SQSTM1 Antibody (Center S207) Blocking Peptide
- Known as:
- SQSTM1 Antibody (Center S207) Blocking Peptide
- Catalog number:
- BP19360c
- Product Quantity:
- 2
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SQSTM1 Antibody (Center S207) Blocking Peptide
Related genes to: SQSTM1 Antibody (Center S207) Blocking Peptide
- Gene:
- RNA5SP207 NIH gene
- Name:
- RNA, 5S ribosomal pseudogene 207
- Previous symbol:
- RN5S207
- Synonyms:
- -
- Chromosome:
- 6p21.1
- Locus Type:
- pseudogene
- Date approved:
- 2011-11-04
- Date modifiied:
- 2014-11-19
- Gene:
- SQSTM1 NIH gene
- Name:
- sequestosome 1
- Previous symbol:
- PDB3, OSIL
- Synonyms:
- p62, p60, p62B, A170
- Chromosome:
- 5q35.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-06-13
- Date modifiied:
- 2019-03-07
Related products to: SQSTM1 Antibody (Center S207) Blocking Peptide
Related articles to: SQSTM1 Antibody (Center S207) Blocking Peptide
- Dihydroorotate dehydrogenase (DHODH) is a critical enzyme involved in pyrimidine biosynthesis anda key suppressor of ferroptosis. This enzyme is commonly overexpressed in colorectal cancer (CRC), and itsupregulation facilitates the malignant progression of CRC tumors. - Source: PubMed
Publication date: 2026/08/20
Wang WeibingHu Xigang - To investigate the effect of electroacupuncture (EA) on hepatic autophagy in obese mice by regulating the adenosine monophosphate-activated protein kinase (AMPK)/mammalian target of rapamycin (mTOR)/unc-51 like autophagy activating kinase 1 (ULK1) signaling pathway. - Source: PubMed
Zhang Ying-RongZhou Zhong-YuXia Jun-NiWang Yi-FeiZhang Zi-YiLiao Lu-LuWang Jia-Jie - Porphyrias are rare metabolic disorders arising from defects in heme biosynthesis, leading to accumulation of toxic porphyrin intermediates, mitochondrial dysfunction, and liver injury. Current therapies are limited in efficacy, emphasizing the need for novel treatments. Prior studies showed hepatocyte-specific β-catenin deletion attenuates porphyrin accumulation and liver injury in 3,5-diethoxycarbonyl-1,4-dihydrocollidine (DDC)-induced porphyria. We hypothesized that inhibiting components of the Wnt-β-catenin-glutamine synthesis (GS) pathway reduces heme synthesis and also enhances porphyrin clearance by activating autophagy and improving mitochondrial quality control. We combined pharmacologic Wnt inhibition and hepatocyte-specific GS deletion in murine models of porphyria. Readouts included spatial transcriptomics, targeted metabolomics, immunohistochemistry, confocal mt-Keima imaging, high-resolution respirometry, and transmission electron microscopy. Human liver biopsies and explants from porphyria patients were also examined by dual-label immunohistochemistry. Wnt inhibition during DDC suppressed upregulation of heme biosynthesis genes, reduced porphyrin intermediate accumulation, and enhanced autophagic flux. GS deletion attenuated porphyrin biosynthesis by limiting intracellular glutamine. Wnt and GS deletion produced additive increases in autophagy, restored zonation, and further reduced porphyrin accumulation. Wnt inhibition restored mitophagy, whereas GS deletion primarily improved mitochondrial coupling efficiency. Wnt inhibition also decreased fibrosis in a genetic mouse model of porphyria. Patient samples mirrored murine findings, with heme enzymes and autophagy inversely correlated with β-catenin expression in porphyria cutanea tarda. By disrupting Wnt-GS signaling, we establish a link between increased autophagy, reduced porphyrin formation, and heme pathway regulation in mouse and human liver. These findings identify the Wnt signaling pathway as a potential therapeutic target in porphyria. ALA: δ-Aminolevulinic acid; AIP: acute intermittent porphyria; ALAS: aminolevulinic acid synthase; ALAD: aminolevulinic acid dehydratase; ALP: alkaline phosphatase: AST: aspartate aminotransferase; ALT: alanine aminotransferase; DAB: 3,3'-diaminobenzidine; DDC: 3,5-diethoxycarbonyl-1,4-dihydrocollidine; EPP: erythropoietic protoporphyria; Fech: ferrochelatase; GAPDH: glyceraldehyde 3-phosphate dehydrogenase; GS: glutamine synthesis; H&E: hematoxylin and eosin: HO-1: heme oxygenase 1; IHC: immunohistochemistry; KO: knockout; LAMP1: lysosomal associated membrane protein 1; LC3: microtubule-associated protein 1 A/1B-light chain 3; mTOR: mechanistic target of rapamycin; PBG: porphobilinogen; PBS: phosphate-buffered saline; PP-IX: protoporphyrin-IX; PCT: porphyria cutanea tarda; RCR: respiratory control ratio; SQSTM1/p62: sequestosome 1; TEM: transmission electron microscopy; Wnt-I: Wnt-C59 (inhibitor). - Source: PubMed
Publication date: 2026/08/19
Balogun OluwashanuCornuet PamelaLee ElizabethPatel GarimaRaheem Abdul-ShahidZhu JunjieVandevender Amber MarieAshokan Anila PNasrollahi RahelehWest Raymond EPeck Palmer OctaviaLiu Jia-JunNolin Thomas DSt Croix ClaudetteMa XiaochaoBullock GrantLiu SilviaMonga Satdarshan PStolz Donna BeerJurczak MichaelOmary M BishrNejak-Bowen Kari - Macroautophagy (MA) and chaperone-mediated autophagy (CMA) are lysosomal degradation pathways with context-dependent roles in cancer. However, how MA- and CMA-associated transcriptional states jointly relate to cancer molecular features and drug responses remains unclear. Here, we developed a transcriptome-based framework integrating MA- and CMA-associated gene signatures to define relative MA and CMA states across cancer types. These states were associated with distinct patterns of genomic instability, oncogenic signaling, immune features, and pharmacogenomic profiles. In pooled cancer cell-line analyses, MA CMA states were associated with relative resistance to EGFR tyrosine kinase inhibitors (EGFR-TKIs), whereas MA CMA states showed greater sensitivity, nominating an autophagy-associated pharmacological pattern for mechanistic investigation. Using KRAS-mutant pancreatic cancer cells as an autophagy-dependent, therapy-resistant model, we found that depletion enhanced sensitivity to EGFR-TKIs in an MA-dependent manner. All-trans retinoic acid (ATRA), a pleiotropic retinoid that modulated CMA-related activity in this system, phenocopied key effects of genetic CMA suppression and potentiated sensitivity to EGFR-TKIs. CMA suppression was associated with increased autophagic flux, TFEB nuclear localization, and ULK1 phosphorylation changes consistent with MA activation. Moreover, transcriptomic analysis reveals that CMA suppression sensitizes cancer cells to EGFR-TKIs at least partially through downregulation of SEMA6D. SEMA6D depletion enhanced autophagic flux, increased lysosomal capacity, and partially contributed to the response to combined EGFR-TKI and ATRA treatment. In PANC-1 xenografts, ATRA potentiated EGFR-TKI-mediated tumor suppression without significant toxicity. Together, these findings establish a transcriptome-based MA-CMA framework for prioritizing context-dependent autophagy-associated vulnerabilities and provide focused mechanistic support for MA-CMA crosstalk in KRAS-mutant pancreatic cancer models. ACTB: actin beta; ANOVA: analysis of variance; ARI: adjusted rand index; ATRA: all-trans retinoic acid; BLCA: bladder urothelial carcinoma; BSA: bovine serum albumin; CMA: chaperone-mediated autophagy; CNV: copy number variation; COAD: colon adenocarcinoma; DEG: differentially expressed gene; DMEM: dulbecco's modified eagle medium; DMSO: dimethyl sulfoxide; EBSS: Earle's balanced salt solution; EGFR: epidermal growth factor receptor; EGFR-TKI: EGFR tyrosine kinase inhibitor; EV: empty vector; FBS: fetal bovine serum; FDR: false discovery rate; FM: full medium; HCQ: hydroxychloroquine; HNSC: head and neck squamous cell carcinoma; H&E: hematoxylin and eosin; i.p.: intraperitoneally; HRD: homologous recombination deficiency; HSPA8/HSC70: heat shock protein family A (Hsp70) member 8; KIRC: kidney renal clear cell carcinoma; LAMP2A: lysosome associated membrane protein 2A; LGG: lower-grade glioma; LOH: loss of heterozygosity; LUAD: lung adenocarcinoma; LUSC: lung squamous cell carcinoma; MA: macroautophagy; MSI: microsatellite instability; MSigDB: molecular signatures database; OR: odds ratio; PDAC: pancreatic ductal adenocarcinoma; qRT-PCR: quantitative real-time PCR; SEMA6D: semaphorin 6D; sgRNA: single-guide RNA; siRNA: small interfering RNA; SKCM: skin cutaneous melanoma; SMD: standardized mean differences; SNV: single-nucleotide variant; SQSTM1/p62: sequestosome 1; ssGSEA: single-sample gene set enrichment analysis; STAD: stomach adenocarcinoma; TCGA: the cancer genome atlas; TMB: tumor mutation burden; TPM: transcripts per million. - Source: PubMed
Publication date: 2026/08/19
Feng JilingZeng YuWu HaoFeng YuanlongLuo ShengnanDong ShuxianLi Shengli - Polymyxins remain indispensable last-line antibiotics for multidrug-resistant Gram-negative infections, yet their clinical use in central nervous system (CNS) infections is constrained by poorly understood neurotoxicity. Here, we define the early molecular signalling events underlying polymyxin B-induced CNS toxicity using an integrated phosphoproteomic and Reverse Phase Protein Array (RPPA) approach in rat brain following intracerebroventricular administration. Global phosphoproteomics revealed extensive phosphosite coverage but identified a highly selective set of significantly regulated phosphosites, implicating calcium-dependent signalling, transcriptional stress regulation, synaptic signalling, and cytoskeletal control, while parallel total proteomics showed minimal changes in protein abundance. RPPA profiling independently confirmed coordinated modulation of stress, apoptotic and survival-associated signalling pathways, including p53, CREB, SQSTM1, Bcl-2, and NFκB related nodes. Network and functional enrichment analyses converged on DNA damage signalling, apoptotic regulation and growth factor-mediated pathways as central features of the polymyxin B early neurotoxicity response, while phosphor to total protein analyses demonstrated suppression of proliferative and pro-survival signalling. Together, these data establish phosphorylation-driven signalling reprogramming as a primary early mechanism of polymyxin B-induced neurotoxicity, providing a mechanistic framework that links membrane-active antibiotic exposure to neuronal stress signalling and identifies candidate pathways for toxicity biomarkers and neuroprotective strategies. - Source: PubMed
Publication date: 2026/08/14
Hussein MaythamAnsaf Thuraya SafaaSian Terry C C Lim KamBaker MarkFaridi PouyaKho Zhi YingSelvakumar NivedhithaKaye Keith SRao Gauri GLi JianVelkov Tony