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Journal articles on the topic 'BAG3 protein'

Author: Grafiati

Published: 10 March 2023

Last updated: 31 July 2025

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1

Qu, Hui-Qi, Ju-Fang Wang, Alexandre Rosa-Campos, Hakon Hakonarson, and Arthur M. Feldman. "The Role of BAG3 Protein Interactions in Cardiomyopathies." International Journal of Molecular Sciences 25, no. 20 (2024): 11308. http://dx.doi.org/10.3390/ijms252011308.

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Bcl-2-associated athanogene 3 (BAG3) plays an important function in cellular protein quality control (PQC) maintaining proteome stability. Mutations in the BAG3 gene result in cardiomyopathies. Due to its roles in cardiomyopathies and the complexity of BAG3–protein interactions, it is important to understand these protein interactions given the importance of the multifunctional cochaperone BAG3 in cardiomyocytes, using an in vitro cardiomyocyte model. The experimental assay was conducted using high pressure liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) in the human AC16

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Kögel, Donat, Benedikt Linder, Andreas Brunschweiger, Silvia Chines, and Christian Behl. "At the Crossroads of Apoptosis and Autophagy: Multiple Roles of the Co-Chaperone BAG3 in Stress and Therapy Resistance of Cancer." Cells 9, no. 3 (2020): 574. http://dx.doi.org/10.3390/cells9030574.

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BAG3, a multifunctional HSP70 co-chaperone and anti-apoptotic protein that interacts with the ATPase domain of HSP70 through its C-terminal BAG domain plays a key physiological role in cellular proteostasis. The HSP70/BAG3 complex determines the levels of a large number of selective client proteins by regulating their turnover via the two major protein degradation pathways, i.e. proteasomal degradation and macroautophagy. On the one hand, BAG3 competes with BAG1 for binding to HSP70, thereby preventing the proteasomal degradation of its client proteins. By functionally interacting with HSP70 a

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3

Kokot, Thomas, Johannes P. Zimmermann, Yamini Chand, et al. "Identification of phosphatases that dephosphorylate the co-chaperone BAG3." Life Science Alliance 8, no. 2 (2024): e202402734. http://dx.doi.org/10.26508/lsa.202402734.

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The co-chaperone BAG3 plays critical roles in maintaining cellular proteostasis. It associates with 14-3-3 proteins during the trafficking of aggregation-prone proteins and facilitates their degradation through chaperone-assisted selective autophagy in cooperation with small heat shock proteins. Although reversible phosphorylation regulates BAG3 function, the involved phosphatases remain unknown. Here, we used affinity purification mass spectrometry to identify phosphatases that target BAG3. Of the hits, we evaluated the involvement of protein phosphatase-1 (PP1) using chemical inhibitors and

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Hiebel, Christof, Elisabeth Stürner, Meike Hoffmeister, et al. "BAG3 Proteomic Signature under Proteostasis Stress." Cells 9, no. 11 (2020): 2416. http://dx.doi.org/10.3390/cells9112416.

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The multifunctional HSP70 co-chaperone BAG3 (BCL-2-associated athanogene 3) represents a key player in the quality control of the cellular proteostasis network. In response to stress, BAG3 specifically targets aggregation-prone proteins to the perinuclear aggresome and promotes their degradation via BAG3-mediated selective macroautophagy. To adapt cellular homeostasis to stress, BAG3 modulates and functions in various cellular processes and signaling pathways. Noteworthy, dysfunction and deregulation of BAG3 and its pathway are pathophysiologically linked to myopathies, cancer, and neurodegene

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Zamotina, Maria A., Lidia K. Muranova, Artur I. Zabolotskii, Pyotr A. Tyurin-Kuzmin, Konstantin Yu Kulebyakin, and Nikolai B. Gusev. "Universal Adapter Protein Bag3 and Small Heat Shock Proteins." Biochemistry (Moscow) 89, no. 9 (2024): 1535–45. http://dx.doi.org/10.1134/s0006297924090013.

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Abstract Bag3 (Bcl-2-associated athanogene 3) protein contains a number of functional domains and interacts with a wide range of different partner proteins, including small heat shock proteins (sHsps) and heat shock protein Hsp70. The ternary Bag3–sHsp–and Hsp70 complex binds denatured proteins and transports them to phagosomes, thus playing a key role in the chaperone-assisted selective autophagy (CASA). This complex also participates in the control of formation and disassembly of stress granules (granulostasis) and cytoskeleton regulation. As Bag3 and sHsps participate in multiple cellular p

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6

Myers, Valerie D., Joseph M. McClung, JuFang Wang, et al. "The Multifunctional Protein BAG3." JACC: Basic to Translational Science 3, no. 1 (2018): 122–31. http://dx.doi.org/10.1016/j.jacbts.2017.09.009.

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7

Han, Ziying, Michael Schwoerer, Philip Hicks, et al. "Host Protein BAG3 is a Negative Regulator of Lassa VLP Egress." Diseases 6, no. 3 (2018): 64. http://dx.doi.org/10.3390/diseases6030064.

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Lassa fever virus (LFV) belongs to the Arenaviridae family and can cause acute hemorrhagic fever in humans. The LFV Z protein plays a central role in virion assembly and egress, such that independent expression of LFV Z leads to the production of virus-like particles (VLPs) that mimic egress of infectious virus. LFV Z contains both PTAP and PPPY L-domain motifs that are known to recruit host proteins that are important for mediating efficient virus egress and spread. The viral PPPY motif is known to interact with specific host WW-domain bearing proteins. Here we identified host WW-domain beari

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Rauch, Jennifer N., and Jason E. Gestwicki. "Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro." Journal of Biological Chemistry 289, no. 3 (2013): 1402–14. http://dx.doi.org/10.1074/jbc.m113.521997.

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Proteins with Bcl2-associated anthanogene (BAG) domains act as nucleotide exchange factors (NEFs) for the molecular chaperone heat shock protein 70 (Hsp70). There are six BAG family NEFs in humans, and each is thought to link Hsp70 to a distinct cellular pathway. However, little is known about how the NEFs compete for binding to Hsp70 or how they might differentially shape its biochemical activities. Toward these questions, we measured the binding of human Hsp72 (HSPA1A) to BAG1, BAG2, BAG3, and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 > BAG1 &g

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9

Carra, Serena, Samuel J. Seguin, Herman Lambert, and Jacques Landry. "HspB8 Chaperone Activity toward Poly(Q)-containing Proteins Depends on Its Association with Bag3, a Stimulator of Macroautophagy." Journal of Biological Chemistry 283, no. 3 (2007): 1437–44. http://dx.doi.org/10.1074/jbc.m706304200.

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Mutations in HspB8, a member of the B group of heat shock proteins (Hsp), have been associated with human neuromuscular disorders. However, the exact function of HspB8 is not yet clear. We previously demonstrated that overexpression of HspB8 in cultured cells prevents the accumulation of aggregation-prone proteins such as the polyglutamine protein Htt43Q. Here we report that HspB8 forms a stable complex with Bag3 in cells and that the formation of this complex is essential for the activity of HspB8. Bag3 overexpression resulted in the accelerated degradation of Htt43Q, whereas Bag3 knockdown p

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Fuchs, Margit, Dominic J. Poirier, Samuel J. Seguin, et al. "Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction." Biochemical Journal 425, no. 1 (2009): 245–57. http://dx.doi.org/10.1042/bj20090907.

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The molecular chaperone HspB8 [Hsp (heat-shock protein) B8] is member of the B-group of Hsps. These proteins bind to unfolded or misfolded proteins and protect them from aggregation. HspB8 has been reported to form a stable molecular complex with the chaperone cohort protein Bag3 (Bcl-2-associated athanogene 3). In the present study we identify the binding regions in HspB8 and Bag3 crucial for their interaction. We present evidence that HspB8 binds to Bag3 through the hydrophobic groove formed by its strands β4 and β8, a region previously known to be responsible for the formation and stability

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11

Fang, Xi, Julius Bogomolovas, Paul Shichao Zhou, et al. "P209L mutation in Bag3 does not cause cardiomyopathy in mice." American Journal of Physiology-Heart and Circulatory Physiology 316, no. 2 (2019): H392—H399. http://dx.doi.org/10.1152/ajpheart.00714.2018.

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Bcl-2-associated athanogene 3 (BAG3) is a cochaperone protein and a central player of the cellular protein quality control system. BAG3 is prominently expressed in the heart and plays an essential role in cardiac protein homeostasis by interacting with chaperone heat shock proteins (HSPs) in large, functionally distinct multichaperone complexes. The BAG3 mutation of proline 209 to leucine (P209L), which resides in a critical region that mediates the direct interaction between BAG3 and small HSPs (sHSPs), is associated with cardiomyopathy in humans. However, the mechanism by which the BAG3 P209

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12

Kyratsous, Christos A., and Saul J. Silverstein. "BAG3, a Host Cochaperone, Facilitates Varicella-Zoster Virus Replication." Journal of Virology 81, no. 14 (2007): 7491–503. http://dx.doi.org/10.1128/jvi.00442-07.

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ABSTRACT Varicella-zoster virus (VZV) establishes a lifelong latent infection in the dorsal root ganglia of the host. During latency, a subset of virus-encoded regulatory proteins is detected; however, they are excluded from the nucleus. ORF29p, a single-stranded DNA binding protein, is one of these latency-associated proteins. We searched for cell proteins that interact with ORF29p and identified BAG3. BAG3, Hsp70/Hsc70, and Hsp90 colocalize with ORF29p in nuclear transcription/replication factories during lytic replication of VZV. Pharmacological intercession of Hsp90 activity with ansamycin

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13

Brenner, Caitlyn M., Muaaz Choudhary, Michael G. McCormick, et al. "BAG3: Nature’s Quintessential Multi-Functional Protein Functions as a Ubiquitous Intra-Cellular Glue." Cells 12, no. 6 (2023): 937. http://dx.doi.org/10.3390/cells12060937.

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BAG3 is a 575 amino acid protein that is found throughout the animal kingdom and homologs have been identified in plants. The protein is expressed ubiquitously but is most prominent in cardiac muscle, skeletal muscle, the brain and in many cancers. We describe BAG3 as a quintessential multi-functional protein. It supports autophagy of both misfolded proteins and damaged organelles, inhibits apoptosis, maintains the homeostasis of the mitochondria, and facilitates excitation contraction coupling through the L-type calcium channel and the beta-adrenergic receptor. High levels of BAG3 are associa

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Staibano, Stefania, Massimo Mascolo, Maria Di Benedetto, et al. "BAG3 protein delocalisation in prostate carcinoma." Tumor Biology 31, no. 5 (2010): 461–69. http://dx.doi.org/10.1007/s13277-010-0055-3.

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15

Lyu, Chuang, Wei-Dong Li, Shu-Wen Wang, et al. "Host BAG3 Is Degraded by Pseudorabies Virus pUL56 C-Terminal 181L-185L and Plays a Negative Regulation Role during Viral Lytic Infection." International Journal of Molecular Sciences 21, no. 9 (2020): 3148. http://dx.doi.org/10.3390/ijms21093148.

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Bcl2-associated athanogene (BAG) 3, which is a chaperone-mediated selective autophagy protein, plays a pivotal role in modulating the life cycle of a wide variety of viruses. Both positive and negative modulations of viruses by BAG3 were reported. However, the effects of BAG3 on pseudorabies virus (PRV) remain unknown. To investigate whether BAG3 could modulate the PRV life cycle during a lytic infection, we first identified PRV protein UL56 (pUL56) as a novel BAG3 interactor by co-immunoprecipitation and co-localization analyses. The overexpression of pUL56 induced a significant degradation o

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Basile, Anna, Nune Darbinian, Rafal Kaminski, et al. "Evidence for modulation of BAG3 by polyomavirus JC early protein." Journal of General Virology 90, no. 7 (2009): 1629–40. http://dx.doi.org/10.1099/vir.0.008722-0.

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Polyomavirus JC (JCV) infects oligodendrocytes and astrocytes in the brain and is the cause of the demyelinating disease progressive multifocal leukoencephalopathy (PML). In cell culture, JCV infection is characterized by severe damage to cellular DNA, which begins early in infection, and a viral cytopathic effect, which is observed late in infection. Nevertheless, these JCV-infected cells show a low level of apoptosis, at both the early and late stages of infection. This suggests that there is conflicting interplay between viral anti-apoptotic pathways that seek to optimize virus production,

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McCollum, Andrea K., Giovanna Casagrande, and Elise C. Kohn. "Caught in the middle: the role of Bag3 in disease." Biochemical Journal 425, no. 1 (2009): e1-e3. http://dx.doi.org/10.1042/bj20091739.

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Bag3 is a Bag family co-chaperone that regulates the ATPase activity of Hsp70 (heat-shock protein 70) chaperones. Recent studies have demonstrated that Bag3 can initiate macroautophagy in co-operation with small heat-shock protein HspB8. In this issue of the Biochemical Journal, Fuchs and co-workers have discovered the IPV motif in Bag3 that is necessary for binding to HspB8. The authors have also identified HspB6 as a new binding partner for Bag3 and characterized further the binding of both HspB8 and HspB6 in Bag3-mediated clearance of aggregated polyglutamine-containing protein Htt43Q (hunt

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18

Chiappetta, Gennaro, Massimo Ammirante, Anna Basile, et al. "The Antiapoptotic Protein BAG3 Is Expressed in Thyroid Carcinomas and Modulates Apoptosis Mediated by Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand." Journal of Clinical Endocrinology & Metabolism 92, no. 3 (2007): 1159–63. http://dx.doi.org/10.1210/jc.2006-1712.

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Abstract Context: We previously showed that BAG3 protein, a member of the BAG (Bcl-2-associated athanogene) co-chaperone family, modulates apoptosis in human leukemias. The expression of BAG3 in other tumor types has not been extensively investigated so far. Objective: The objective of this study was to analyze BAG3 expression in thyroid neoplastic cells and investigate its influence in cell apoptotic response to TNF-related apoptosis-inducing ligand (TRAIL). Design, Setting, and Patients: We investigated BAG3 expression in human thyroid carcinoma cell lines, including NPA, and the effect of B

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19

Meriin, Anatoli B., Arjun Narayanan, Le Meng, et al. "Hsp70–Bag3 complex is a hub for proteotoxicity-induced signaling that controls protein aggregation." Proceedings of the National Academy of Sciences 115, no. 30 (2018): E7043—E7052. http://dx.doi.org/10.1073/pnas.1803130115.

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Protein abnormalities in cells are the cause of major pathologies, and a number of adaptive responses have evolved to relieve the toxicity of misfolded polypeptides. To trigger these responses, cells must detect the buildup of aberrant proteins which often associate with proteasome failure, but the sensing mechanism is poorly understood. Here we demonstrate that this mechanism involves the heat shock protein 70–Bcl-2–associated athanogene 3 (Hsp70–Bag3) complex, which upon proteasome suppression responds to the accumulation of defective ribosomal products, preferentially recognizing the stalle

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Wang, Yingying, and Yongjie Tian. "miR-206 Inhibits Cell Proliferation, Migration, and Invasion by Targeting BAG3 in Human Cervical Cancer." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 26, no. 6 (2018): 923–31. http://dx.doi.org/10.3727/096504017x15143731031009.

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miR-206 and Bcl-2-associated athanogene 3 (BAG3) have been suggested as important regulators in various cancer types. However, the biological role of miR-206 and BAG3 in cervical cancer (CC) remains unclear. We investigated the expressions and mechanisms of miR-206 and BAG3 in CC using in vitro and in vivo assays. In the present study, miR-206 expression was expressed at a lower level in CC tissues and cells than adjacent normal tissues and NEECs. By contrast, BAG3 mRNA and protein were expressed at higher levels in CC tissues and cells. Furthermore, miR-206 overexpression repressed cell proli

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De Marco, Margot, Raffaella D’Auria, Alessandra Rosati, et al. "BAG3 Protein in Advanced-Stage Heart Failure." JACC: Heart Failure 2, no. 6 (2014): 673–75. http://dx.doi.org/10.1016/j.jchf.2014.05.012.

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Marzullo, Liberato, Maria Caterina Turco, and Margot De Marco. "The multiple activities of BAG3 protein: Mechanisms." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 8 (2020): 129628. http://dx.doi.org/10.1016/j.bbagen.2020.129628.

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Rocchi, Angela, Hassen S. Wollebo, and Kamel Khalili. "Protein Quality Control in Glioblastoma: A Review of the Current Literature with New Perspectives on Therapeutic Targets." International Journal of Molecular Sciences 23, no. 17 (2022): 9734. http://dx.doi.org/10.3390/ijms23179734.

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Protein quality control allows eukaryotes to maintain proteostasis under the stress of constantly changing conditions. In this review, we discuss the current literature on PQC, highlighting flaws that must exist for malignancy to occur. At the nidus of PQC, the expression of BAG1-6 reflects the cell environment; each isoform directs proteins toward different, parallel branches of the quality control cascade. The sum of these branches creates a net shift toward either homeostasis or apoptosis. With an established role in ALP, Bag3 is necessary for cell survival in stress conditions including th

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Liu, Xia, Toru Yamashita, Jingwei Shang, et al. "Molecular switching from ubiquitin-proteasome to autophagy pathways in mice stroke model." Journal of Cerebral Blood Flow & Metabolism 40, no. 1 (2018): 214–24. http://dx.doi.org/10.1177/0271678x18810617.

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The ubiquitin-proteasome system (UPS) and autophagy are two major pathways to degrade misfolded proteins that accumulate under pathological conditions. When UPS is overloaded, the degeneration pathway may switch to autophagy to remove excessive misfolded proteins. However, it is still unclear whether and how this switch occurs during cerebral ischemia. In the present study, transient middle cerebral artery occlusion (tMCAO) resulted in accelerated ubiquitin-positive protein aggregation from 0.5 h of reperfusion in mice brain after 10, 30 or 60 min of tMCAO. In contrast, significant reduction o

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Luthold, Carole, Herman Lambert, Solenn M. Guilbert, et al. "CDK1-Mediated Phosphorylation of BAG3 Promotes Mitotic Cell Shape Remodeling and the Molecular Assembly of Mitotic p62 Bodies." Cells 10, no. 10 (2021): 2638. http://dx.doi.org/10.3390/cells10102638.

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The cochaperone BCL2-associated athanogene 3 (BAG3), in complex with the heat shock protein HSPB8, facilitates mitotic rounding, spindle orientation, and proper abscission of daughter cells. BAG3 and HSPB8 mitotic functions implicate the sequestosome p62/SQSTM1, suggesting a role for protein quality control. However, the interplay between this chaperone-assisted pathway and the mitotic machinery is not known. Here, we show that BAG3 phosphorylation at the conserved T285 is regulated by CDK1 and activates its function in mitotic cell shape remodeling. BAG3 phosphorylation exhibited a high dynam

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De Marco, M., A. Falco, F. Reppucci, et al. "POS0624 BAG3 PROTEIN: A PROMISING NOVEL BIOMARKER OF FIBROSIS IN SYSTEMIC SCLEROSIS." Annals of the Rheumatic Diseases 82, Suppl 1 (2023): 585.3–586. http://dx.doi.org/10.1136/annrheumdis-2023-eular.4071.

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BackgroundSystemic Sclerosis (SSc) is a rare autoimmune disease characterized by an abnormal remodelling of tissue matrix, leading to fibrosis of skin and internal organs. Despite progresses made in terms of knowledge of pathogenic mechanisms, no study has yet identified specific biomarkers useful for assessing disease evolution and response to therapies. Bcl2-associated athanogene 3 (BAG3) protein is a member of a family of co-chaperones that interact with the ATPase domain of the heat shock protein (Hsp) 70 through their BAG domain. BAG3 is constitutively present in a few normal cell types a

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Sarparanta, Jaakko, Per Harald Jonson, Sabita Kawan, and Bjarne Udd. "Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results." International Journal of Molecular Sciences 21, no. 4 (2020): 1409. http://dx.doi.org/10.3390/ijms21041409.

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Skeletal muscle and the nervous system depend on efficient protein quality control, and they express chaperones and cochaperones at high levels to maintain protein homeostasis. Mutations in many of these proteins cause neuromuscular diseases, myopathies, and hereditary motor and sensorimotor neuropathies. In this review, we cover mutations in DNAJB6, DNAJB2, αB-crystallin (CRYAB, HSPB5), HSPB1, HSPB3, HSPB8, and BAG3, and discuss the molecular mechanisms by which they cause neuromuscular disease. In addition, previously unpublished results are presented, showing downstream effects of BAG3 p.P2

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Lee, Jae Chang, Sung Ae Koh, Kyung Hee Lee, and Jae-Ryong Kim. "BAG3 contributes to HGF-mediated cell proliferation, migration, and invasion via the Egr1 pathway in gastric cancer." Tumori Journal 105, no. 1 (2018): 63–75. http://dx.doi.org/10.1177/0300891618811274.

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Introduction: Bcl2-associated athanogene 3 (BAG3) is elevated in several types of cancers. However, the role of BAG3 in progression of gastric cancer is unknown. Therefore, the present study aims to find out the role of BAG3 in hepatocyte growth factor (HGF)–mediated tumor progression and the molecular mechanisms by which HGF regulates BAG3 expression. Methods: BAG3 mRNA and protein were measured using reverse transcription polymerase chain reaction and Western blot in the 2 human gastric cancer cell lines, NUGC3 and MKN28, treated with or without HGF. The effects of BAG3 knockdown on cell pro

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Ruggiero, Dafne, Stefania Terracciano, Gianluigi Lauro, et al. "Structural Refinement of 2,4-Thiazolidinedione Derivatives as New Anticancer Agents Able to Modulate the BAG3 Protein." Molecules 27, no. 3 (2022): 665. http://dx.doi.org/10.3390/molecules27030665.

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The multidomain BAG3 protein is a member of the BAG (Bcl-2-associated athanogene) family of co-chaperones, involved in a wide range of protein–protein interactions crucial for many key cellular pathways, including autophagy, cytoskeletal dynamics, and apoptosis. Basal expression of BAG3 is elevated in several tumor cell lines, where it promotes cell survival signaling and apoptosis resistance through the interaction with many protein partners. In addition, its role as a key player of several hallmarks of cancer, such as metastasis, angiogenesis, autophagy activation, and apoptosis inhibition,

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Luthold, Carole, Alice-Anaïs Varlet, Herman Lambert, François Bordeleau, and Josée N. Lavoie. "Chaperone-Assisted Mitotic Actin Remodeling by BAG3 and HSPB8 Involves the Deacetylase HDAC6 and Its Substrate Cortactin." International Journal of Molecular Sciences 22, no. 1 (2020): 142. http://dx.doi.org/10.3390/ijms22010142.

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The fidelity of actin dynamics relies on protein quality control, but the underlying molecular mechanisms are poorly defined. During mitosis, the cochaperone BCL2-associated athanogene 3 (BAG3) modulates cell rounding, cortex stability, spindle orientation, and chromosome segregation. Mitotic BAG3 shows enhanced interactions with its preferred chaperone partner HSPB8, the autophagic adaptor p62/SQSTM1, and HDAC6, a deacetylase with cytoskeletal substrates. Here, we show that depletion of BAG3, HSPB8, or p62/SQSTM1 can recapitulate the same inhibition of mitotic cell rounding. Moreover, depleti

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Ruggiero, Dafne, Emis Ingenito, Eleonora Boccia, et al. "Identification of a New Promising BAG3 Modulator Featuring the Imidazopyridine Scaffold." Molecules 29, no. 21 (2024): 5051. http://dx.doi.org/10.3390/molecules29215051.

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The antiapoptotic BAG3 protein plays a crucial role in cellular proteostasis and it is involved in several signalling pathways governing cell proliferation and survival. Owing to its multimodular structure, it possesses an extensive interactome including the molecular chaperone HSP70 and other specific cellular partners, which make it an eminent factor in several pathologies, particularly in cancer. Despite its potential as a therapeutic target, very few BAG3 modulators have been disclosed so far. Here we describe the identification of a promising BAG3 modulator able to bind the BAG domain of

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Franceschelli, Silvia, Anna Paola Bruno, Michela Festa, et al. "BAG3 Protein Is Involved in Endothelial Cell Response to Phenethyl Isothiocyanate." Oxidative Medicine and Cellular Longevity 2018 (May 31, 2018): 1–12. http://dx.doi.org/10.1155/2018/5967890.

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Phenethyl isothiocyanate (PEITC), a cruciferous vegetable-derived compound, is a versatile cancer chemopreventive agent that displays the ability to inhibit tumor growth during initiation, promotion, and progression phases in several animal models of carcinogenesis. In this report, we dissect the cellular events induced by noncytotoxic concentrations of PEITC in human umbilical vein endothelial cells (HUVECs). In the early phase, PEITC treatment elicited cells’ morphological changes that comprise reduction in cell volume and modification of actin organization concomitantly with a rapid activat

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Rosati, A., V. Graziano, V. De Laurenzi, M. Pascale, and M. C. Turco. "BAG3: a multifaceted protein that regulates major cell pathways." Cell Death & Disease 2, no. 4 (2011): e141-e141. http://dx.doi.org/10.1038/cddis.2011.24.

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Bruno, Anna Paola, Michela Festa, Fabrizio Dal Piaz, et al. "Identification of a synaptosome- associated form of BAG3 protein." Cell Cycle 7, no. 19 (2008): 3104–5. http://dx.doi.org/10.4161/cc.7.19.6774.

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Romano, M. F., M. Festa, G. Pagliuca, et al. "BAG3 protein controls B-chronic lymphocytic leukaemia cell apoptosis." Cell Death & Differentiation 10, no. 3 (2003): 383–85. http://dx.doi.org/10.1038/sj.cdd.4401167.

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Gout, E., M. Gutkowska, S. Takayama, J. C. Reed, and J. Chroboczek. "Co-chaperone BAG3 and adenovirus penton base protein partnership." Journal of Cellular Biochemistry 111, no. 3 (2010): 699–708. http://dx.doi.org/10.1002/jcb.22756.

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Esposito, Veronica, Carlo Baldi, Pio Zeppa, et al. "BAG3 Protein Is Over-Expressed in Endometrioid Endometrial Adenocarcinomas." Journal of Cellular Physiology 232, no. 2 (2016): 309–11. http://dx.doi.org/10.1002/jcp.25489.

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Liu, Yubo, Renjie Xu, Jinfu Xu, Tiantian Wu, and Xiangxin Zhang. "BAG3 regulates bone marrow mesenchymal stem cell proliferation by targeting INTS7." PeerJ 11 (August 9, 2023): e15828. http://dx.doi.org/10.7717/peerj.15828.

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Background BAG3 is an essential regulator of cell survival and has been investigated in the context of heart disease and cancer. Our previous study used immunoprecipitation-liquid chromatography-tandem mass spectrometry to show that BAG3 might directly interact with INTS7 and regulate bone marrow mesenchymal stem cell (BMMSCs) proliferation. However, whether BAG3 bound INTS7 directly and how it regulated BMMSCs expansion was unclear. Methods BAG3 expression was detected by quantitative real-time PCR in BMMSCs after siRNA-mediated BAG3 knockdown. BMMSC proliferation was determined using the CCK

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Zhang, Jiankai, Zhangyou He, Wenjian Xiao, et al. "Overexpression of BAG3 Attenuates Hypoxia-Induced Cardiomyocyte Apoptosis by Inducing Autophagy." Cellular Physiology and Biochemistry 39, no. 2 (2016): 491–500. http://dx.doi.org/10.1159/000445641.

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Background: Hypoxia is a well-known factor in the promotion of apoptosis, which contributes to the development of numerous cardiac diseases, such as heart failure and myocardial infarction. Inhibiting apoptosis is an important therapeutic strategy for the treatment of related heart diseases caused by ischemia/hypoxic injury. Previous studies have demonstrated that BAG3 plays an important role in cardiomyocyte apoptosis and survival. However, the role of BAG3 in hypoxia-induced cardiomyocyte apoptosis remains to be clarified. Here, we demonstrate that BAG3 is induced by hypoxia stimuli in cultu

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De Luca, Pietro, Francesco Antonio Salzano, Angelo Camaioni, et al. "BAG3 Positivity as Prognostic Marker in Head and Neck Squamous Cell Carcinoma." Cancers 17, no. 11 (2025): 1843. https://doi.org/10.3390/cancers17111843.

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Background: Head and neck squamous cell carcinoma (HNSCC) exhibit considerable heterogeneity, complicating the prediction of disease progression and treatment response. Consequently, researchers are actively investigating reliable biomarkers to forecast disease trajectories and inform therapeutic decisions. This study examines the role of BAG3, a protein involved in cell survival and stress response, as a potential predictive marker in HNSCC. The objective is to analyze BAG3 expression across various HNSCC types and correlate it with disease-free survival (DFS), aiming to elucidate the influen

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Mukhtar, Idris. "Modelling and docking analysis of a tumor target protein BAG3." Bioinformation 16, no. 4 (2020): 351–58. http://dx.doi.org/10.6026/97320630016351.

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Carrizzo, Albino, Antonio Damato, Mariateresa Ambrosio, et al. "The prosurvival protein BAG3: a new participant in vascular homeostasis." Cell Death & Disease 7, no. 10 (2016): e2431-e2431. http://dx.doi.org/10.1038/cddis.2016.321.

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Brooks, David, Fawwaz Naeem, Marta Stetsiv, et al. "Drosophila NUAK functions with Starvin/BAG3 in autophagic protein turnover." PLOS Genetics 16, no. 4 (2020): e1008700. http://dx.doi.org/10.1371/journal.pgen.1008700.

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Franco, Renato, Giosuè Scognamiglio, Vincenzo Salerno, et al. "Expression of the Anti-Apoptotic Protein BAG3 in Human Melanomas." Journal of Investigative Dermatology 132, no. 1 (2012): 252–54. http://dx.doi.org/10.1038/jid.2011.257.

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Bruno, Anna Paola, Francesca Isabella De Simone, Vittoria Iorio, et al. "HIV-1 Tat protein induces glial cell autophagy through enhancement of BAG3 protein levels." Cell Cycle 13, no. 23 (2014): 3640–44. http://dx.doi.org/10.4161/15384101.2014.952959.

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Ijabi, Roghayeh, Parisa Roozehdar, Reza Afrisham та ін. "Association of GRP78, HIF-1α and BAG3 Expression with the Severity of Chronic Lymphocytic Leukemia". Anti-Cancer Agents in Medicinal Chemistry 20, № 4 (2020): 429–36. http://dx.doi.org/10.2174/1871520619666191211101357.

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Introduction: Parallel with the progression of Chronic Lymphocytic Leukemia (CLL), the levels of 78KDa Glucose-Regulated Protein (GRP78) and Hypoxia-Inducible Factor 1 alpha (HIF-1α) are increased as they may activate the induction of anti-apoptotic proteins such as BCL2 Associated Athanogene 3 (BAG3). Previous studies have indicated that there is a positive correlation among GRP78, HIF-1α and BAG3. Objective: This study aimed to evaluate the effect of metabolic factors involved in invasive CLL on apoptotic factors. Methods: A case-control study was conducted on 77 patients diagnosed with CLL

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Zhang, Liang, Zhi-Ping Zhang, Xian-En Zhang, Fu-Sen Lin, and Feng Ge. "Quantitative Proteomics Analysis Reveals BAG3 as a Potential Target To Suppress Severe Acute Respiratory Syndrome Coronavirus Replication." Journal of Virology 84, no. 12 (2010): 6050–59. http://dx.doi.org/10.1128/jvi.00213-10.

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ABSTRACT The discovery of a novel coronavirus (CoV) as the causative agent of severe acute respiratory syndrome (SARS) has highlighted the need for a better understanding of CoV replication. The replication of SARS-CoV is highly dependent on host cell factors. However, relatively little is known about the cellular proteome changes that occur during SARS-CoV replication. Recently, we developed a cell line expressing a SARS-CoV subgenomic replicon and used it to screen inhibitors of SARS-CoV replication. To identify host proteins important for SARS-CoV RNA replication, the protein profiles of th

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Lövenich, Lukas, Georg Dreissen, Christina Hoffmann, et al. "Strain-induced mechanoresponse depends on cell contractility and BAG3-mediated autophagy." Molecular Biology of the Cell 32, no. 20 (2021): ar9. http://dx.doi.org/10.1091/mbc.e21-05-0254.

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The mechanosensitivity of mammalian cells and protein degradation via autophagy are two essential regulatory cell mechanisms. The close interplay between these two mechanisms is characterized in detail and proves a strong bidirectional cross-talk between BAG3-mediated chaperone-assisted selective autophagy and mechanosensitivity.

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Romano, Maria Fiammetta, Michelina Festa, Antonello Petrella, et al. "BAG3 Protein Regulates Cell Survival in Childhood Acute Lymphoblastic Leukemia Cells." Cancer Biology & Therapy 2, no. 5 (2003): 508–10. http://dx.doi.org/10.4161/cbt.2.5.524.

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Basile, Anna, Morena d'Avenia, Alessandra Rosati, et al. "Novel Targets for Apoptosis Modulation: BAG3 Protein and Other Co- Chaperones." Recent Patents on Endocrine, Metabolic & Immune Drug Discovery 3, no. 2 (2009): 80–86. http://dx.doi.org/10.2174/187221409788452318.

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