Ask about this productRelated genes to: PRPSAP1 antibody
- Gene:
- PRPSAP1 NIH gene
- Name:
- phosphoribosyl pyrophosphate synthetase associated protein 1
- Previous symbol:
- -
- Synonyms:
- PAP39
- Chromosome:
- 17q25.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-01
- Date modifiied:
- 2016-10-05
Related products to: PRPSAP1 antibody
Related articles to: PRPSAP1 antibody
- OBJECTIVE: Sepsis remains a leading cause of mortality worldwide, with cardiac dysfunction contributing substantially to sepsis-related deaths. Due to the unique biology of myocardial tissue, the mechanisms underlying sepsis-induced cardiac injury are incompletely understood. This exploratory study aimed to apply integrated proteomic and metabolomic profiling to characterize molecular alterations in cardiac tissue from a cecal ligation and puncture mouse model of sepsis. RESULTS: Comparative analysis identified 118 significantly altered proteins (75 upregulated and 43 downregulated) and 190 significantly altered metabolites (174 upregulated and 16 downregulated). Integrated pathway and network analyses implicated biological processes including platelet activation, mineral absorption, drug metabolism, terpenoid backbone biosynthesis, and butanoate metabolism. Notably, several previously under-recognized proteins (Prpsap1, Qsox1 and Prph), were identified as differentially expressed and ranked highly in our integrated network analyses, while prostaglandin H2, prostaglandin I2, thromboxane A2 and L-glutamine emerged as central metabolic nodes. These data extend the molecular landscape of septic cardiomyopathy and nominate prioritized candidates for orthogonal validation and mechanistic study. - Source: PubMed
Publication date: 2026/01/21
Ji HeyuXiao TingLi PeijunXu JunmeiCui Yulong - Chromatin formation requires both an adequate nucleotide supply and histone availability. Newly synthesized histones are escorted by histone chaperones that mediate their orderly transfer from ribosomes to DNA. While nucleotide and histone synthesis are the two major biosynthetic processes required for chromatin assembly, how these processes are coordinated remains unknown. Phosphoribosyl pyrophosphate synthetases (PRPSs), which catalyze the first and rate-limiting step in nucleotide biosynthesis, form a complex with PRPS-associated proteins (PRPSAPs). Using a rapid degron system in multiple human cell lines, we show that PRPS enzymes, together with PRPSAPs, play a key role in early histone maturation independent of their nucleotide biosynthetic function. Depletion of either PRPS1 or PRPSAP1 limits histone availability and disrupts chromatin assembly. These findings reveal a previously unrecognized synchrony between nucleotide metabolism and chromatin regulation, providing insight into how nucleotide production and histone deposition are coordinated. - Source: PubMed
Publication date: 2025/12/03
Srivastava ShashankSamaniego-Castruita DanielaSrivastava ShubhiKhurana SakshiRehman JaleesShukla VipulBen-Sahra IssamFoltz Daniel R - The phosphoribosyl pyrophosphate synthetase (PRPS) enzyme conducts a chokepoint reaction connecting central carbon metabolism and nucleotide production pathways, making it essential for life. Here, we show that the presence of multiple PRPS-encoding genes is a hallmark trait of eukaryotes, and we trace the evolutionary origins and define the individual functions of each of the five mammalian PRPS homologs - three isozymes (one testis-restricted) and two non-enzymatic associated proteins (APs) - which we demonstrate operate together as a large molecular weight complex capable of attaining a heterogeneous array of functional multimeric configurations. Employing a repertoire of isogenic fibroblast clones in all viable individual or combinatorial assembly states, we define preferential interactions between subunits, and we show that cells lacking PRPS2, PRPSAP1, and PRPSAP2 render PRPS1 into aberrant homo-oligomeric assemblies with diminished metabolic flux and impaired proliferative capacity. We demonstrate how numerous evolutionary innovations in the duplicated genes have created specialized roles for individual complex members and identify translational control mechanisms that enable fine-tuned regulation of PRPS assembly and activity, which provide clues into the positive and negative selective pressures that facilitate metabolic flexibility and tissue specialization in advanced lifeforms. Collectively, our study demonstrates how evolution has transformed a single PRPS gene into a multimeric complex endowed with functional and regulatory features that govern cellular biochemistry. - Source: PubMed
Publication date: 2024/10/01
Karki Bibek RMacmillan Austin CVicente-Muñoz SaraGreis Kenneth DRomick Lindsey ECunningham J Tom - There is a pressing need for non-invasive preoperative prediction of microvascular invasion (MVI) in hepatocellular carcinoma (HCC). This study investigates the potential of exosome-derived mRNA in plasma as a biomarker for diagnosing MVI. - Source: PubMed
Publication date: 2024/07/07
Xin ZhaodanChen HaoXu JingtongZhang HailiPeng YufuRen JingGuo QinSong JiajiaJiao LinYou LitingBai LingWei YonggangZhou JuanYing Binwu - Molecular investigations have led to increased therapeutic options for prostatic adenocarcinoma. A single case report of a :: gene fusion occurring in prostate cancer was previously reported. A review of the literature revealed that gene rearrangements are exceedingly rare molecular events in prostate cancer. gene fusions can be oncogenic drivers or develop as resistance mechanisms. The tumor-agnostic approvals of TRK inhibitors by the FDA provide additional rationale for molecular investigations of aggressive prostatic adenocarcinomas. This may prove to be an additional therapeutic option for patients with aggressive prostatic carcinomas refractory to initial therapy. We report a case of an aggressive castrate-resistant prostatic adenocarcinoma with a :: gene fusion. - Source: PubMed
Publication date: 2024/05/21
Whaley Rumeal DTekin BurakMcCarthy Michael RZia Hamid MPitel Beth AAl-Kateb HussamCheville John CGupta Sounak