Ask about this productRelated genes to: GDE1 antibody
- Gene:
- GDE1 NIH gene
- Name:
- glycerophosphodiester phosphodiesterase 1
- Previous symbol:
- -
- Synonyms:
- MIR16
- Chromosome:
- 16p12.3
- Locus Type:
- gene with protein product
- Date approved:
- 2008-01-25
- Date modifiied:
- 2016-10-05
Related products to: GDE1 antibody
Related articles to: GDE1 antibody
- Beef flavor is a trait difficult to evaluate since different senses (taste, touch, and smell) are involved in its perception. In the last 20 years, 102 Quantitative Trait Loci (QTLs), associated with the variability of different beef flavor notes, have been reported. These QTLs are spread on all chromosomes, including BTA X. In these QTL regions, 2509 genes are located and, among them, 594 are involved in the metabolic processes of lipids, proteins, and carbohydrates, the main meat components for the production of volatile substances responsible for flavor. Only 19 of these genes (, , , , , , , , , , , , , , , , , , and ) are also present in the QTL regions affecting pork flavor. The applied approach allowed us to strongly restrict the number of candidate genes to affect the variability of both beef and pork flavor. - Source: PubMed
Publication date: 2026/03/25
Rando AndreaGrassi GiuliaPerna Anna MariaDi Gregorio Paola - BACKGROUND: Post-traumatic headache (PTH) is a debilitating neurological sequela of mild traumatic brain injury (mTBI) characterized by secondary cephalic pain. The endocannabinoid system (ECS) is a critical modulator of nociception, yet the specific spatiotemporal changes in its metabolic machinery within cephalic pain circuits following mTBI are poorly understood. METHODS: Using in-situ hybridization (ISH), we first characterized the levels of gene expression of major endocannabinoid (eCB) synthesizing enzymes (Napepld, Gde1, Dagla, Daglb), hydrolyzing enzymes (Faah, Mgll) and cannabinoid receptors (Cnr1 and Cnr2) in the trigeminal complex (trigeminal ganglion - TG, trigeminal root entry zone - TREZ, and trigeminal nucleus caudalis - TNC) and midbrain (periaqueductal gray - PAG, dorsal raphe - DR) regions involved in the modulation of pain. Subsequently, employing a mouse model of repetitive closed head mTBI that induces cephalic pain, we assessed global eCB enzymatic gene expression changes via qPCR and region-specific changes via ISH at one-week post-injury. RESULTS: Baseline characterization revealed complex co-expression patterns, with Gde1 and Daglb transcripts being significantly more abundant than Napepld and Dagla in the TG, TNC, and PAG. Seven days post-mTBI, coinciding with the onset of PTH-like symptoms, we identified a significant upregulation of the hydrolyzing enzymes Faah in the peripheral TREZ but not in the TG sensory neurons. Centrally, although no difference was observed in the TNC, mTBI induced an upregulation of Mgll in the ventrolateral PAG (vlPAG) and the DR, particularly within DR VGlut3+ neurons. CONCLUSION: These findings demonstrate a novel neuropathological mechanism whereby mTBI triggers a persistent, region-specific upregulation of genes encoding eCB-degrading enzymes. Thus, sub-acute modulation of eCB hydrolyzing enzymes in critical peripheral and central pain-modulating regions may contribute to the maintenance of cephalic pain associated with mTBI. CLINICAL TRIAL NUMBER: Not applicable. - Source: PubMed
Publication date: 2026/04/11
Nagarajan GurueswarZhang Yumin - Genistein, a bioactive isoflavone with therapeutic potential in treating oxidative stress, cardiovascular diseases, and cancer, faces production limitations during microbial biosynthesis due to product feedback inhibition of isoflavone synthase (IFS). To overcome this bottleneck, a biosensor-assisted continuous directed evolution platform was developed. Specifically, a genistein-specific biosensor was engineered using the Bradyrhizobium japonicum transcription factor FrrA, capable of distinguishing genistein from its precursor, (2S)-naringenin. The biosensor was systematically optimized to eliminate background fluorescence at inhibitory genistein concentrations while maintaining strong responses to elevated product levels, enabling precise detection during high-throughput screening. By coupling this biosensor with droplet microfluidic sorting, a high-quality mutant library of Trifolium pratense IFS (TpIFS) generated through deaminase-T7 RNA polymerase fusion-mediated continuous evolution, was screened. This approach successfully identified TpIFS, a feedback-resistant mutant exhibiting a 6.6-fold increase in the product inhibition constant and a 3.8-fold reduced binding affinity for genistein. Consequently, the genistein yield obtained with TpIFS was 3.1 times that of the wild-type. Molecular dynamics simulations revealed that mutations I187R and F303A prevented inhibitor-induced conformational displacement of the catalytic I-helix. This work establishes a generalizable high-throughput screening strategy to mitigate enzyme feedback inhibition, facilitating the robust biosynthesis of plant-derived natural products. - Source: PubMed
Publication date: 2026/03/01
Wang ZheZhao DanshanBaghdady Ghada SaidWang JiyuanDai YiqiangXu WeiminWang DaoyingWang YuetongXia Xiudong - Glycerophosphocholine (GPC) and glycerophosphoinositol (GPI) are phospholipid metabolites generated by phospholipase-mediated deacylation. In budding yeast, they enter cells via the Git1 permease; in fission yeast, the homolog is Tgp1. This study investigates why GPC is toxic to mutants, where Tgp1 is upregulated due to loss of Asp1 pyrophosphatase, resulting in elevated inositol pyrophosphate 1,5-IP. We show that Tgp1 specifically transports GPC, explaining why GPC, but not GPI, impairs growth. Increased GPC uptake slows doubling time but does not reduce viability. Toxicity is relieved by deletion of Gde1, a phosphodiesterase that hydrolyzes GPC to choline and glycerol-3-phosphate. Mutations in either the Gde1 active site or SPX domain also suppress toxicity, and radiolabeling confirms both domains are required for enzymatic activity. GPC is toxic in cells vastly overexpressing Tgp1 even without elevated IP, but Gde1 loss does not suppress this effect. Similarly, in overexpressing the Git3 transporter, GPC provision causes toxicity independent of Gde1. Loss of Gpc1, the acyltransferase converting GPC to lysophosphatidylcholine, does not alter toxicity in either yeast. These findings highlight a conserved process by which GPC regulates growth and reveal a role for IP in modulating this process. - Source: PubMed
Publication date: 2026/02/16
Hrach Victoria LeeSchwer BeateVitek LaneBorowicz MichaelInnokentev AlekseiSanchez Ana MSinger Justin RShuman StewartPatton-Vogt Jana - Colorectal cancer (CRC) is a highly lethal gastrointestinal malignancy with substantial global health implications. Although mitochondrial metabolism genes play a crucial role in CRC development, their prognostic significance remains unclear. - Source: PubMed
Publication date: 2025/07/08
Wang HouZhang KaiNing Guang