AAMP
- Known as:
- AAMP
- Catalog number:
- 000871A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- AAMP
Related genes to: AAMP
- Gene:
- AAMP NIH gene
- Name:
- angio associated migratory cell protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2q35
- Locus Type:
- gene with protein product
- Date approved:
- 1996-11-13
- Date modifiied:
- 2016-10-04
Related products to: AAMP
Related articles to: AAMP
- Myocardial ischemia/reperfusion injury (MI/RI) is an inevitable consequence of reperfusion therapy for ischemic myocardium. Endothelial protection and therapeutic angiogenesis are pivotal strategies for attenuating MI/RI and restoring myocardial perfusion. To investigate the chemical basis underlying the vasoprotective potential of Carthamus tinctorius, we utilized both in vivo (PTK787-induced intersegmental vessel injury in zebrafish) and in vitro (OGD/R-injured HUVECs) assays. The 30% EtOH eluate obtained from D101 macroporous resin chromatography of the Carthamus tinctorius extract exhibited significant pro-angiogenic and endothelial-protective activities. Subsequent HPLC-UV-guided fractionation afforded seven previously undescribed quinochalcone C-glycosides (QCGs, 1-7). Their structures were established by comprehensive spectroscopic analysis, including HRMS (ESI), 1D/2D NMR, UV, IR, CD, and NMR chemical shift calculations. Saffloquinoside G (1) is a monomeric QCG bearing a furan moiety, whereas carthorquinosides CH (2-7) are rare dimers consisting of quinochalcone and flavonol glucoside units linked by a methylene or methine unit. Biological evaluation demonstrated that all dimeric QCGs restored the formation of PTK787-injured intersegmental vessels. Notably, compounds 1 and 2 significantly increased HUVEC viability under OGD/R conditions. Compound 2 also promoted cell migration and tube formation, concomitantly upregulating angiogenic markers (VEGF, CD31, and Ki-67). SILAC-based proteomic profiling identified angio-associated migratory cell protein (AAMP) as a potential target of 2. CETSA and DARTS assays confirmed the direct interaction between 2 and AAMP, and molecular dynamics simulations revealed moderate conformational rearrangements upon binding. Further studies revealed that 2 rescued PTK787-impaired intersegmental and subintestinal vessels in a dose-dependent manner in vivo. - Source: PubMed
Publication date: 2026/09/12
Wang Yong-XiangZhang XianBao Jia-XuZhao Yun-FangTu Peng-FeiHuo Hui-XiaLi Jun - The C-terminal to LisH (CTLH) complex is a modular multi-subunit E3 ligase with diverse biological functions, yet how its overall ubiquitylation activity is tuned remains unclear. Here, we identify CDK- and mTOR-dependent phosphorylation of the cognate E2 enzyme UBE2H as a key regulator of CTLH E3 catalytic capacity. Phosphorylation of two N-terminal serine residues (S3/S5) reduces UBE2H charging with ubiquitin, thereby limiting the pool of active E2 available to CTLH. Mitotic CDK activity inactivates UBE2H during mitosis, whereas mTOR restrains UBE2H charging in interphase to couple CTLH-dependent ubiquitylation to nutrient status. Preventing this phosphorylation maintains UBE2H charging, enhances CTLH-mediated substrate degradation, promotes CTLH subunit turnover, and causes proliferation and mitotic defects. Using hyperactive UBE2H, we identify two additional CTLH substrates, the mitotic kinase NEK9 and Angio-associated migratory cell protein (AAMP) and define a DR-like C-degron recognized by the CTLH subunit MKLN1. These findings reveal how regulation of an E2 enzyme by cell cycle and nutrient signaling pathways dynamically shape CTLH activity. - Source: PubMed
Publication date: 2026/03/09
Chen YingqianRossio ValentinaPaulo Joao AKarki MenukaManohar SandhyaOzimek NoelleFrizzi LauraGygi Steven PKing Randall W - Gallium-68 labeled peptide radiotracers have attracted significant attention in positron emission tomography (PET) imaging of various diseases. While Ga-DOTA radiolabeling protocols are well-established, two classes of peptides, disulfide-directed multicyclic peptides (DDMPs) and amphiphilic antimicrobial peptides (AAMPs), presented challenges in achieving satisfactory radiolabeling efficiency using existing methods. This study therefore aimed to establish optimized Ga-DOTA radiolabeling protocols specifically tailored to these peptides, in order to achieve high radiochemical purity (RCP) and radiochemical yield (RCY) suitable for clinical translation. By systematically varying key labeling conditions and purification methods such as pH, GaCl concentration, reaction time, purification cartridge and eluent types, and sterile filtration, two new radiolabeling protocols were developed for DDMP- and AAMP-based radiotracers. Detailed optimization identified an optimal pH of 3.6 combined with the use of concentrated GaCl for efficient radiolabeling of DDMPs, achieving RCY > 60% and RCP > 95%. For AAMPs, extended reaction time, hydrophilic-lipophilic balanced (HLB) cartridges, and ethanol/HCl elution improved RCY to > 60% with RCP > 90%. These results demonstrate that precise pH control and concentrated GaCl are essential for high labeling efficiency of DDMPs, whereas optimized purification methods are key for AAMPs. Importantly, this work provides efficient radiolabeling strategies for these two clinically promising classes of peptides and offers insights for optimizing labeling protocols for other peptides. The established methods will support subsequent Good Manufacturing Practice (GMP)-compliant manufacturing and facilitate the clinical translation of high-value radiopharmaceuticals with favorable in vivo performance. - Source: PubMed
Publication date: 2026/03/03
Chen XueyaoZhang SiqiJiang ShuoHu Kuan - Many E3 ubiquitin ligases recognize cognate degron motifs located at protein termini, but the paucity of substrates of N-degron and C-degron pathways hampers our understanding of their physiological significance. Here, by devising an expression screening approach to assess the effect of C-terminal "capping" on the stability of thousands of human proteins, we systematically identify a suite of full-length substrates harboring C-terminal degrons. Interrogating one leading candidate, ZMYND19, we characterize a C-degron pathway governed by the Muskelin substrate adaptor of the CTLH E3 ligase complex. Cell-to-cell variability in ZMYND19 stability uncovered conditional regulation, with CTLH-mediated degradation impaired by TNF-α stimulation but enhanced by mTOR inhibition. Parallel genetic and proteomic screens identified two poorly characterized proteins, AAMP and AEN, as additional substrates of the CTLH C-degron pathway, leading us to define an essential role for AAMP in ribosome maturation through chaperone activity towards ribosomal protein uL16. Altogether, these data define a C-degron pathway through which the Muskelin substrate adaptor connects conditional regulation of the CTLH E3 ligase complex to control of ribosome biogenesis. - Source: PubMed
Publication date: 2026/01/14
Grant Drew WTan ShengjiangRamage Dylan ELi Mamie ZDi YingTchasovnikarova Iva AWeekes Michael PElledge Stephen JWarren Alan JTimms Richard T - To investigate the clinical significance of abnormal expression of angio-associated migratory cell protein (AAMP) in hepatocellular carcinoma (HCC). - Source: PubMed
Li ChaoYin GuozhiCheng XiaoJiang Yezhen