an ortholog of human CIC, Hsl, an ortholog of human LIPE, and Paf-AHα, an ortholog of human PAFAH1B3.
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
Reduced Aβ production was not attributable to altered β-amyloid precursor protein (APP) ectodomain shedding but was a result of an enhanced degradation of APP C-terminal fragments (CTFs) in the absence of PAFAH1B2 but not its close homolog PAFAH1B3.
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).
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.
GeneRIF
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
Development of a platelet-activating factor antagonist for HIV-1 associated neurocognitive disorders.
GeneRIF
Gendelman et al., Omaha, United States. In J Neuroimmunol, 2009
These observations support the further development of PMS-601 as an adjunctive therapy for HIV-1 associated neurocognitive disorders.
Opposing effects of Ndel1 and alpha1 or alpha2 on cytoplasmic dynein through competitive binding to Lis1.
GeneRIF
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.
GeneRIF
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
Pafah1b2 mutations suppress the development of hydrocephalus in compound Pafah1b1; Reln and Pafah1b1; Dab1 mutant mice.
D'Arcangelo et al., Houston, United States. In Neurosci Lett, 2008
Lis1, the product of the Pafah1b1 gene associates with Alpha1 (the product of the Pafah1b3 gene) and Alpha2 (the product of the Pafah1b2 gene) to form the Pafah1b heterotrimeric complex.
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
Intracellular paf-ah (paf-ah-Ib) is composed of a regulatory subunit, Pafah1b1, and two highly conserved but non-identical catalytic subunits, Pafah1b2 and Pafah1b3.
The Pafah1b complex interacts with the reelin receptor VLDLR.
GeneRIF
D'Arcangelo et al., Houston, United States. In Plos One, 2006
Catalytic subunits of the Pafah1b complex, Pafah1b2 and Pafah1b3, specifically bind to the NPxYL sequence of VLDLR, but not to ApoER2.
Genome-wide expression analysis detects eight genes with robust alterations specific to bipolar I disorder: relevance to neuronal network perturbation.
Yoshikawa et al., Saitama, Japan. In Hum Mol Genet, 2006
Validation studies using quantitative RT-PCR on the two original diagnostic cohorts plus tissue from schizophrenic subjects, confirmed the differential expressions of eight genes (RAP1GA1, SST, HLA-DRA, KATNB1, PURA, NDUFV2, STAR and PAFAH1B3) in a bipolar-specific manner and one gene (CCL3) which was downregulated in both bipolar and schizophrenic brains.
Previously uncharacterized roles of platelet-activating factor acetylhydrolase 1b complex in mouse spermatogenesis.
GeneRIF
Clark et al., Houston, United States. In Proc Natl Acad Sci U S A, 2003
role in spermatogenesis
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