Ask about this productRelated genes to: BASP1 antibody
- Gene:
- BASP1 NIH gene
- Name:
- brain abundant membrane attached signal protein 1
- Previous symbol:
- -
- Synonyms:
- NAP-22, NAP22, CAP23, CAP-23
- Chromosome:
- 5p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1999-12-08
- Date modifiied:
- 2016-01-06
Related products to: BASP1 antibody
Related articles to: BASP1 antibody
- The persistent HIV reservoir constitutes the main obstacle to curing HIV/AIDS disease. Our understanding of how non-productive HIV infections are established in primary human CD4 T cells during the first round of infection remains, however, incomplete. In this study, we leveraged the HIV reporter virus pMorpheus-V5 to delineate cellular expression patterns that are upregulated in non-productively infected primary CD4 T memory stem cells (T). We found that CD4 T harboring non-productive proviruses displayed a distinct transcriptomic signature comprising 118 upregulated genes. This non-productive expression profile was distinct from that of productively infected cells as well as from negative-exposed and mock-infected cells. Among the cellular genes most upregulated in CD4 T cells harboring non-productive proviruses were CCR4-binding migratory chemokines (), tryptophan catabolic enzymes (), and genes encoding cytoskeletal rearrangement proteins (). Intracellular flow cytometry-based analyses confirmed that non-productively infected CD4 T cells were enriched for CCL22 and IDO1 co-expression compared to the other CD4 memory subsets, underscoring a clear CD4 T cell subset specificity for the upregulation of these two immune gene sets associated with non-productive infections. These findings suggest that primary human CD4 T harboring non-productive proviruses display a distinct immunoregulatory phenotype which may facilitate immune evasion and contribute to the persistence of the HIV reservoir. - Source: PubMed
Publication date: 2026/03/21
Butta Giacomo MAlburquerque BremyKearns CharlotteHadas YoavVanDyck Max WScaglioni SusannaPeña NoahWong Hoi TongLevendosky ElizabethGleason CharlesLin XiaoManganaro LaraPinto DalilaMulder Lubbertus C FSimon Viviana - Extracellular vesicles, which carry bioactive cargos such as proteins, RNAs, and lipids, represent promising drug delivery vehicles owing to their biocompatibility, low immunogenicity, and inherent tissue-targeting capabilities. To address the current limitations in controlled cargo loading, we developed an abscisic acid (ABA)-inducible proximity system that directs proteins into exosomes during biogenesis. We engineered exosomal scaffolds by fusing the ABA receptor PYL1 to EV-enriched proteins-including BASP1, CD9, PTGFRN, and a truncated form PTGFRNΔ687-thereby creating docking sites within the exosomal lumen, while the target cargo (e.g., EGFP, firefly luciferase, or Cas9) was tagged with the ABI1 phosphatase domain. We demonstrate that ABA administration in producer cells induces PYL1-ABI1 complex formation, which recruits ABI1-fused cargo for selective encapsulation into EVs. Among the scaffolds tested, BASP1-PYL1 proved the most effective, enabling robust, ABA-dependent enrichment of cargo proteins. Purified EVs maintained canonical morphology, size, and marker expression (CD63, syntenin-1, CD9), confirming preserved biogenesis. Critically, these loaded exosomes efficiently delivered functional cargo to recipient cells, enabling Cas9/sgRNA-mediated genome editing. Together, our findings establish an ABA-triggered molecular switch for controllable EV protein loading, providing a versatile platform for next-generation therapeutic delivery. - Source: PubMed
Publication date: 2026/02/26
Wei SaiLi JianTuo HuacanWang WeiLi GuoWen Luan - Starting from human colon cancer cells showing aberrant WNT/β-catenin/TCF signaling, hyperactivated and silenced , we generated stable cell lines overexpressing , either ectopically, or by reactivating the dormant promoter using a lentiviral CRISPR-based system. encodes a neuronal signaling protein and transcriptional corepressor, from which tumor-suppressive functions have been described in avian cell systems and in multiple human cancer cell types. Proteome and transcriptome analyses revealed activation of several tumor and metastasis suppressors in BASP1-expressing cells, which also show strong repression of the transformed phenotype in terms of contact inhibition, anchorage-independent growth, and tumor formation. Cells with reactivated BASP1 display a flat and differentiated morphology with enhanced migratory potential, accompanied by expression of multiple genes implicated in actin polymerization, focal adhesion, and neuronal migration. Furthermore, MYC protein expression is substantially repressed due to BASP1-mediated transcriptional downregulation involving BASP1 interaction with β-catenin and binding to the promoter. Upon activation, multiple key proteins of the canonical WNT signaling pathway become suppressed. One of these BASP1 targets is the protein kinase TNIK catalyzing phosphorylation of TCF7L2, the latter required for transcriptional activation. Results obtained with a preclinical TNIK inhibitor in human colorectal cancer cells show efficient abrogation of MYC expression and consequently impaired dimerization with its interaction partner MAX. The antagonistic BASP1 effect on MYC and the MYC dependency on TNIK could enhance the development of strategies to interfere with oncogenic functions of the cancer driver MYC. - Source: PubMed
Publication date: 2026/03/05
Weber Leonie ITimpen Lea EEgger-Hörschinger Anna-SophiaSchöpf PhilemonAyhan Nesin DDemmel DavidHotze MadlenZhang YangMehrabi MahdiPuglisi KaneStefan EduardGhaffari-Tabrizi-Wizsy NassimRamos-Pittol José MKwiatkowski MarcelHartl Markus - Pyroptosis, an inflammatory form of programmed cell death, contributes to intestinal inflammation in inflammatory bowel disease (IBD), but the key cell types and regulatory genes remain unclear. - Source: PubMed
Publication date: 2026/02/04
Lu YaoLin YahuiLi YuansenSai HuanChen ChengLi Jinjiao - We performed a label-free quantitative plasma proteomic analysis on samples from eight astronauts who completed a 6-month mission aboard the International Space Station, using an Orbitrap Fusion Lumos mass spectrometer (MS). Blood samples were collected from each astronaut at different times, i.e., pre-flight, in-flight, and post-flight. We found that the abundance levels of 16 proteins were significantly altered (p ≤ 0.05), particularly in the in-flight samples. The functions of these 16 proteins are associated with four major pathways that pose health risks to astronauts: impairment of the immune system, reorganization of the cytoskeleton, coagulation disorders, and abnormal metabolism. Following the spaceflight, the levels of certain proteins, such as Apolipoprotein L1 (APOL1) and inter-alpha-trypsin inhibitor heavy chain H2 (ITIH2), returned to or close to their preflight levels. While the abundance levels of some proteins involved in the actin cytoskeleton (e.g., pleckstrin or PLEK) and coagulation (e.g., platelet glycoprotein 1b alpha chain or GP1BA) decreased, others such as Brain acid soluble protein 1 (BASP1) and Insulin-like growth factor-binding protein 4 (IGFBP4) increased postflight. Although the mechanisms underlying the upregulation or downregulation of these proteins are not yet fully understood, they may play functional roles in response to spaceflight or in re-adjusting to Earth. This may impact cellular and tissue integrity as well as homeostasis, potentially leading to long-term health risks. Our findings have important implications for developing strategies to mitigate the adverse effects of spaceflight on human health. - Source: PubMed
Publication date: 2025/09/09
Rithidech KanokpornMohallem RodrigoAryal Uma KPeanlikhit TanatCrucian Brian