Ask about this productRelated genes to: HRSP12 antibody
- Gene:
- RIDA NIH gene
- Name:
- reactive intermediate imine deaminase A homolog
- Previous symbol:
- HRSP12
- Synonyms:
- UK114, P14.5, PSP
- Chromosome:
- 8q22.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-06-03
- Date modifiied:
- 2016-10-05
Related products to: HRSP12 antibody
Related articles to: HRSP12 antibody
- Among senescence-accelerated prone mice (SAMP), the SAMP8 and SAMP10 strains exhibit significant age-related deteriorations in learning and memory. Previous studies have reported that SAMP strains carry high level of Akv-type endogenous ecotropic murine leukemia virus (E-MuLV), whereas the senescence-accelerated resistant strain SAMR1 contains very low or undetectable levels of the virus. Retroviral infections, including MuLV, have been implicated in the acceleration of prion pathogenesis. Prion diseases are characterized by neuronal loss, spongiform degeneration, and astrogliosis and are caused by the infectious prion protein (PrP), which arises from the misfolding of the normal cellular prion protein (PrP). Notably SAMP8 mice infected with scrapie exhibit shortened survival and increased PrP accumulation compared with SAMR1 mice. In this study, we investigated the role of endogenous E-MuLV to prion disease progression using senescence-accelerated mouse models. Following infection with the 22L scrapie strain, SAMP10 mice displayed significantly shortened survival compared with SAMR1 mice after both intracerebral (IC: 121.8±1.3 vs. 141.0±2.2 days) and intraperitoneal (IP: 184.4±1.3 vs. 216.2±2.7 days) inoculation. SAMP10 mice also showed earlier and more pronounced PrP accumulation during the clinical phase, along with enhanced vacuolation. Furthermore, in a cerebellar slice culture model of 22L scrapie infection, treatment with the antiretroviral drug zidovudine significantly reduced PrP accumulation in SAMP10 mice. Taken together, these findings suggest that endogenous E-MuLV contribute to the accelerated prion pathogenesis by promoting early and elevated PrP accumulation, leading to shortened survival. - Source: PubMed
Publication date: 2026/04/29
Choi Min-WooMostafa Mohd NajibKim Mo-JongJang ByungkiChoi Myung-JuKim Jae-IlKim Yong-SunChoi Eun-Kyoung - Inadequate dietary intake among pregnant women is a major public health challenge in Ethiopia. Although nutrition interventions exist, they often overlook dietary diversity and face sustainability issues. This study evaluated a community-based intervention designed to improve dietary diversity for pregnant women in Southern Ethiopia by leveraging the women's development army (WDA) platform. - Source: PubMed
Publication date: 2026/03/04
Tariku YihunFekadu AbelBaye Kaleab - Neurodegenerative diseases (NDs), such as Alzheimer's, Parkinson's, and prion diseases, are characterized by the dynamical spread of toxic proteins through the brain. In prion diseases, cellular prion protein ( ), produced by neurons, misfolds into a toxic form, known as scrapie prion protein ( ). induces neuronal stress which ultimately leads to cell death. In this paper, we develop mathematical models for the progression of prion diseases, incorporating a cellular defense mechanism that introduces a delay term affecting protein translation and a volatility term accounting for unaccounted biological factors influencing the system. We also extend the model to capture the spatial spread of toxic proteins over the brain connectome. Our first objective is to establish the existence and uniqueness of a global positive solution to the prion disease models. Afterwards, we analyze the asymptotic behavior of the models by identifying regimes of persistence and extinction of toxic proteins. For the deterministic delayed systems, we perform a stability analysis for the persistence and demonstrate that the system undergoes a Hopf bifurcation. We also study the intensity of fluctuations of the equilibrium state of the stochastic model. Additionally, we present numerical simulations to illustrate the model dynamics using biologically relevant parameters. - Source: PubMed
Publication date: 2026/04/23
Boregowda GangadharaSharif OmarGutierrez Iii DanielSimmons AllegraPujo-Menjouet LaurentOraby TamerLindstrom Michael R - Recent studies have shown that significant expression of PrP protein is also present in skeletal muscle, and it plays a significant role in maintaining skeletal muscle homeostasis. Although the expression of PrP in skeletal muscle has been clarified, the effects of PrP-mediated prion protein infection on sarcopenia in mice and its potential regulatory mechanisms remain unclear. This study investigated the role of PrP in Prion-induced sarcopenia, using an animal model of prion disease based on intraperitoneal injection of the scrapie strain ME7 into wild-type mice and Prnp knockout mice. The results indicate that prion infection-induced sarcopenia exhibits muscle fiber type specificity, and that the lack of PrP can prevent prion protein infection-induced sarcopenia, although the lack of PrP may lead to reduced mitochondrial-endoplasmic reticulum homeostasis. These data provide novel evidence that prion infection affects skeletal muscle system health through myofiber-specific mechanisms. - Source: PubMed
Liu WenduoKim Yong-ChanWon Sae-YoungKieu Thi Thu TrangKook Sung HoJeong Byung-HoonKim Sang Hyun - Real-time quaking-induced conversion (RT-QuIC) is highly sensitive for prion detection; however, inhibitory factors present in tissue homogenates readily interfere with the assay. We previously reported that recombinant cervid prion protein (rCerPrP) enabled the establishment of practical RT-QuIC for detecting chronic wasting disease and atypical bovine spongiform encephalopathy (BSE) prions, i.e., detecting low levels of prions in high concentration of brain tissue homogenates. Accordingly, the present study aimed to establish RT-QuIC for detecting classical BSE (C-BSE) and classical and atypical scrapie (C- and A-scrapie, respectively). A single-step lipid extraction using a 3:1 mixture of 2-butanol and methanol was effective as a pretreatment to remove inhibitors from brain homogenates. Among three rPrPs extensively evaluated, recombinant sheep PrP (rShPrP) was the most suitable substrate for practical detection of C-BSE prions. rCerPrP-173S/177N and rCerPrP-98S/173S/177N, which carry sheep-type amino acid substations at codons 173 and 177 and at codons 98, 173, and 177, showed excellent performance for detecting C-scrapie prions. Moreover, rCerPrP-98S/173S/177N, but not rCerPrP-173S/177N, was identified as an optimal substrate for detecting A-scrapie prions. These results suggested that combining inhibitor-removal pretreatment with the optimization of rPrP substrate for each animal prions further enhanced of RT-QuIC performance. - Source: PubMed
Publication date: 2026/03/20
Suzuki AkioSawada KazuheiNakashima TakuSato ToyotakaMiyazawa KohtaroMatsuura YuichiIkeda KeigoIwamaru YoshifumiHoriuchi Motohiro