SQSTM1 Antibody (N-term S24) Blocking Peptide
- Known as:
- SQSTM1 Antibody (N-terminus S24) Blocking Peptide
- Catalog number:
- BP19120a
- Product Quantity:
- 2
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SQSTM1 Antibody (N-term S24) Blocking Peptide
Related genes to: SQSTM1 Antibody (N-term S24) Blocking Peptide
- Gene:
- CHMP3 NIH gene
- Name:
- charged multivesicular body protein 3
- Previous symbol:
- VPS24
- Synonyms:
- NEDF, CGI-149
- Chromosome:
- 2p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-11
- Date modifiied:
- 2014-11-19
- Gene:
- HSPA4 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 4
- Previous symbol:
- -
- Synonyms:
- HS24/P52, HSPH2
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-26
- Date modifiied:
- 2015-11-19
- Gene:
- KLRK1 NIH gene
- Name:
- killer cell lectin like receptor K1
- Previous symbol:
- D12S2489E
- Synonyms:
- NKG2D, KLR, NKG2-D, CD314
- Chromosome:
- 12p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-12
- Date modifiied:
- 2016-10-05
- Gene:
- MRPS24 NIH gene
- Name:
- mitochondrial ribosomal protein S24
- Previous symbol:
- -
- Synonyms:
- MRP-S24, HSPC335
- Chromosome:
- 7p13
- Locus Type:
- gene with protein product
- Date approved:
- 2001-01-26
- Date modifiied:
- 2016-10-05
- Gene:
- RNA5SP24 NIH gene
- Name:
- RNA, 5S ribosomal pseudogene 24
- Previous symbol:
- RN5S24
- Synonyms:
- -
- Chromosome:
- 13q12.11
- Locus Type:
- pseudogene
- Date approved:
- 2011-08-08
- Date modifiied:
- 2012-08-07
Related products to: SQSTM1 Antibody (N-term S24) Blocking Peptide
Related articles to: SQSTM1 Antibody (N-term S24) Blocking Peptide
- Ischemic stroke is the most prevalent form of stroke worldwide and remains a major cause of long-term disability. Impaired autophagic flux is a critical pathological mechanism that worsens neuronal injury after ischemia. This study aimed to elucidate the role of phosphatidylinositol-5-phosphate 4-kinase type II alpha (PIP4K2A) and its regulation of autophagy in cerebral ischemia/reperfusion (I/R) injury. Exploratory TMT-based serum proteomics identified PIP4K2Aas an elevated candidate protein in patients with acute ischemic stroke (AIS). Whole-blood RT-qPCR validation showed increased PIP4K2A mRNA in AIS patients and an association between higher PIP4K2A expression and lower NIHSS scores, although the small clinical cohort and peripheral sampling design preclude causal or tissue-origin conclusions. Using a transient middle cerebral artery occlusion (tMCAO) mouse model and a primary neuronal oxygen-glucose deprivation/reperfusion (OGD/R) model, we found that I/R injury markedly upregulated PIP4K2A expression in ischemic brain tissue and primary neurons. AAV-mediated PIP4K2A overexpression in vivo alleviated ischemic brain injury, preserved neuronal survival, reduced infarct volume, and improved long-term cognitive and motor functions, whereas PIP4K2A knockdown exacerbated these outcomes. In vitro, lentiviral-mediated PIP4K2A overexpression improved neuronal viability after OGD/R. Mechanistically, RNA-seq, co-immunoprecipitation, and mCherry-EGFP-LC3 tandem reporter analyses showed that PIP4K2A overexpression was associated with reduced TRIB3 mRNA and protein levels, decreased abundance of the stress-induced TRIB3-p62 complex, improved autophagic flux, and reduced autophagosomal accumulation. Concurrently, PIP4K2A-associated TRIB3 reduction was accompanied by enhanced AKT/mTOR signaling. These findings identify PIP4K2A as an endogenous protective regulator in cerebral ischemia/reperfusion injury and suggest that thePIP4K2A/TRIB3/p62 axis may represent a potential therapeutic target for ischemic stroke. - Source: PubMed
Publication date: 2026/07/17
Ma BodunYu XiaotianLi MeiZhu HaoDong XiaofengYu ShuaiWang MeixiaWu GuanhuiWang XiaoHu RuiyaoFeng Hongxuan - T. Fan, H. Pi, M. Li, Z. Ren, Z. He, F. Zhu, L. Tian, M. Tu, J. Xie, M. Liu, Y. Li, M. Tan, G. Li, W. Qing, R. J. Reiter, Z. Yu, H. Wu, and Z. Zhou, "Inhibiting MT2-TFE3-Dependent Autophagy Enhances Melatonin-Induced Apoptosis in Tongue Squamous Cell Carcinoma," Journal of Pineal Research 64, no. 2 (2018): e12457, https://doi.org/10.1111/jpi.12457. The above article, published online on 08 May 2017 in Wiley Online Library (wileyonlinelibrary.com) and its corrigendum (https://doi.org/10.1111/jpi.12645), has been retracted by agreement between the journal Editor-in-Chief, Gianluca Tosini; and John Wiley & Sons Ltd. A third party brought the publisher's attention to a report on PubPeer [1] which suggested that the row of BAX bands in Figure 7E had been duplicated in Figure 8E and represented as CL-PARP following a vertical flip, while the row of GAPDH bands in Figure 7E had also likely been duplicated with further brightness changes and vertical resizing. Additionally, the row of CL-PARP bands in Figure 1B had been duplicated in Figure 2B and represented as SQSTM1 following a horizontal flip, while the row of GAPDH bands had also been duplicated between those same figures. While the corrigendum published online on 28 March 2020 corrected the duplication in Figure 2B, the corrigendum did not address how the mistake was made and did not address the duplications between Figure 7E and 8E. Further investigation by the publisher also found that most of the row of p-TFE3 bands in Figure 6A had been potentially duplicated from another article which shares one of the same authors [Chen et al. 2016 (https://doi.org/10.18632/oncotarget.12894)]. Both articles represented the data as being from different samples. Additionally, one further potential duplication between the c-TFEB and Histone H3 bands in Figure 4B was also detected. The authors responded to an inquiry by the publisher and presented original data as well as original experimental documentation. A review of these data by the publisher found that, while some of the bands in question were not duplicated, there were further discrepancies between the labeling of the original data and the data presented in the article. There were also further discrepancies between the presentation of the original data and the data included in the corrigendum. Following contact with the authors, an additional round of checks found further evidence of image duplication in the supplementary data. Part of the MT2 band in Figure S2A was potentially shared with the p-P70S6K band in Supplementary Figure S4B. Part of the GAPDH band in Figure S3A was shared with the GAPDH band in Figure S3B. A portion of the GAPDH band in Figure S4A was duplicated and represented as P70S6K in Figure S4C. Lastly, a portion of the row of GAPDH bands in Figure S3A was duplicated in Figure 6B in the main article text and represented as Histone H3 while the BAX band in Figure S5 was duplicated in Figure 4B in the main article text and represented as Histone H3. The Retraction has been agreed to because the evidence of image duplication of different samples within this work fundamentally compromises the editors' confidence in the results presented in this article. The authors were informed of the retraction. Reference 1. Phytotoma raimondii. Comments on "Inhibiting MT2-TFE3-Dependent Autophagy Enhances Melatonin-Induced Apoptosis in Tongue Squamous Cell Carcinoma," PubPeer, February 2020. https://pubpeer.com/publications/982C03B89308C90F5E87B7A19843AC. - Source: PubMed
- Longitudinal bone growth occurs via endochondral ossification, involving a complex interplay of chondrocyte proliferation, differentiation, and matrix remodeling. As with all mammalian cells, chondrocytes require dynamin for mitochondrial fission, to shuttle vesicles from the Golgi apparatus, and for both clathrin- and caveolin-mediated endocytosis. Here, we aimed to test the functions of dynamin on bone growth. To do so, we applied dynasore-a small molecule that is a reversible dynamin inhibitor-to mouse metatarsal bones cultured ex vivo. We assessed gross changes using bone length measurements combined with EdU detection, immunostaining, super-resolution microscopy and transmission electron microscopy. - Source: PubMed
Publication date: 2026/07/16
Marchan-Alvarez Jose GKoikkara SanyaZhou RuihanNazaraliyev AmalWiklander Oscar P BNewton Phillip T - The current study examines the role of testosterone and androgen deprivation in regulating mitochondrial quality control, autophagy, and apoptosis during CCl-induced chronic liver injury. Male rats were allocated to Sham, CCl, TP + CCl (testosterone-treated), and Cas + CCl (castrated) groups for 4, 8, and 12 weeks, validated through in vitro assays. Mitochondrial function (MitoTracker, MFN2), lysosomal integrity (LAMP1), autophagy markers (LC3B, Beclin-1, p62/SQSTM1), apoptosis regulators (Bcl-2, cleaved caspase-3), and mTOR signaling were assessed by qRT-PCR, immunohistochemistry, and immunofluorescence. CCl exposure caused progressive increases in cellular stress and fibrotic markers (α-SMA, TGF-β1, and TXNIP), progressive mitochondrial dysfunction, impaired mitochondrial-lysosomal coordination, reduced Beclin-1 and LC3B, p62 accumulation, and a shift toward an anti-apoptotic Bcl-2 imbalance. Testosterone treatment restored mitochondrial membrane potential in vitro, normalized MitoTracker and MFN2 expression, preserved LAMP1 levels, and partially sustained mitochondrial-lysosomal coupling. TP also enhanced Beclin-1 and LC3B, reduced p62 accumulation, and sustained mTOR activity, consistent with improved autophagic flux. Moreover, TP-lowered Bcl-2 was associated with controlled cleaved caspase-3 activation, suggesting selective clearance of damaged hepatocytes rather than widespread apoptosis. In contrast, Cas + CCl animals showed exaggerated mitochondrial impairment, persistent p62 accumulation, reduced LC3B and mTOR signaling, and a pro-apoptotic cleaved caspase-3 profile. Together, these findings demonstrate that testosterone supports mitochondrial-lysosomal homeostasis and autophagy during toxic liver injury, whereas androgen deprivation favors defective autophagy and maladaptive apoptosis, underscoring hormone-dependent regulation of hepatocellular stress responses. - Source: PubMed
Publication date: 2026/07/16
Verma ShobhitVaishnav SomyaYadav ManishaVerma SmritiWashimkar Kaveri RKumar AkhileshMugale Madhav Nilakhanth - Mitophagy-mediated mitochondrial quality control is essential for normal cardiac physiology. In this study, we observed that cardiac RNF10 expression was induced by multiple chronic stressors, including aging, angiotensin II (Ang II) exposure, and obesity. Cardiac-specific RNF10 knockout (RNF10-CKO) mice developed cardiac hypertrophy with aging, characterized by cardiomyocyte enlargement, exacerbated myocardial fibrosis, and impaired cardiac function. Aged RNF10-CKO mice exhibited elevated reactive oxygen species (ROS) levels and reduced mitochondrial membrane potential in cardiomyocytes. Transmission electron microscopy revealed mitochondrial rounding, matrix expansion, and cristae disorganization. Similarly, compared with control mice, Ang II-exposed RNF10-CKO mice exhibited cardiomyocyte hypertrophy, increased fibrosis, and cardiac dysfunction, accompanied by mitochondrial membrane potential depolarization, ROS accumulation, and mitochondrial morphological abnormalities equivalent to those in aged RNF10-CKO mice. Mechanistically, chronic stressors upregulated RNF10 expression, which subsequently mediated the K63-linked polyubiquitination of the mitochondrial outer membrane protein mitofusin 2 (MFN2). This modification stabilized MFN2 on mitochondria and facilitated Parkin recruitment. The accumulated Parkin in mitochondria further promoted the robust recruitment of the autophagy adaptor sequestosome 1 (SQSTM1/p62), leading to increased LC3-II lipidation and the initiation of mitophagy. Notably, this RNF10-mediated mitophagy is dependent on MFN2. However, the effects of RNF10 are independent of those of PINK1. This study identifies RNF10 as a critical regulator of cardiac mitophagy, suggesting that targeting cardiac RNF10 may represent a therapeutic strategy for treating cardiac pathologies. - Source: PubMed
Publication date: 2026/07/15
Song Jia-NiQiu Tong-TongZhang LeiHuang Jin-CanZhang Yu-JieZhang Yin-LiangChang Yong-Sheng