SIRT4 Blocking Peptide
- Known as:
- SIRT4 Blocking Peptide
- Catalog number:
- 3224BP-50
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Biovis
- Gene target:
- SIRT4 Blocking Peptide
Related genes to: SIRT4 Blocking Peptide
- Gene:
- SIRT4 NIH gene
- Name:
- sirtuin 4
- Previous symbol:
- -
- Synonyms:
- SIR2L4
- Chromosome:
- 12q24.31
- Locus Type:
- gene with protein product
- Date approved:
- 2001-03-20
- Date modifiied:
- 2014-11-19
Related products to: SIRT4 Blocking Peptide
Related articles to: SIRT4 Blocking Peptide
- Circadian rhythm (CR) dysregulation is increasingly recognized as a contributor to gastric cancer (GC) development, yet the biological and immunological consequences of CR-related alterations remain unclear. In this study, integrative transcriptomic analyses identified 147 CR-related differentially expressed genes in GC. Functional enrichment revealed significant involvement in circadian processes, cytokine activity, and immune-related signaling pathways. By applying three complementary machine learning algorithms, five robust hub genes (INHBA, DEPTOR, PDCD4, SELENBP1, and SIRT4) were identified. Among them, INHBA and SELENBP1 showed significant prognostic value, and SELENBP1 expression was strongly associated with immune infiltration patterns. Experimental validation confirmed that SELENBP1 overexpression suppressed GC cell proliferation, migration, and inflammatory cytokine secretion, and displayed a clear 24-h circadian oscillation. Collectively, these findings highlight key CR-related molecular alterations in GC and identify SELENBP1 as a promising diagnostic biomarker with potential immunoregulatory and circadian-dependent functional relevance. - Source: PubMed
Publication date: 2026/06/13
Li FuxinZhang ZequnXie ZhihuiDong YunhongLan Yongting - Heart failure with preserved ejection fraction (HFpEF) is a complex cardiovascular disorder characterized by diastolic dysfunction, metabolic dysregulation and limited therapeutic options. Post-translational modifications (PTMs) are key regulators of cardiac metabolism, but the role of butyrylation in HFpEF pathogenesis remains unclear. This study explored the mechanistic role of butyrylation in myocardial energy metabolism of HFpEF and evaluate the therapeutic potential of ginsenoside Rb3 (G-Rb3). A "two-hit" (high-fat diet + L-NAME) mouse model and a phenylephrine (PE)-induced hypertrophic and metabolically stressed cellular model were established. Myocardial PTM screening identified butyrylation as the target for proteomic analysis. G-Rb3 efficacy was evaluated in vivo and in vitro, with mechanistic studies involving Sirtuin 4 (SIRT4) inhibitor and overexpression experiments to confirm its regulatory role. Male mice model displayed earlier and more severe HFpEF phenotypes than females, thus justifying their use in mechanistic studies. Butyrylome analysis revealed hyperbutyrylation of succinate-CoA ligase subunit alpha (SUCLG1) at K90, which impaired its enzymatic function in tricarboxylic acid (TCA) cycle, resulting in reduced succinate and ATP production. SIRT4 was identified as a key regulator of SUCLG1 debutylation, with downregulated SIRT4 expression leading to SUCLG1 hyperbutyrylation. G-Rb3 directly bound SIRT4, reversing SUCLG1 hyperbutyrylation, restoring TCA cycle flux and ATP levels, improving diastolic dysfunction and metabolic abnormalities. These effects were nullified by SIRT4 inhibition, confirming SIRT4 as G-Rb3's critical target. Our study reveals SUCLG1 butyrylation as a novel metabolic regulator in the pathogenesis of HFpEF, orchestrated by SIRT4. G-Rb3, a SIRT4-interacting regulator, rescues this axis, offering a mechanism-based therapy for HFpEF. - Source: PubMed
Publication date: 2026/04/14
Yu XiaohanGuo YingfeiLiu ShenfanLi ShiqiLiu YuntaoJin LiliWang YuanpingLiu ZhongqiuCheng YuanyuanWang Dawei - Tumor cells adapt to therapeutic stress by preserving mitochondrial integrity through mitophagy, but excessive mitophagy can overwhelm this adaptative mechanism and precipitate mitochondrial collapse. Here, we demonstrate that 1,25-dihydroxyvitamin D3 (1,25D3) reduces glioblastoma resistance to the standard chemotherapeutic temozolomide by driving mitophagic overload and mitochondrial dysfunction. We identified mitochondrial sirtuin SIRT4 as a key downstream effector of mitochondrial metabolism and quality control triggered by 1,25D3-induced mitochondrial stress. Pharmacological levels of 1,25D3 activate mitophagy by transcriptionally upregulating SIRT4 through vitamin D receptor (VDR) signaling. SIRT4, which is frequently downregulated in glioblastoma, suppresses glioblastoma glutamine metabolism by inhibiting glutamate dehydrogenase activity and limiting α-ketoglutarate availability, thereby integrating metabolic stress with enhanced mitophagy. This VDR-SIRT4 axis shifts mitophagy from a cytoprotective process to a lethal pathway, selectively sensitizing tumor cells while sparing normal astrocytes and brain tissue. By exploiting mitochondrial quality control as a metabolic vulnerability, 1,25D3 enhances chemotherapeutic efficacy and provides a translational rationale for repurposing 1,25D3 in resistant glioblastoma. - Source: PubMed
Publication date: 2026/03/06
Kiang Karrie MShen YixiongWong Yogesh K HChen BoLiao JunboMnahal AnzaTang WanjunZhu ZhiyuanCao ShuhanLo Carmen S CLee Sang JinGuo HongboZhang LiyangLeung Gilberto Ka-Kit - Malonyl-CoA decarboxylase (MCD) is an enzyme that controls malonyl-CoA levels and regulates fatty acid synthesis and oxidation. Although its physiological relevance in peripheral tissues is well known, the role of MCD in the central nervous system remains poorly understood. MCD is expressed in mitochondria, cytosol, and peroxisomes and may be regulated by PPAR-α, AMPK, and SIRT4 in tissues such as muscle, liver and kidney. In the brain, MCD expression varies during development and can respond to nutritional states. Inherited MCD deficiency (malonic aciduria) leads to the toxic accumulation of malonic acid and predominantly affects the central nervous system. The underlying mechanisms leading to brain damage in MCD patients remain unclear. Conversely, pharmacological modulation of MCD activity has been studied in obesity, diabetes, and ischemic injury, highlighting its therapeutic potential. There are still major gaps regarding MCD cellular distribution, regulatory pathways, and metabolic interaction with CPT1c (carnitine palmitoyltransferase 1c) in neural metabolism. A deeper understanding of the role of MCD in brain physiology and pathology may indicate novel therapeutic strategies targeting metabolic disorders that involve altered malonyl-CoA dynamics. Here, we discuss the current knowns and unknowns regarding MCD physiology, regulation, and pathophysiology, emphasizing brain aspects. - Source: PubMed
Publication date: 2026/02/12
Fonseca-Teixeira MoniqueBrito Elaine SilvaBeltrao-Valente ClaraFerreira Bruna KlippelSchuck Patricia FernandaFerreira Gustavo Costa - - Source: PubMed
Publication date: 2026/02/24
Chang ShutingZhang GuanzhaoLi LanlanLi HaiyingJin XiaodongWang YunshanLi Bo