Human PINK1 Antigen Immunoaffinity Purified Polyclonal
- Known as:
- Human PINK1 Antigen Immunoaffinity Purified Polyclonal
- Catalog number:
- x2764p
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Exalpha
- Gene target:
- Human PINK1 Antigen Immunoaffinity Purified Polyclonal
Related genes to: Human PINK1 Antigen Immunoaffinity Purified Polyclonal
- Gene:
- PINK1 NIH gene
- Name:
- PTEN induced kinase 1
- Previous symbol:
- PARK6
- Synonyms:
- BRPK
- Chromosome:
- 1p36.12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-02-08
- Date modifiied:
- 2018-08-29
- Gene:
- PINK1-AS NIH gene
- Name:
- PINK1 antisense RNA
- Previous symbol:
- PINK1-AS1
- Synonyms:
- FLJ00387, PINK1AS, naPINK1
- Chromosome:
- 1p36.12
- Locus Type:
- RNA, long non-coding
- Date approved:
- 2010-08-19
- Date modifiied:
- 2014-09-24
Related products to: Human PINK1 Antigen Immunoaffinity Purified Polyclonal
Related articles to: Human PINK1 Antigen Immunoaffinity Purified Polyclonal
- This study investigated the effects and mechanisms of Suanzao Ren Decoction on anxiety symptoms of chronic unpredictable stress (CUS) model rats. - Source: PubMed
Luo TianyanXiang GuifangLiu Qing - Intervertebral disc degeneration (IVDD) is one of the main causes of lower back pain. The chronic accumulation of aging and apoptosis of nucleus pulposus cells (NPCs) is believed to be related to IVDD. In recent years, mitochondrial autophagy which as an important clearance mechanism within cells, has gradually attracted attention. The PINK1/Parkin signaling pathway is regarded as the key pathway regulating mitochondrial autophagy, and it plays a significant role in physiological and pathological processes of NPCs. The mechanism by which PINK1/Parkin signaling pathway mediates mitochondrial autophagy could be understood as follows, PINK1, as the sensor for mitochondrial quality regulation, is activated. It recruits and activates Parkin to the mitochondrial membrane through phosphorylation of ubiquitin, and then undergoes Parkin-dependent substrate ubiquitination, recruitment of autophagy receptors, formation of autophagosomes, and fusion with lysosomes, ultimately completing the extremely important autophagy process. Current research indicates that abnormality of PINK1/Parkin signaling pathway may be closely related to IVDD, but the specific mechanism still requires further exploration. The paper explores research progress of mechanism by which mitochondrial autophagy affects IVDD based on PINK1/Parkin signaling pathway, with the aim of providing new strategies and targets for the treatment of IVDD. - Source: PubMed
Guo JieLei LingTian HongjingGuo TiefengLuo LinzhaoZhang Yanjun - Mitochondria play a major role in cellular health, yet their contribution to chronic diseases has been underestimated. Mitochondria are essential for all tissues and are the major source of ATP in high-energy-demand organs such as brain and heart, which consequently are vulnerable to mitochondrial dysfunction. Failure to repair or remove damaged mitochondria contributes to aging and chronic diseases. Cells have evolved quality control mechanisms, including mitophagy to eliminate damaged mitochondria and mitobiogenesis to replenish them. The ubiquitin-proteasome system (UPS) is responsible for removing misfolded proteins, a process that is highly ATP dependent and therefore reliant on mitochondrial function. In turn, damaged mitochondria are eliminated through coordinated actions of the UPS and lysosomal degradation through mitophagy. Many neurodegenerative diseases are characterized by the presence of disease-specific protein aggregates, such as α-synuclein aggregates in Parkinson's disease and tau neurofibrillary tangles in Alzheimer's disease. These aggregates impair mitochondrial function, while dysfunctional mitochondria generate reactive oxygen species that further exacerbate proteotoxic stress, creating a pathogenic cycle. This highlights the functional interplay between mitochondria and the UPS. Recent studies have uncovered phosphorylation of ubiquitin at serine 65 by the mitochondrial kinase PINK1 as a key signal of mitochondrial dysfunction. Phospho-Ser65-ubiquitin (pUb) has emerged as an indicator of mitochondrial health and a potential biomarker for aging and neurodegenerative disease. However, due largely to a lack of tools, little is known about the role of pUb in cellular physiology. Here, we review the current landscape of pUb biology, the phospho-ubiquitome, and its role as biomarker for mitochondrial health and neurodegeneration. - Source: PubMed
Publication date: 2026/05/07
Suresh KumarRainville ChristopherSterner David EGoldberg Matthew SButt Tauseef R - Parkinson's disease (PD) is increasingly recognised as a multifactorial and heterogeneous condition rather than a single uniform disorder, supported by advances in molecular biology, genetics and pathology. This review provides a perspective on the shifting concept of PD from an idiopathic, strictly defined pathological entity to a highly heterogeneous clinical and etiopathological condition. We outline the diverse aetiologic pathways and clinical expressions of PD, with particular emphasis on genetic contributors and the role of neuroinflammation. Genetic studies have identified monogenic causes - including SNCA, LRRK2, VPS35, RAB32, PRKN and PINK1 - as well as increased risk linked to heterozygous GBA1variants and more than 90 susceptibility loci from genome-wide association studies (GWAS), highlighting converging pathogenic mechanisms. Recent work underscores significant involvement of innate and adaptive immune responses from the earliest disease stages, suggesting a central shared role in PD onset and progression. This contemporary framework opens new avenues for biology-based, disease-modifying therapeutic strategies. - Source: PubMed
Publication date: 2026/03/30
Kumar Kishore RajWong RussellÇakmak Özgür ÖztopErtan Sibel - : Pressure overload-induced heart failure (HF) involves cardiac remodeling, ferroptosis, and impaired mitophagy. Yixinjiedu formula (YXJDF), a traditional Chinese medicine, shows cardiovascular protective effects, but its underlying mechanisms remain largely unclear. This study aims to evaluate the cardioprotective effect of YXJDF in pressure overload-induced HF and explore its regulatory role in ferroptosis and mitophagy. : A transverse aortic constriction (TAC) mouse model and angiotensin II-induced HL-1 cardiomyocytes were used to assess the therapeutic effects of YXJDF. Cardiac function, ferroptosis, and mitophagy were evaluated using histological, biochemical, molecular, and imaging analyses. Autophagic flux was assessed using lysosomal inhibition. Network pharmacology was applied to identify potential targets, while LC-MS/MS profiling and molecular docking were used to characterize major constituents of YXJDF and predict target interactions. : In TAC mice, YXJDF significantly improved cardiac function and attenuated myocardial hypertrophy and fibrosis. YXJDF suppressed ferroptotic injury, as evidenced by reduced lipid peroxidation, restoration of GPX4 and FTH1 expression, and normalization of antioxidant capacity. Mitophagy was restored, as indicated by increased PINK1 and Parkin expression, enhanced LC3-II accumulation, and reduced p62 and TOM20 levels, and as confirmed by autophagic flux analysis. Consistent protective effects on ferroptosis and mitophagy were observed in angiotensin II-induced cardiomyocytes. Network pharmacology analysis identified PINK1 as a key target, which was validated by in vivo and in vitro experiments. LC-MS/MS identified 20 major chemical constituents in YXJDF, and molecular docking showed strong binding affinity between several compounds (e.g., calycosin, salvianolic acid A) and PINK1. : YXJDF ameliorates pressure overload-induced cardiac injury by restoring PINK1/Parkin-mediated mitophagy and suppressing ferroptosis. These findings reveal a multi-target mechanism underlying the therapeutic potential of YXJDF in HF. - Source: PubMed
Publication date: 2026/02/25
Xie KangZhuang HaowenDong XinOuyang YulinLiu XinZhang ZhongzhengWang MengyuanChen JinhongTeng XinmengWang WeiLi ChunWang Junyan