Ask about this productRelated genes to: Apbb1 antibody
- Gene:
- APBB1 NIH gene
- Name:
- amyloid beta precursor protein binding family B member 1
- Previous symbol:
- RIR
- Synonyms:
- Fe65
- Chromosome:
- 11p15.4
- Locus Type:
- gene with protein product
- Date approved:
- 1997-03-27
- Date modifiied:
- 2016-10-04
Related products to: Apbb1 antibody
Related articles to: Apbb1 antibody
- Pathogenic variants in the amyloid precursor protein gene (APP) have been linked to Alzheimer's disease and intracerebral haemorrhage resulting from cerebral amyloid angiopathy. In these disorders, variants are generally located within or surrounding the amyloid-beta domain of APP and mostly increase the production or aggregation properties of the toxic amyloid-beta peptide. Here, we report a novel APP p.V742L variant in the APP intracellular domain (AICD) in a patient with a clinical and neuroradiological ischemic small vessel disease phenotype and a positive family history. We investigate the functional consequences of the variant on AICD function. We obtained patient fibroblasts through a skin biopsy and applied immunocytochemistry to examine the subcellular localization of APP. Subsequently, 3' mRNA sequencing was deployed to investigate changes in gene expression. Finally, the effect of the variant on the binding of FE65 to AICD was investigated using co-immunoprecipitation followed by western blot. Localization of APP p.V742L to lysosomes was increased, without affecting lysosomal motility. Transcriptome analysis showed altered expression of AICD target genes as well as dysregulation of genes relevant to the ischemic stroke phenotype. Finally, APP p.V742L was associated with an increased interaction with FE65, its most important intracellular binding partner. Taken together, our data demonstrate that the APP p.V742L variant enhances the interaction of the AICD with FE65, resulting in dysregulation of gene transcription. This study illustrates the diverse roles of APP in brain disorders, and suggests ischemic small vessel disease as a novel APP-associated phenotype. - Source: PubMed
Publication date: 2026/01/25
Voesenek Bas J BRutten Julie WMulder Monique P CMei HailiangNibbeling Esther A Rvan Etten Ellis Svan Roon-Mom Willeke M CLesnik Oberstein Saskia A JDaoutsali ElenaBuijsen Ronald A M - Understanding of the impacts of seminal plasma and sperm proteins on both animal and human fertility has expanded rapidly in the last decade. However, little is known about the reproductive proteomes of endangered species. In this study, we characterized for the first time the seminal plasma and sperm proteomes of the critically endangered Red Wolf and evaluated differences in proteomic signatures between ejaculates which experienced "High" versus "Baseline" (i.e. population average) sperm cryo-resilience. Highly cryo-resilient ejaculates (High_CR, n = 5) maintained > 50% sperm total motility relative to fresh samples following cryopreservation and post-thaw incubation, as well as acrosome integrity post-thaw. These samples had significantly higher expression of A1BG, APBB1, KRT1, KRT10, LOC609402 and LOC100685620 (AGP) proteins in seminal plasma, and significantly reduced expression of RHOA, NUP62, SMYD4, ARHGD1B, CAPG, CSTB, and CFL1 proteins in sperm compared with Baseline cryo-resilient samples (Base_CR, n = 5). Differences in protein expression indicated that alterations in physiological pathways including blood clotting cascades (seminal plasma) and both actin dynamics and immune pathways (sperm) are associated with sperm cryo-resilience. This new knowledge may prove useful in future optimization of semen cryopreservation and assisted reproductive technologies for the critically endangered Red Wolf. - Source: PubMed
Publication date: 2025/10/29
Celedon Jasmin JCorder Molly LMcConnell MeghannSongsasen NucharinNagashima Jennifer B - Spermatogonial stem cells (SSCs) are essential for initiating and maintaining normal spermatogenesis, and notably, they have important applications in both reproduction and regenerative medicine. Nevertheless, the molecular mechanisms controlling the fate determinations of human SSCs remain elusive. In this study, we identified a selective expression of APBB1 in dormant human SSCs. We demonstrated for the first time that APBB1 interacted with KAT5, which led to the suppression of GDF15 expression and consequent inhibition of human SSC proliferation. Intriguingly, Apbb1 mice assumed the disrupted spermatogenesis and markedly reduced fertility. SSC transplantation assays revealed that Apbb1 silencing enhanced SSC colonization and impeded their differentiation, which resulted in the impaired spermatogenesis. Notably, 4 deleterious mutation sites were identified in 2,047 patients with non-obstructive azoospermia (NOA), and patients with the c.1940C>G mutation had a similar testicular phenotype with Apbb1 mice. Additionally, we observed lower expression levels of APBB1 in NOA patients with spermatogenic arrest than in obstructive azoospermia patients with normal spermatogenesis. Collectively, our findings highlight an essential role of APBB1/KAT5/GDF15 in governing human SSC fate decisions and maintaining normal spermatogenesis and underscore them as therapeutic targets for treating male infertility. - Source: PubMed
Publication date: 2025/03/27
Zhou DaiLiu BangLiu LvjunLiu GuangminZhu FangHuang ZenghuiZhang ShushengHe ZupingFan Liqing - Precise diagnostic biomarkers of anticitrullination protein antibody (ACPA)-negative and early-stage RA are still to be improved. We aimed to screen autoantibodies in ACPA-negative patients and evaluated their diagnostic performance. The human genome-wide protein arrays (HuProt arrays) were used to define specific autoantibodies from the sera of 182 RA patients and 261 disease and healthy controls. Statistical analysis was performed with SPSS 17.0. In Phase I study, 51 out of 19,275 recombinant proteins covering the whole human genome were selected. In Phase II validation study, anti-ANAPC15 (anaphase promoting complex subunit 15) exhibited 41.8% sensitivity and 91.5% specificity among total RA patients. There were five autoantibodies increased in ACPA-negative RA, including anti-ANAPC15, anti-LSP1, anti-APBB1, anti-parathymosin, and anti-UBL7. Anti-parathymosin showed the highest prevalence of 46.2% ( = 0.016) in ACPA-negative early stage (<2 years) RA. To further improve the diagnostic efficacy, a prediction model was constructed with 44 autoantibodies. With increased threshold for RA calling, the specificity of the model is 90.8%, while the sensitivity is 66.1% (87.8% in ACPA-positive RA and 23.8% in ACPA-negative RA) in independent testing patients. Therefore, HuProt arrays identified RA-associated autoantibodies that might become possible diagnostic markers, especially in early stage ACPA-negative RA. - Source: PubMed
Publication date: 2024/08/11
Liu XuZhang XiaoyingKang Yu-JianHuang FeiLiu ShuangGuo YixueLi YingniYin ChangchengLiu MinglingHan QimaoWang QingwenYe HuaYao HaihongLi ChunLi JiahePingcuo WangzhaZhang YanSu YinGao GeLi ZhanguoSun Xiaolin - Anaplastic lymphoma kinase (ALK) is a well-known oncogene involved in various malignancies such as anaplastic large cell lymphoma, lung cancer and neuroblastoma. Several substrates for fused ALK have been identified and their biological functions have been described. However, the lack of a comprehensive identification of ALK substrates limits our understanding of the biological roles of receptor ALK. Thus, this study aimed to identify novel ALK substrates and characterize their biological functions. We screened the interactors of the kinase domain of receptor ALK using proximity-dependent biotin identification and identified 43 interactors. We narrowed down the candidates by evaluating whether these interactors were downstream of ALK in a neuroblastoma cell line, NB-1. Amongst these, we identified amyloid beta precursor protein-binding family B member 1 (APBB1) as an ALK downstream molecule involved in NB-1 cell viability. Finally, we assessed the kinase-substrate relationship between ALK and APBB1 and found that ALK phosphorylated multiple tyrosine residues in APBB1 both in-cell and in-tube assays, with tyrosine 269 as a major target. In conclusion, we successfully identified a new substrate for receptor ALK. Our results may help further elucidate the molecular mechanism of ALK downstream signalling in neuroblastoma. - Source: PubMed
Suzuki YujiTsubota ShomaKadomatsu KenjiSakamoto Kazuma