Ask about this productRelated genes to: LDHD antibody
- Gene:
- LDHD NIH gene
- Name:
- lactate dehydrogenase D
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 16q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-11-13
- Date modifiied:
- 2016-10-05
Related products to: LDHD antibody
Related articles to: LDHD antibody
- Behavioral and psychological symptoms of dementia (BPSD) are common, profoundly troubling to patients and caregivers, and difficult to treat, yet their molecular underpinnings remain poorly understood. Here, we generated a large brain proteomic dataset with nine BPSD domains assessed in life from 376 donors from three cohorts. Protein associations with BPSD were examined using complementary approaches - domain-specific BPSD, multi-domain BPSD, and latent factor modeling - and integrated via cross-cohort meta-analysis. Four proteins (NMT1, DCAKD, DNPH1, and HIBADH) were associated with anxiety in dementia and five proteins (ABL1, SAP18, PLXND1, CTRB2, and LDHD) with multi-domain BPSD or BPSD latent factors after adjusting for sex, age, and other covariates (FDR < 0.05). Additionally, eight protein co-expression networks were associated with BPSD across cohorts. Together, these results link BPSD to dysregulation of synaptic signaling, protein folding, and humoral immune response, providing a molecular framework for therapeutic discovery. - Source: PubMed
Publication date: 2026/04/24
Vattathil Selina MDuong Duc MGearing MarlaSeyfried Nicholas TWilson Robert SBennett David AWoltjer Randall LWingo Thomas SWingo Aliza P - To investigate metabolic reprogramming-especially pyruvate metabolism-in hepatocellular carcinoma (HCC) before and after immune checkpoint inhibitor (ICI) therapy, construct a metabolism-related prognostic model, and evaluate the therapeutic potential of targeting LDHA. - Source: PubMed
Publication date: 2026/04/13
Li XinTang LingCao JuLiu Yao - ConspectusWater appears simple, yet its anomalous behavior reveals an unexpected structural complexity. A growing body of evidence indicates that many of water's anomalies arise from fluctuations between low-density (LD) and high-density (HD) local structural motifs, a form of polymorphism that is well established in the supercooled regime and increasingly supported at ambient conditions. Yet, how these structural motifs manifest within hydration layers, where water interacts with nanoparticles, proteins, and charged interfaces, remains far less understood. This interfacial water governs colloidal stability, biomolecular function, and chemical reactivity, but its microscopic organization is difficult to probe directly with conventional bulk techniques.In this Account, we describe how luminescence nanothermometry provides a powerful and versatile approach to accessing density fluctuations in the hydration layer. By monitoring temperature-dependent optical and Brownian observables of luminescent probes, structural reorganizations of the surrounding hydration layer can be inferred with nanoscale sensitivity. Over the past several years, our group has shown that lanthanide-doped upconversion nanoparticles (UCNPs) and fluorescent proteins, such as enhanced green fluorescent protein (EGFP), act as local reporters of hydration-water density fluctuations.A central observation emerging from these studies is the existence of a crossover temperature, , at which hydration-water observables exhibit bilinear temperature dependencies. This correlates with the depletion of LD motifs in the hydration shell and typically falls within the 315-330 K range, close to the minimum of water's isothermal compressibility. Importantly, depends on the nature of the probe and its interaction with the surrounding water.By systematically varying nanoparticle size, pH, surface chemistry, and probe type, we show that previously contradictory trends in can be unified by a single parameter: the effective surface charge density of the probe. When is plotted against this quantity, data from UCNPs with different sizes and surface functionalizations, as well as from fluorescent proteins at different concentrations, collapse onto a master curve. This result demonstrates that interfacial electrostatics govern the stability of LD motifs in the hydration layer, providing a physically intuitive framework that links nanoscale charge distributions to local water structure.We further extend this framework by examining nuclear quantum effects through isotopic substitution. Using EGFP as a model biomolecular probe, we show that replacing HO with DO shifts upward by ≈10 K and enhances protein thermal stability, consistent with stronger hydrogen bonding and the displacement of thermodynamic anomalies in heavy water. In contrast, several inorganic and molecular probes fail to resolve a comparable isotopic shift, highlighting that the detectability of LD/HD fluctuations might be probe-dependent. Control experiments in HO confirm that hydrogen, rather than oxygen, dominates these quantum effects.Together, these results establish luminescent nanoprobes as sensitive reporters of hydration-water density fluctuations and reveal how interfacial charge, confinement, and quantum effects sculpt water structure at the nanoscale. Beyond resolving long-standing questions about water's anomalies, this approach opens new avenues for understanding protein stability, designing functional nanomaterials, and exploiting hydration-water density fluctuations in chemical and biological systems. - Source: PubMed
Publication date: 2026/03/13
Raposo Filho Ramon SGuo YongweiMaturi Fernando EBrites Carlos D SCarlos Luís D - Exercise performance and skeletal muscle homeostasis are influenced by myofiber type composition. Cysteine and glycine-rich protein 3 (CSRP3) is highly expressed in the oxidative fiber-rich mammalian soleus muscle. However, the mechanistic basis of CSRP3's involvement in skeletal muscle development and myofiber type specification remains unclear. Here, we used various exercise training (aerobic/anaerobic) bioinformatics datasets and experimental model systems involving live mice and cell lines to determine the role of CSRP3 in driving mitochondrial metabolic reconfiguration, skeletal muscle fiber type remodeling, and improved exercise endurance. CSRP3 promotes the formation of oxidative myofibers while suppressing glycolytic myofiber differentiation. It enhances mitochondrial biogenesis, oxidative phosphorylation capacity, and elevates mitochondrial membrane potential. Conversely, AAV-mediated CSRP3 knockdown perturbs mitochondrial energy metabolism, compromises exercise performance, and reduces the proportion of oxidative myofibers. Mechanistically, CSRP3 binds to D-lactate dehydrogenase (LDHD) via a specific 33-amino acid region, promoting D-lactate metabolism in skeletal muscle. This interaction regulates mitochondrial morphology, biogenesis, oxidative phosphorylation efficiency, and TCA cycle activity, ultimately driving skeletal muscle mitochondrial energy metabolic rewiring and skeletal muscle fiber type remodeling. - Source: PubMed
Publication date: 2026/03/09
Jiang XiuyingWang ZhaoluLi RuiLiu YihaoLiu BopingYang GongsheJin JianjunShi Xin'e - Lactic acid bacteria are widely exploited in biotechnology due to their fermentation capacity and metabolite production. In this study, 19 isolates were recovered from tree bark collected across Thailand, representing the genera (11 isolates), (2 isolates), (3 isolates), (2 isolates) and (1 isolate). All exhibited homofermentative metabolism, producing l-, dl- or d-lactic acid. Among them, strain STCC-11, isolated from the bark of in Satun Province, Thailand, demonstrated strong potential for d-lactic acid production, achieving 96.31% optical purity, 1.082 g l concentration and 0.451 g g glucose yield. This novel Gram-positive, spore-forming, facultatively anaerobic bacterium STCC-11 grew at 30-45 °C, pH 6.0-9.0 and up to 3% NaCl. Phylogenetic analysis of the 16S rRNA gene revealed 99.71% similarity with subsp. ATCC 700379. In addition, whole-genome analyses indicated that STCC-11 is distinct, with average nucleotide identity based on BLAST (ANIb) (94.12%), average nucleotide identity based on MUMmer (ANIm) (95.29%) and digital DNA-DNA hybridization (dDDH) (60.3%) values below species delineation thresholds. The genome (3.57 Mb, 43.8% G+C) encodes both and genes, and safety assessment confirmed the absence of pathogenicity or transferable resistance genes. Based on polyphasic taxonomic evidence, STCC-11 represents a novel species of the genus , for which the name S sp. nov. is proposed. The type strain is STCC-11 (LMG 33980 TISTR 10806). - Source: PubMed
Mahittikon JenjuireeThitiprasert SitananThongchul NutthaTanaka NaotoShiwa YuhChamroensaksri NitchaPhongsopitanun WongsakornTanasupawat Somboon