ArticleArteriosclerosis, thrombosis, and vascular biology2012
p62 binding to protein kinase C ζ regulates tumor necrosis factor α-induced apoptotic pathway in endothelial cells.
Article in Arteriosclerosis, thrombosis, and vascular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- p62 Binding to Protein Kinase C Regulates HIV-1 gp120 V3 Loop Induced Microglial Inflammation.Inflammation · 2025Article
- p62/SQSTM1 in cancer: phenomena, mechanisms, and regulation in DNA damage repair.Cancer metastasis reviews · 2025Review
- Polyphenol-Based Prevention and Treatment of Cancer Through Epigenetic and Combinatorial Mechanisms.Nutrients · 2025Review
- Diesel exhaust particles induce human umbilical vein endothelial cells apoptosis by accumulation of autophagosomes and caspase-8 activation.Scientific reports · 2022Article
- PKC-ζ Aggravates Doxorubicin-Induced Cardiotoxicity by Inhibiting Wnt/β-Catenin Signaling.Frontiers in pharmacology · 2022Article
- PKC and PKN in heart disease.Journal of molecular and cellular cardiology · 2019Review
- Autophagic Regulation of p62 is Critical for Cancer Therapy.International journal of molecular sciences · 2018Review
- Flow signaling and atherosclerosis.Cellular and molecular life sciences : CMLS · 2017Review
- Target acquired: Selective autophagy in cardiometabolic disease.Science signaling · 2017Review
- IRS-1 Functions as a Molecular Scaffold to Coordinate IGF-I/IGFBP-2 Signaling During Osteoblast Differentiation.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2016Article
- Hyperglycemia stimulates p62/PKCζ interaction, which mediates NF-κB activation, increased Nox4 expression, and inflammatory cytokine activation in vascular smooth muscle.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- The activation of the atypical PKC zeta in light-induced retinal degeneration and its involvement in L-DNase II control.Journal of cellular and molecular medicine · 2015Article
- The Novel PKCθ from Benchtop to Clinic.Journal of immunology research · 2015Review
- Novel mechanisms of endothelial mechanotransduction.Arteriosclerosis, thrombosis, and vascular biology · 2014Review
- Acetylation of cyclophilin A is required for its secretion and vascular cell activation.Cardiovascular research · 2014Article
- Bcl-2-dependent upregulation of autophagy by sequestosome 1/p62 in vitro.Acta pharmacologica Sinica · 2013Article
- Regulation of cytochrome P450 2e1 expression by ethanol: role of oxidative stress-mediated pkc/jnk/sp1 pathway.Cell death & disease · 2013Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
objectiveProtein kinase C (PKC) ζ is a key pathological mediator of endothelial cell apoptosis. p62 is a scaffold protein that regulates several cell signaling pathways by binding to target proteins. Because PKCζ and p62 contain Phox/Bem1p (PB1) modules that mediate protein-protein interactions, we hypothesized that an interaction between p62 and PKCζ is required for tumor necrosis factor α-induced PKCζ signaling in endothelial cells. METHODS AND
resultsIn human umbilical vein endothelial cell, tumor necrosis factor α (10 ng/mL) enhanced the interaction between p62 and PKCζ. Transfection with p62 small interfering RNA reduced the activation of both PKCζ and its downstream targets JNK and caspase 3, suggesting that p62 is necessary for PKCζ signaling. Overexpression of only the PB1 domain of p62 inhibited p62-PKCζ interaction, showing that binding of these 2 proteins is mediated by their PB1 domains. Furthermore, overexpression of the p62 PB1 domain suppressed tumor necrosis factor α-induced PKCζ activation and subsequent activation of JNK and caspase 3. Finally, transfection of either p62 small interfering RNA or the PB1 domain of p62 inhibited human umbilical vein endothelial cell apoptosis.
conclusionsOur results suggest a novel function of p62 that regulates the activity of PKCζ by binding to PKCζ, thereby activating the PKCζ-JNK-caspase 3 apoptotic pathway in endothelial cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.