KAT5 Control Peptide antibody _CP
- Known as:
- KAT5 Control Peptide (anti-) _CP
- Catalog number:
- 'AP11108CP-N
- Product Quantity:
- 0.1 mg
- Category:
- -
- Supplier:
- ACR
- Gene target:
- KAT5 Control Peptide antibody _CP
Related genes to: KAT5 Control Peptide antibody _CP
- Gene:
- KAT5 NIH gene
- Name:
- lysine acetyltransferase 5
- Previous symbol:
- HTATIP
- Synonyms:
- TIP60, PLIP, cPLA2, HTATIP1, ESA1, ZC2HC5
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2000-04-13
- Date modifiied:
- 2016-10-05
Related products to: KAT5 Control Peptide antibody _CP
Related articles to: KAT5 Control Peptide antibody _CP
- Polycystic ovary syndrome (PCOS) is characterized by oxidative stress (OS). This study reveals a novel epigenetic mechanism linking lysine acetyltransferase 5 (KAT5) and thrombospondin-1 (TSP-1) in PCOS pathogenesis. A meta-analysis of 50 clinical studies demonstrated elevated systemic oxidative markers (total oxidant status, nitric oxide, malondialdehyde) and reduced paraoxonase-1 levels in PCOS patients, alongside compromised total antioxidant capacity in follicular fluid. Bioinformatic analysis identified TSP-1 as a key downregulated gene in PCOS, and the hTFtarget database predicted KAT5 as an upstream regulator of TSP-1. In vitro, H₂O₂-induced oxidative stress in KGN granulosa cells suppressed TSP-1, KAT5, and H2AK5ac levels, which were restored by N-acetylcysteine (NAC). Mechanistically, KAT5 was found to regulate TSP-1 expression via H2AK5 acetylation at its promoter. Knockdown of KAT5 exacerbated oxidative stress, apoptosis, and senescence, while TSP-1 overexpression counteracted these effects. In a letrozole-induced PCOS rat model, ovarian tissues exhibited decreased H2AK5 acetylation, reduced KAT5 and TSP-1 expression, and impaired redox homeostasis. Interventions with N-acetylcysteine or TSP-1 ameliorated ovarian pathological changes, hormonal imbalances, oxidative stress, apoptosis, and cellular senescence. Collectively, these findings establish the KAT5-TSP-1 axis as a critical regulator of ovarian redox homeostasis, unveiling a novel epigenetic mechanism and proposing a dual-target therapeutic strategy for PCOS. - Source: PubMed
Publication date: 2026/07/21
Jin QiuYang WeiWang ChaoLiu YuWang RuijingLiu LiZhang XianghanYan JinLiu Meimei - Cisplatin resistance is a major barrier to effective treatment of squamous cell carcinoma (SCC) including cutaneous SCC and Head and neck SCC, where resistance develops in more than half of advanced cases. Our previous work demonstrated that genetic knockdown or pharmacological inhibition of TIP60 (KAT5), a histone acetyl transferase, sensitizes cisplatin-resistant SCC cells, induces cell cycle arrest and promotes cell death, suggesting a key role for TIP60 in mediating resistance. Here, we use cisplatin-sensitive and -resistant SCC cell lines, together with siRNA-mediated gene silencing, stable overexpression, pharmacological inhibition, immunodot-blot assays, and ICP-MS to demonstrate that TIP60 promotes resistance through two complementary pathways: (1) upregulation of the efflux transporter ABCC1, which reduces intracellular cisplatin accumulation, and (2) increased expression of XPC, a key component of the nucleotide excision repair pathway, involved in recognition and removal of cisplatin-DNA adducts. Elevated TIP60 levels correlate with reduced cisplatin-DNA adduct levels, enhanced removal of cisplatin-DNA adducts and increased cell survival in resistant lines. TIP60 depletion reduces ABCC1 expression and increases cisplatin-DNA adduct levels, effects similarly observed with the ABCC1 inhibitor, MK-571. In parallel, TIP60 knockdown impairs removal of cisplatin-DNA adducts and reduces expression of multiple DNA damage response (DDR) genes, including XPC. Combined inhibition of TIP60 with spironolactone (targeting XPB/NER) or with MK-571 further reduces cell survival and increases cell death in resistant cells. These findings establish TIP60 as a regulator of cisplatin resistance that integrates drug efflux and DNA repair pathways, highlighting TIP60 inhibition as a promising therapeutic strategy to overcome platinum resistance in SCC. - Source: PubMed
Publication date: 2026/07/16
Hira AkshayCraig Michael PMcLaughlin CarolineZhang JinTurchi John JKemp Michael GNahhas Ramzi WKadakia Madhavi P - Lysine acetyltransferase 5 (KAT5) plays a critical role in epigenetic regulation and is closely associated with the progression of various cancers, particularly hepatocellular carcinoma. However, convenient and portable methods for monitoring KAT5 activity remain limited. Herein, we report a coordination-regulated colorimetric sensing platform based on the localized surface plasmon resonance of gold nanoparticles (AuNPs) for KAT5 activity detection. In this strategy, Zn coordinates with ethylenediamine (en) to form Zn(en) complexes, which induce AuNPs aggregation and a distinct plasmonic color change. In the presence of coenzyme A (CoA), generated during the KAT5-catalyzed acetylation reaction, Zn preferentially binds to thiol-containing CoA, suppressing Zn(en) formation and inhibiting AuNPs aggregation. As a result, KAT5 activity is indirectly converted into a measurable colorimetric signal with a detection limit of 1.9 pg/mL (3σ/slope). To enable portable analysis, smartphone-based image processing was integrated, using the blue-to-red (B/R) ratio for quantification. The platform was further applied to investigate histone acetylation in cancer cells and circulating tumor cell (CTCs)-like models during epithelial-mesenchymal transition, revealing dynamic changes in KAT5 activity. This coordination-mediated AuNPs strategy provides a simple and portable tool for monitoring cancer-related enzymatic activity, with potential applications in liquid biopsy, early cancer diagnosis, and precision medicine. - Source: PubMed
Publication date: 2026/05/28
Zhao XingyuCheng CaizhaoChen JiayunYao JingluZhang QingqingHu YufangQing Zhihe - Anaplastic thyroid carcinoma (ATC) is an exceptionally aggressive malignancy with dismal survival, largely due to intrinsic cisplatin resistance. This study identifies a novel mechanism by which small extracellular vesicles (sEVs) promote chemoresistance by enhancing DNA repair via protein lactylation. ATC cells secrete sEVs enriched with Annexin A2 (ANXA2). Upon delivery to recipient ATC cells, ANXA2 stabilizes the interaction between SRC kinase and lactate dehydrogenase A (LDHA), leading to increased LDHA phosphorylation (Y10), enzyme activity, and lactate production. The resulting lactate surge serves as a substrate for lysine lactylation. Ku80 (XRCC5) is identified as a key lactylation target at K265, catalyzed by the acyltransferase KAT5. This lactylation modification strengthens the interaction between Ku80 and its partner Ku70 (XRCC6), stabilizing the initial DNA-end binding complex in the non-homologous end-joining (NHEJ) repair pathway. Consequently, NHEJ efficiency is significantly enhanced, enabling ATC cells to rapidly repair cisplatin-induced DNA double-strand breaks and survive treatment. Genetic disruption of the XRCC5-K265 lactylation site or pharmacological inhibition of LDHA sensitizes ATC xenograft tumors to cisplatin, while in vitro, inhibition of the SRC/LDHA axis produces a similar chemosensitizing effect. This work unveils the ANXA2 sEV/SRC/LDHA/lactate/XRCC5-lactylation axis as a critical driver of NHEJ-mediated chemoresistance in ATC, offering new potential therapeutic targets. - Source: PubMed
Publication date: 2026/07/03
Su ShanshanXiong YiShanLiang YuxuanMin XiangDai Daofeng - Pulmonary fibrosis (PF) remains a lethal progressive disease with poorly defined molecular drivers. Epithelial dysfunction and metabolic reprogramming contribute to PF, but the mechanistic link between these processes remains unclear. Here, we identify a Kat5-STAT6 epigenetic-metabolic axis that governs fibrotic progression. Kat5 directly acetylates STAT6 at lysine 636 (K636), thereby suppressing STAT6 dimerization, phosphorylation and nuclear translocation. In fibrotic lungs, STAT6 acetylation at K636 is reduced, leading to its hyperactivation. Activated STAT6 drives transcription of pro-glycolytic enzyme hexokinase 2 (HK2), promoting metabolic reprogramming in alveolar type II (ATII) cells and extracellular matrix deposition. ATII cell-specific restoration of Kat5 rescues STAT6 acetylation, normalizes its activity and ameliorates fibrosis in vivo. Mechanistically, Kat5-mediated STAT6 acetylation functions as a biochemical brake that limits cooperation with profibrotic mediators such as tissue plasminogen activator (tPA). These findings redefine STAT6 regulation, highlight an acetylation-phosphorylation checkpoint controlling fibrogenesis, and suggest that Kat5 enhancers or STAT6 acetylation mimetics may represent potential therapeutic strategies for chronic lung disease. - Source: PubMed
Publication date: 2026/07/03
Yang YoujingLing YiLi JianzhongLi QianminFeng YanmeiXiao JunMa YuTao Shasha