Ask about this productRelated genes to: ACPP antibody
- Gene:
- ACPP NIH gene
- Name:
- acid phosphatase, prostate
- Previous symbol:
- -
- Synonyms:
- ACP3, ACP-3, PAP
- Chromosome:
- 3q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-05-30
- Date modifiied:
- 2019-01-28
Related products to: ACPP antibody
Related articles to: ACPP antibody
- Extracellular cathepsin B is a driver of tumor progression and metastasis, and its potential as a diagnostic and prognostic marker is increasingly recognized. To harness its activity for triggering the uptake of activatable cell-penetrating peptides (ACPPs) , kinetically suitable and stable endopeptidase substrates for this cysteine protease, which mainly acts as a carboxydipeptidase, are required. This challenge was tackled by C-terminal elongation of the previously identified GIVRAK sequence to octapeptides and systematic structural variation, which has revealed that the endopeptidase activity of cathepsin B is associated with kinetic hysteresis and the P4' residue plays a key role in this regard, as further investigated by enzyme-substrate docking in silico. By replacing the N-terminal motif with GFLG and focused -methylation of the backbone, the substrate serum half-life was extended from 3.7 min to 23.4 h. Integrating this sequence into the fluorophore-conjugated ACPP and fluorescence microscopy in U87MG cells confirmed cathepsin B-mediated uptake on the basis of selective inhibitors and control probes. PET imaging and biodistribution studies with a NODAGA-conjugated ACPP analogue radiolabeled with copper-64 in a murine U87MG-derived xenograft model together with radiopharmacological investigations in normal Wistar rats demonstrated more favorable pharmacokinetics compared to the corresponding CPP. Although tumor-associated proteolytic activation is indicated, this does not contribute to tumor retention as judged from control experiments under pharmacological blockade of cathepsin B and with nonfunctional analogues. The obtained results are discussed in the context of previous data for radiolabeled ACPPs, and limitations for the general use of ACPPs for radiotheranostic approaches are highlighted. - Source: PubMed
Publication date: 2026/02/18
Kuhne KonstantinStrohbach LydiaNeuber ChristinWodtke RobertRuiz-Gómez GloriaBelter BirgitBrandt FlorianGluhacevic von Krüchten LaraKeller MaxPisabarro M TeresaKopka KlausPietzsch JensLöser Reik - Abdominal aortic aneurysm (AAA) is a life-threatening vascular disorder characterized by excessive oxidative stress, chronic inflammation, and extracellular matrix (ECM) degradation. Despite its high prevalence and poor clinical outcomes, no effective pharmacological therapies currently exist. Here, we developed a theranostic liposomal nanoplatform co-loaded with kaempferol (KPF), a natural flavonoid with potent anti-inflammatory and antioxidant activity, and indocyanine green (ICG), a photoacoustic imaging agent. The platform was surface-modified with an activatable cell-penetrating peptide (ACPP), a protease-cleavable cell-penetrating peptide that becomes active upon exposure to MMP-9 in AAA lesions, thereby enabling targeted delivery. The resulting formulation (ICG-KPF@ALNPs) exhibited selective accumulation in aneurysmal tissues and produced strong photoacoustic signals in vitro and in vivo. Therapeutically, ICG-KPF@ALNPs markedly reduced reactive oxygen species (ROS), suppressed inflammatory cytokines, and preserved ECM integrity. Mechanistically, kaempferol exerted a dual protective effect by activating the Nrf2/HO-1 pathway to scavenge ROS and inhibiting the NLRP3 inflammasome to limit macrophage pyroptosis, collectively mitigating oxidative stress and inflammation. These findings highlight ICG-KPF@ALNPs as a promising nanotheranostic strategy for noninvasive imaging and targeted treatment of AAA. - Source: PubMed
Publication date: 2026/03/27
Chen AnqiHuang ZhenganZeng WeiLiang YanxiaWen GuanxiYe JiayuGuo YanbinXu JinfengLiu YingyingFei Hongwen - To assess patency and characterize anatomical patterns of restenosis following percutaneous transluminal angioplasty (PTA) of cephalic arch stenosis (CAS) from patients with hemodialysis arteriovenous fistulas who were enrolled in the ArterioVeNous Stent Graft in the TreatmEnt of Venous OutfloW Stenosis in Arteriovenous Fistula Access Circuits (AVeNEW) trial. - Source: PubMed
Publication date: 2026/03/20
Strieder de Oliveira GuilhermeUnderwood MargoDolmatch Bart - The development of effective delivery systems for peptide nucleic acids (PNAs) into bacterial cells remains a critical challenge in antisense therapeutics. We report the design and evaluation of hydroxamate siderophore-PNA conjugates that exploit bacterial iron uptake pathways for targeted delivery. We demonstrate that modulating the backbone flexibility of hydroxamate siderophores, through glycine or alanine spacers, enhances iron(III) binding affinity and PNA delivery efficiency into Escherichia coli cells. Molecular dynamics simulations revealed that glycine insertion increases backbone flexibility, enabling optimal coordination of all three hydroxamate groups to iron(III). Circular dichroism spectroscopy and iron(III) competition assays confirmed that the siderophores form stable Λ-configured ferric complexes, with the flexible siderophore showing superior iron(III)-binding affinity compared to the less flexible analog. Growth recovery experiments using E. coli mutants deficient in several transporters indicated recognition and internalization of the siderophores via the TonB-dependent hydroxamate pathway. Molecular docking demonstrated the affinity of these siderophores for E. coli hydroxamate receptors, with binding scores comparable to those of natural siderophores. All three siderophore carriers successfully delivered functional PNA targeting the mrfp reporter gene into bacterial cells, achieving sequence-specific gene silencing as confirmed by fluorescence measurements and confocal microscopy. Additionally, bacteriostatic activity was observed for the best-performing siderophore mimic conjugated with a PNA targeting the essential acpP gene. - Source: PubMed
Publication date: 2026/03/17
Tsylents UladzislavaMaj PiotrWdowiak MateuszStadnicki JanMieczkowski AdamWojciechowska MonikaTrylska Joanna - Spinal cord injury (SCI) is a debilitating disorder characterized by intricate pathological processes that result in severe motor and sensory deficits. Existing therapeutic approaches remain insufficient to achieve comprehensive functional restoration, indicating the necessity of alternative treatment strategies. In this study, an advanced nanoparticle-based drug delivery system was established using extracellular vesicles (EVs) modified with a matrix metalloproteinase (MMP)-responsive peptide, ACPP, to achieve the targeted delivery of paclitaxel (PTX). The ACPP-EVs@PTX formulation integrates the drug loading capacity of EVs, the lesion-targeting capability conferred by ACPP, and the neuroprotective properties of PTX. Enhanced accumulation of PTX at the SCI lesion site was achieved, accompanied by a reduction in the off-target distribution. Both in vitro and in vivo experiments demonstrated marked therapeutic efficacy of ACPP-EVs@PTX through modulation of the SCI microenvironment, including stimulation of angiogenesis, attenuation of inflammatory responses, alleviation of oxidative stress, and promotion of axonal regeneration. In addition, the activation of PINK1-Parkin-mediated mitophagy was observed, leading to improved mitochondrial function and enhanced neuronal repair. Behavioral evaluations further confirmed significant recovery of neurological function, supporting the translational potential of this multitarget, synergistic therapeutic strategy. Collectively, this work establishes an integrated therapeutic strategy for spinal cord repair and supports its translational potential. - Source: PubMed
Publication date: 2026/03/03
Zhao ShuxianDuan LiqunLv ZuogangHan ZhiqiangXu WenbinZhang KaikaiLiu WeiBai JiaxiangCai WeihuaZhang WenzhiGao YufengRong Yuluo