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Littérature scientifique sur le sujet « BAG3 protein »

Auteur : Grafiati
Publié le 10 mars 2023

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Articles de revues sur le sujet "BAG3 protein"

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Myers, Valerie D., Joseph M. McClung, JuFang Wang, Farzaneh G. Tahrir, Manish K. Gupta, Jennifer Gordon, Christopher H. Kontos, Kamel Khalili, Joseph Y. Cheung et Arthur M. Feldman. « The Multifunctional Protein BAG3 ». JACC : Basic to Translational Science 3, no 1 (février 2018) : 122–31. http://dx.doi.org/10.1016/j.jacbts.2017.09.009.

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Kögel, Donat, Benedikt Linder, Andreas Brunschweiger, Silvia Chines et 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 (28 février 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 and LC3, BAG3 also delivers polyubiquitinated proteins to the autophagy pathway. BAG3 exerts a number of key physiological functions, including an involvement in cellular stress responses, proteostasis, cell death regulation, development, and cytoskeletal dynamics. Conversely, aberrant BAG3 function/expression has pathophysiological relevance correlated to cardiomyopathies, neurodegeneration, and cancer. Evidence obtained in recent years underscores the fact that BAG3 drives several key hallmarks of cancer, including cell adhesion, metastasis, angiogenesis, enhanced autophagic activity, and apoptosis inhibition. This review provides a state-of-the-art overview on the role of BAG3 in stress and therapy resistance of cancer, with a particular focus on BAG3-dependent modulation of apoptotic signaling and autophagic/lysosomal activity.
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Hiebel, Christof, Elisabeth Stürner, Meike Hoffmeister, Georg Tascher, Mario Schwarz, Heike Nagel, Christian Behrends, Christian Münch et Christian Behl. « BAG3 Proteomic Signature under Proteostasis Stress ». Cells 9, no 11 (4 novembre 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 neurodegenerative disorders. Here, we report a BAG3 proteomic signature under proteostasis stress. To elucidate the dynamic and multifunctional action of BAG3 in response to stress, we established BAG3 interactomes under basal and proteostasis stress conditions by employing affinity purification combined with quantitative mass spectrometry. In addition to the identification of novel potential BAG3 interactors, we defined proteins whose interaction with BAG3 was altered upon stress. By functional annotation and protein-protein interaction enrichment analysis of the identified potential BAG3 interactors, we confirmed the multifunctionality of BAG3 and highlighted its crucial role in diverse cellular signaling pathways and processes, ensuring cellular proteostasis and cell viability. These include protein folding and degradation, gene expression, cytoskeleton dynamics (including cell cycle and transport), as well as granulostasis, in particular.
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Han, Ziying, Michael Schwoerer, Philip Hicks, Jingjing Liang, Gordon Ruthel, Corbett Berry, Bruce Freedman et al. « Host Protein BAG3 is a Negative Regulator of Lassa VLP Egress ». Diseases 6, no 3 (13 juillet 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 bearing protein BCL2 Associated Athanogene 3 (BAG3) as a LFV Z PPPY interactor using our proline-rich reading array of WW-domain containing mammalian proteins. BAG3 is a stress-induced molecular co-chaperone that functions to regulate cellular protein homeostasis and cell survival via Chaperone-Assisted Selective Autophagy (CASA). Similar to our previously published findings for the VP40 proteins of Ebola and Marburg viruses, our results using VLP budding assays, BAG3 knockout cells, and confocal microscopy indicate that BAG3 is a WW-domain interactor that negatively regulates egress of LFV Z VLPs, rather than promoting VLP release. Our results suggest that CASA and specifically BAG3 may represent a novel host defense mechanism, whereby BAG3 may dampen egress of several hemorrhagic fever viruses by interacting and interfering with the budding function of viral PPxY-containing matrix proteins.
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Rauch, Jennifer N., et 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 (5 décembre 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 > Hsp105 ≫ BAG2. All of the NEFs competed for binding to Hsp70, and their relative affinity values predicted their potency in nucleotide and peptide release assays. Finally, we combined the Hsp70-NEF pairs with cochaperones of the J protein family (DnaJA1, DnaJA2, DnaJB1, and DnaJB4) to generate 16 permutations. The activity of the combinations in ATPase and luciferase refolding assays were dependent on the identity and stoichiometry of both the J protein and NEF so that some combinations were potent chaperones, whereas others were inactive. Given the number and diversity of cochaperones in mammals, it is likely that combinatorial assembly could generate a large number of distinct permutations.
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Staibano, Stefania, Massimo Mascolo, Maria Di Benedetto, Maria Luisa Vecchione, Gennaro Ilardi, Giuseppe Di Lorenzo, Riccardo Autorino et al. « BAG3 protein delocalisation in prostate carcinoma ». Tumor Biology 31, no 5 (10 juin 2010) : 461–69. http://dx.doi.org/10.1007/s13277-010-0055-3.

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Carra, Serena, Samuel J. Seguin, Herman Lambert et 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 (15 novembre 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 prevented HspB8-induced Htt43Q degradation. Additionally, depleting Bag3 caused a reduction in the endogenous levels of LC3-II, a key molecule involved in macroautophagy, whereas overexpressing Bag3 or HspB8 stimulated the formation LC3-II. These results suggested that the HspB8-Bag3 complex might stimulate the degradation of Htt43Q by macroautophagy. This was confirmed by the observation that treatments with macroautophagy inhibitors significantly decreased HspB8- and Bag3-induced degradation of Htt43Q. We conclude that the HspB8 activity is intrinsically dependent on Bag3, a protein that may facilitate the disposal of doomed proteins by stimulating macroautophagy.
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Fuchs, Margit, Dominic J. Poirier, Samuel J. Seguin, Herman Lambert, Serena Carra, Steve J. Charette et Jacques Landry. « Identification of the key structural motifs involved in HspB8/HspB6–Bag3 interaction ». Biochemical Journal 425, no 1 (14 décembre 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 of higher-order oligomers of many sHsps (small Hsps). Moreover, we demonstrate that two conserved IPV (Ile-Pro-Val) motifs in Bag3 mediate its binding to HspB8 and that deletion of these motifs suppresses HspB8 chaperone activity towards mutant Htt43Q (huntingtin exon 1 fragment with 43 CAG repeats). In addition, we show that Bag3 can bind to the molecular chaperone HspB6. The interaction between HspB6 and Bag3 requires the same regions that are involved in the HspB8–Bag3 association and HspB6–Bag3 promotes clearance of aggregated Htt43Q. Our findings suggest that the co-chaperone Bag3 might prevent the accumulation of denatured proteins by regulating sHsp activity and by targeting their substrate proteins for degradation. Interestingly, a mutation in one of Bag3 IPV motifs has recently been associated with the development of severe dominant childhood muscular dystrophy, suggesting a possible important physiological role for HspB–Bag3 complexes in this disease.
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Fang, Xi, Julius Bogomolovas, Paul Shichao Zhou, Yongxin Mu, Xiaolong Ma, Zee Chen, Lunfeng Zhang et al. « P209L mutation in Bag3 does not cause cardiomyopathy in mice ». American Journal of Physiology-Heart and Circulatory Physiology 316, no 2 (1 février 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 P209L missense mutation leads to cardiomyopathy remains unknown. To determine the molecular basis underlying the cardiomyopathy caused by the BAG3 P209L mutation, we generated a knockin (KI) mouse model in which the endogenous Bag3 gene was replaced with mutant Bag3 containing the P215L mutation, which is equivalent to the human P209L mutation. We performed physiological, histological, and biochemical analyses of Bag3 P209L KI mice to determine the functional, morphological, and molecular consequences of the P209L mutation. We found that Bag3 P209L KI mice exhibited normal cardiac function and morphology up to 16 mo of age. Western blot analysis further revealed that levels of sHSPs, stress-inducible HSPs, ubiquitinated proteins, and autophagy were unaffected in P209L mutant mouse hearts. In conclusion, the P209L mutation in Bag3 does not cause cardiomyopathy in mice up to 16 mo of age under baseline conditions. NEW & NOTEWORTHY Bcl-2-associated athanogene 3 (BAG3) P209L mutation is associated with human cardiomyopathy. A recent study reported that transgenic mice overexpressing human BAG3 P209L in cardiomyocytes have cardiac dysfunction. In contrast, our P209L mice that express mutant BAG3 at the same level as that of wild-type mice displayed no overt phenotype. Our results suggest that human cardiomyopathy may result from species-specific requirements for the conserved motif that is disrupted by P209L mutation or from genetic background-dependent effects.
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Kyratsous, Christos A., et Saul J. Silverstein. « BAG3, a Host Cochaperone, Facilitates Varicella-Zoster Virus Replication ». Journal of Virology 81, no 14 (2 mai 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 antibiotics or depletion of BAG3 by small interfering RNA results in inhibition of virus replication. Replication in BAG3-depleted cell lines is restored by complementation with exogenous BAG3. Alteration of host chaperone activity provides a novel means of regulating virus replication.
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Thèses sur le sujet "BAG3 protein"

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Guerriero, Luana. « Studio del ruolo della proteina anti-apoptotica BAG3 nel melanoma umano ». Doctoral thesis, Universita degli studi di Salerno, 2016. http://hdl.handle.net/10556/2350.

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2014 - 2015
BAG3 protein, a member of BAG family of co-chaperones, has a pro-survival role in several tumor types. BAG3 anti-apoptotic properties rely on its characteristic to bind several intracellular partners, thereby modulating crucial events such as apoptosis, differentiation, cell motility and autophagy. In human melanomas, BAG3 positivity is correlated with the aggressiveness of the tumor cells and can sustain IKK-γ levels, allowing a sustained activation of NF-B. Furthermore, BAG3 is able to modulate BRAFV600E levels and activity in thyroid carcinomas. BRAFV600E mutation is the most frequent detected in malignant melanomas and is targeted by Vemurafenib, a molecule used for the treatment of advanced melanoma. However a subset of patients resulted not sensitive or acquired resistance to this molecule. Here we confirmed that BAG3 expression is significantly enhanced in metastasis in respect to primary tumors, than we demonstrated that BAG3 protein expression was significantly enhanced in metastasis of patients carring BRAFV600E mutation. Furthermore we found a significant correlation between BAG3 positivity and patients’ overall survival (OS), disease-specific survival (DSS) and disease-free survival (DFS) from surgery in patients with melanoma metastatic lymph nodes. Moreover here we show that BAG3 down-modulation interferes with BRAF levels in melanoma cells and sensitizes them to Vemurafenib treatment. Furthermore, in an in vitro model of acquired resistance to Vemurafenib, we demonstrated that the down-modulation of BAG3 protein can resensitize this cells to BRAFV600E specific inhibition interfering with BRAF pathway, causing reduction of ERK and its targets phosphorylation. Further studies will be focused in demonstrating our hypothesis that the molecular interactions between BAG3 and mutated BRAF can represent a target for novel multi-drugs treatment design and that BAG3 expression could contribute to prognosis and patient stratification for specific therapeutic approaches. [edited by Author]
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Knezevic, Tijana. « TRANSLATIONAL APPROACH TO INVESTIGATE INVOLVEMENT OF BAG3 IN PROTEIN QUALITY CONTROL AND HEART FAILURE ». Diss., Temple University Libraries, 2016. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/374885.

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Biology
Ph.D.
Heart failure continues to be a global problem, even with all the drugs currently available, leading to a need of new therapeutics to decrease incidence of heart failure. Heart failure is the inability of the heart muscle to pump sufficient blood and oxygen to the rest of the body. One of the causes of heart failure is cardiomyopathy, where cardiac muscle becomes larger and weaker. Genetic mutations in genes encoding sarcomeric, structural and cytoskeletal proteins were found in families that developed cardiomyopathy. Our laboratory has indentified a family with heart failure in whom a novel mutation in the BCL2-associated athanogene 3 (BAG3) has been characterized. Among other cardiomyopathy-causing BAG3 mutations reported in various laboratories. Several BAG3 mutations in humans are known to cause familial dilated cardiomyopathy, myofibrilar myopathy, and giant axonal neuropathy. BAG3 is a stress induced co-chaperone protein that interacts with several heat shock proteins and acts as an important regulator of protein quality control. Expression of BAG3 is high in cardiac, skeletal and smooth muscle. BAG3 is localized at the z-disk of cardiomyocytes and was shown to be essential in keeping a normal assembly of z-disk proteins during mechanical stretch. Interaction of BAG3 with actin capping protein CapZbeta1 prevents degradation of CapZbeta1 via proteasome system and maintains the integrity of the z-disk. BAG3 was shown to promote clearance of misfolded proteins, such as filamin C, via autophagy. Not only that BAG3 is able to promote clearance of dysfunctional filamin C, but it was found to enhance synthesis of the new filamin. BAG3 deficient mice develop fulminant myopathy and cardiomyopathy with disorganization of z-disk and die after one month of age. Not only that BAG3 is involved in myofibrilar stability in the cardiomyocytes and that patients with BAG3 mutations develop cardiomyopathy, but our lab showed that patients with heart failure have decrease levels of BAG3. Since heart failure patients have decreased levels of BAG3, the therapy where BAG3 levels are restored to normal levels may improve heart function. Here, I show that in mouse model of heart failure after MI left ventricle function is restored after administration of AAV9 BAG3. BAG3 overexpression in mouse heart helped the stability of z-disk proteins after mechanical stress and myocardial infarction. Overexpressed BAG3 localizes to z-disk and is also able to increase autophagy in cardiomyocytes and help with clearance of misfolded proteins. Taken together, this study shows that BAG3 is a valid and promising new therapeutic target for heart failure patients. BAG3 overexpression is able to induce autophagy and help the heart cope better with stress. Also, AAV9 vector is robustly expressed in the heart after systemic administration, and is a promising vector for gene delivery in the patient heart.
Temple University--Theses
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Falco, Antonia. « Ruolo della proteina BAG3 nel microambiente tumorale ». Doctoral thesis, Universita degli studi di Salerno, 2012. http://hdl.handle.net/10556/293.

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2009 - 2010
Recenti studi hanno dimostrato che il microambiente tumorale subisce numerosi cambiamenti nel corso dello sviluppo del tumore e influenza l’evoluzione e la progressione del cancro. L'ambiente ipossico del tumore stimola l'angiogenesi che può direttamente promuovere la sopravvivenza delle cellule tumorali e la loro invasione. Anche l'infiltrato infiammatorio, associato a molti tumori solidi, è in grado di modulare il comportamento delle cellule tumorali, con effetti anti- e pro-tumorali. Un ruolo importante è svolto anche dai fibroblasti che circondano il tumore, i quali sono in grado di rilasciare fattori di crescita e citochine che stimolano l’ angiogenesi, la crescita del tumore e l'invasione. Tutti questi componenti sono potenziali bersagli per nuove strategie terapeutiche, e, infatti, diverse molecole che agiscono su tali target, sono attualmente utilizzate nelle sperimentazioni cliniche. Inoltre, dati recenti dimostrano che alcuni componenti del microambiente tumorale sono in grado di fornire importanti informazioni prognostiche e predittive. A tale scopo diventa sempre più evidente che, una caratterizzazione completa delle molecole e delle cellule coinvolte nel microambiente del tumore, è richiesta per una maggiore conoscenza della biologia del tumore. BAG3 è una proteina citoplasmatica che è stata recentemente caratterizzata per il suo ruolo centrale in diversi processi associati al tumore quali la sopravvivenza, la proliferazione, la migrazione e l'autofagia. Il ruolo di BAG3 nel microambiente associato al tumore non è stato caratterizzato finora. Pur non avendo un dominio transmembrana, i nostri studi hanno dimostrato che BAG3 può essere associata alla membrana plasmatica e rilasciata nel mezzo extracellulare di alcune cellule neoplastiche e in particolare cellule tumorali del pancreas. Abbiamo anche confermato la presenza di una forma extracellulare di BAG3 nel siero di pazienti affetti da adenocarcinoma pancreatico. Dopo il rilascio nello spazio extracellulare, BAG3 può legare la superficie di cellule adiacenti al tumore, e in particolare abbiamo cercato di stabilire se BAG3 può avere un effetto sui macrofagi che svolgono un ruolo importante nel microambiente infiammatoria associato al tumore. Abbiamo trovato che BAG3 è in grado di legare la superficie cellulare dei macrofagi e di indurre la produzione di componenti associati al processo infiammatorio. Abbiamo anche individuato un nuovo ruolo per BAG3 intracellulare nella regolazione della neo-angiogenesi. Infatti, abbiamo dimostrato che BAG3 è espressa nelle cellule endoteliali e che è in grado di regolare la proliferazione cellulare interagendo con ERK1/2 e la sua fosfatasi DUSP6. Come conseguenza, la riduzione di BAG3 determina una sostenuta fosforilazione di ERK1/2 e una ridotta crescita delle cellule endoteliali in vitro e in vivo. Questo, a sua volta induce una ridotta crescita del tumore in vivo in conseguenza alla ridotta angiogenesi. Complessivamente questi risultati permettono di individuare per la proteina BAG3 un ruolo nuovo nella regolazione dello sviluppo del tumore. [a cura dell'autore]
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Koay, Yee Hui. « The role of BAG6 in protein quality control ». Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/the-role-of-bag6-in-protein-quality-control(75b6fdaa-5c34-4328-b1b8-9f8ba3b94c58).html.

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Proteins must be folded into their correct three-dimensional structure for functions. Failure of proteins to achieve their native conformation is harmful to cells because these proteins are prone to aggregate and engage in non-native interactions. Cells possess extensive protein quality control systems to deal with misfolded proteins, either by refolding the proteins or degrading terminally misfolded proteins. BAG6 has been implicated in cellular protein quality control systems, specifically by recognising stretches of hydrophobic amino acids, recruiting E3 ubiquitin ligase(s) to promote substrate ubiquitination and preventing substrate aggregation. Such stretches of hydrophobic amino acids are typically found in transmembrane domains and endoplasmic reticulum targeting sequences, and BAG6 has been shown to play a role in the quality control and degradation of these proteins. In addition, cytoplasmic proteins may also contain hydrophobic sequences but these would normally be buried within the native structure, and only become exposed if the proteins misfold. However, the precise role of BAG6 in these pathways and the wider contribution of BAG6 to the handling of other aggregation-prone proteins in the cytosol are yet to be studied. Hence, the aim of this project was to determine BAG6 substrate specificity and to gain a better understanding of BAG6 role by identifying endogenous BAG6 substrates and co-factors through targeted and unbiased approaches. UBR4 has been identified as a protein that interacts with a BAG6 substrate (Sec61β) and interacting factor (SGTA) in two independent experiments. UBR4 was found to play a role in endoplasmic reticulum-associated degradation of a BAG6 substrate (opsin-degron), possibly by affecting BAG6-substrate and BAG6-E3 ligase interactions. The unspliced form of XBP1 was predicted to be a BAG6 substrate since XBP1 is a cytoplasmic protein with hydrophobic domain likely to be exposed in the cytoplasm for BAG6 recognition. BAG6 was shown to interact with XBP1 through the hydrophobic domain and affect XBP1 turnover through ubiquitination. Unspliced XBP1 acts as a negative regulator of the spliced XBP1, which is an important transcription factor in the unfolded protein response. BioID was performed as an unbiased approach for BAG6 substrates and co-factors identification. Biotin ligase fused to BAG6 biotinylated proteins coming into close proximity to BAG6, and biotinylated proteins were isolated and analysed with mass spectrometry. Based on bioinformatic analysis of the mass spectrometry data, hydrophobicity of BAG6 'substrates' varied greatly. Biochemical analysis is needed in the future to validate these BAG6-substrate interactions. Together, these results further our understanding of BAG6 role in the protein quality control, especially in the unfolded protein response which was reported for the first time.
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Manchen, Steven T. « Characterization and subcellular localization of the human BAT3 protein ». Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/MQ62248.pdf.

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Iorio, Vittoria. « Determinazione del ruolo della proteina BAG3 nelle isole del Langerhans e suo coinvolgimento nel meccanismo di secrezione dell’insulina ». Doctoral thesis, Universita degli studi di Salerno, 2015. http://hdl.handle.net/10556/2041.

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2012 - 2013
Diabetes is a metabolic alteration due to a decrease in activity of insulin. In particular, it may be a consequence of a reduced availability of this hormone, of an impediment to its normal action, or of a combination of these two factors. The secretion of insulin is a specialized activity of t β cells of the Langerhans islets that are functional endocrine pancreatic part. Diabetes is a widespread disease, particularly in so-called affluent countries, where some risk factors promotes the onset. Actually, it should be considered a syndrome more complex than the simple hyperglycemia. In fact, it is associated to lipid metabolism abnormalities, and increased blood pressure, that, together with abdominal obesity and alterations in glucose homeostasis constitute the so called 'metabolic syndrome': a multifactorial disease that increases the risk of cardiovascular disease. Given to the wide prevalence of this disease, it is therefore necessary a deeper understanding of the normal physiology of β cells and a complete characterization of the molecules involved in the mechanism of insulin secretion. Recently, there has been much progress in this direction, but much remains to be clarified. BAG3 is a protein involved in some of the most important biological processes, such as apoptosis, autophagy, adhesion, migration, and cell invasion. The strong positivity of BAG3 protein in Langerhans islets, recently found in our laboratory, has prompted us to analyze the role of this protein in the β cells physiological functions. To this end, we analyzed BAG3 expression and subcellular localization in the murine insulinoma cell line β TC 6. BAG3 has an apparent mass of 74kDa and is localized in the cytoplasm, here has been shown the presence of a 60 kDa BAG3 form in the insulin- containing granules. The presence in this fraction can be explained by the fact that BAG3 appears to be associated with proteins constitutely expressed on the granules membranes involved in their exocytosis. Indeed, in this work, has been shown the physical interaction of BAG3 protein with t - SNARE SNAP -25 / Syntaxin, which mediate the fusion and exocytosis of insulin vesicles to the plasma membrane. In particular, BAG3 appears to regulate the assembly of the complex allowing a regulated secretion of insulin. In addition, we have shown that BAG3 interacts with the focal adhesion complex FAK / Paxilllin, involved in glucose induced F – actin remodeling. The interaction with FAK, induced by high glucose concentrations, appears to be essential for the phosphorylation of BAG3 by such kinases. BAG3 is also able to sustain ERK phosphorylation, contributing to the destruction of the actin cytoskeleton and increased secretion of insulin. All together these findings disclose a role for BAG3 in regulating insulin release by islet β- cell. [edited by author]
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Casson, Joe. « Investigating the role of TRC40 in post-translational protein delivery and quality control ». Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/investigating-the-role-of-trc40-in-posttranslational-protein-delivery-and-quality-control(02dac94c-857b-4c66-9ea7-8813241dcbce).html.

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Membrane compartmentalisation allows eukaryotic cells to perform complex processes by combining dedicated sets of proteins in the same organelle. To achieve this, the cell must first target the appropriate proteins, primarily synthesised on cytosolic ribosomes, to the correct subcellular location. Components of the secretory pathway/endomembrane system begin this journey via their signal sequence-dependent delivery to the endoplasmic reticulum (ER). These ER targeting signals are hydrophobic, and typically function whilst the protein is being synthesised, via a so-called 'co-translational' pathway. However, some hydrophobic signals can also facilitate post-translational protein targeting to the ER, or initiate regulated protein degradation in the cytosol. Tail-anchored (TA) proteins are transmembrane proteins with a single C-terminal transmembrane domain that functions as both their subcellular targeting signal and membrane anchor. Recent evidence suggests that the canonical TRC40 pathway, through which mammalian TA proteins are delivered to the ER, may not be essential in vivo. In this thesis, I provide functional evidence for the existence of an orthologous SRP-independent (SND) pathway in mammalian cells and identify roles for both the signal recognition particle (SRP)-mediated pathway and presumptive mammalian SND pathway in the biogenesis of TA proteins. I conclude that although TRC40 normally plays a role in TA protein biogenesis, it is not essential, and speculate that these alternative pathways make a significant contribution to the apparent redundancy of the TRC40 pathway in vivo. The soluble components that act upstream of TRC40 during protein biogenesis also play an important role in the recognition and selective degradation of hydrophobic membrane and secretory proteins that mislocalise to the cytosol. I now provide preliminary evidence that TRC40 appears to exhibit dual functionality, having a non-essential role in TA protein delivery, whilst also contributing to protein quality control by acting as a putative holdase. My data suggest that both TRC40 and BAG6 can influence the proteasomal degradation of a novel class of substrates, which I have termed the aberrant short secretory proteins.
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Witcher, Michael. « Interaction of the anti-apoptotic protein BAG-1 with the vitamin D receptor ». Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1999. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape7/PQDD_0010/MQ52698.pdf.

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Wood, Jemma Claire. « The function of Bag-1 proteins in epidermal squamous cell carcinoma ». Thesis, University of Bristol, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.550326.

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The incidence of epidermal squamous cell carcinoma (SCC) has increased significantly over recent years, largely due to increased exposure to its major aetiological factor, UVB radiation. Despite its increasing prevalence, relatively little is known regarding the genetic changes involved in SCC development. The aim of this study was to investigate the potential involvement of the anti-apoptotic protein BcI-2-associated athanogene-l (Bag-i), which shows deregulated expression in a range of human tumours, in epidermal SCC development, in addition to investigating a potential functional role for Bag-l in the epidermal response to UVB radiation. Expression of Bag-l and its key interaction partner Hsp70, which is associated with Bag-l anti- apoptotic function, was investigated in a panel of 60 epidermal SCCs and 10 samples of normal epidermal epithelium. Bag-l expression was deregulated in a subset of tumours compared with normal epidermis, with high Bag-l protein levels associated with reduced tumour differentiation. A positive correlation was observed between cytoplasmic expression of Bag-l and Hsp70, with strong Hsp70 staining also correlating with reduced tumour differentiation. In an attempt to investigate potential functional consequences of elevated Bag-l expression in epidermal tumours, the role of Bag-l in the keratinocyte response to UVB was investigated using the non-tumorigenic, spontaneously immortalised HaCaT cell line as a model system. siRNA-mediated Bag-l knockdown sensitised HaCaT cells to UVB-induced apoptosis, implicating an anti-apoptotic role for Bag-l in this context. The anti-apoptotic function of Bag-l was found to involve the Bag-iS protein isoform, using' stablv-Bag-LS transfected clones of the HaCaT cell line, in addition to transient overexpression of Bag-iS using an adenoviral vector. Bag-l anti- apoptotic function was dependent on amino acid residues required for Hsp70 and Raf-l binding. In HaCaT cells, UVB-irradiation resulted in downregulation of anti-apoptotic McI-l 2 to 8 hours post-irradiation. Levels of the BH3-only pro-apoptotic proteins Bim and Noxa were elevated at 24 hours and 6 to 24 hours post-irradiation, respectively. Overexpression of Bag-iS attenuated UVB-induced McI-l protein reduction, highlighting a potential role for Bag-l in control of McI-l levels. Further to this, a pilot study of 8 samples of normal epidermal epithelium and 14 SCCs highlighted potential overexpression of McI-l in epidermal tumours compared with normal epidermis. The results presented in this thesis demonstrate that expression of Bag-l and Hsp70 is deregulated in epidermal SCC, implicating the Bag-l:Hsp70 axis as a potential novel therapeutic target. Elevated Bag-l expression in epidermal SCC may be associated with its role in protection against apoptosis induced by UVB irradiation in epidermal keratinocytes. Bag-l anti-apoptotic function in this context appears to be mediated, at least in part, via control of levels ofthe anti-apoptotic protein McI-1. Further to its role in protection against UVB-induced apoptosis, an anti-apoptotic role for Bag-l was identified in the response to the chemotherapeutic drug 5-fluorouracil in the SCC-13 epidermal SCC cell line. Levels of Bag-l in epidermal SCC may therefore affect the tumour response to chemotherapeutic agents.
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Clemo, Nadine Kathryn. « The role of the anti-apoptotic protein BAG-1 in colorectal tumour cell survival ». Thesis, University of Bristol, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.441659.

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Livres sur le sujet "BAG3 protein"

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R. A. Yeni Widiawati, Bess Tiesnamurti, Cecep Hidayat, Imas Sri Nurhayati, Teguh Wahyono, Rantan Krisnan, Mohammad Nasir Rofiq et al. Emisi Gas Rumah Kaca dari Peternakan di Indonesia dengan TIER 2 IPCC. Penerbit BRIN, 2021. http://dx.doi.org/10.55981/brin.461.

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Subsektor peternakan merupakan salah satu kontributor gas rumah kaca (GRK) nasional. Kontribusi GRK dari subsektor ini masih di bawah 2% dari total emisi GRK secara nasional. Kontribusi ini diasumsikan akan terus meningkat sejalan dengan upaya penambahan populasi ternak sebagai efek dari diterapkannya salah satu program pemerintah untuk pemenuhan protein hewani asal ternak. Penghitungan emisi GRK dari peternakan mengikuti panduan yang dikeluarkan oleh Intergovernmental Panel on Climate Changes (IPCC). Metode Tier 1 telah digunakan untuk menghitung emisi GRK dari peternakan yang dilaporkan oleh Kementerian Lingkungan Hidup dalam National Communication dan 1st Biennial update progress yang didaftarkan ke United Nations Development Programme (UNDP). Pada metode Tier 1, nilai faktor emisi yang digunakan adalah faktor acuan IPCC yang umum untuk wilayah Asia. Akurasi penghitungan perlu dilakukan dengan menggunakan informasi dan data lokal sehingga dapat menggambarkan emisi GRK yang sesuai dengan kondisi peternakan di Indonesia. Buku ini berisi tentang proses dan hasil penghitungan emisi GRK dengan menggunakan metode yang lebih akurat, yaitu Tier 2 pada semua jenis ternak di Indonesia. Kami berharap buku ini bermanfaat bagi pihak-pihak yang bergerak di bidang perubahan iklim.
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Activity, Jake. Virus Transmission Protect : Activity for Age 10 45 Image Quizzes Words Activity Coloring Books Vegetable, Blood Bag, Virus, Transmission, Pulse, Hand Sanitizer, Disease, Virus. Independently Published, 2020.

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Password Book Charlie Mackesy Captain Sir Tom Moore Tote Bag : Charlie Mackesy Captain Sir Tom Moore Tote Bag Password Log Book and Internet Password Book Organizer, Alphabetical Password Book, Password to Protect Usernames and Charlie Mackesy Captain Sir. Independently Published, 2021.

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RAJEEV, Batra BATRA. Password Book : Suitable for Home and Office , Protect Usernames and Passwords , Logins and Web Addresses, to Keep Usernames , Personal Internet and Password Keeper , Passwords Web Addresses Alphabetical Sort , the Mother Tote Bag, Never Forget a Password. Independently Published, 2021.

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publishing, My Password. WTF Is My Password : Password Book Log Book : MI Trademark CheckMI Popsockets CheckMI Tote Bag CheckMI Pillows Check WTF Is My Password : Password Book, Password Log Book and Internet Password Organizer, Logbook to Protect Usernames and ... Notebook, Passwo. Independently Published, 2021.

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Chapitres de livres sur le sujet "BAG3 protein"

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Behl, Christian. « The role of the co-chaperone BAG3 in selective macroautophagy : implications for aging and disease ». Dans Protein Quality Control in Neurodegenerative Diseases, 87–96. Berlin, Heidelberg : Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-642-27928-7_7.

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Pascale, Maria, Alessandra Rosati, Michelina Festa, Anna Basile, Morena d’Avenia, Antonia Falco, Gaetano Torino et Maria Caterina Turco. « BAG3 Protein : Role in Some Neoplastic Cell Types and Identification as a Candidate Target for Therapy ». Dans Apoptosome, 137–46. Dordrecht : Springer Netherlands, 2009. http://dx.doi.org/10.1007/978-90-481-3415-1_7.

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Brower, Richard C., et S. Roy Kimura. « Semi-explicit bag model for protein solvation ». Dans Computer Simulation of Biomolecular Systems, 223–43. Dordrecht : Springer Netherlands, 1997. http://dx.doi.org/10.1007/978-94-017-1120-3_8.

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Cucci, Andrea, Pietro Lovato et Manuele Bicego. « Enriched Bag of Words for Protein Remote Homology Detection ». Dans Lecture Notes in Computer Science, 463–73. Cham : Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-49055-7_41.

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Bracher, Andreas, et Jacob Verghese. « GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG Domain Proteins : Nucleotide Exchange Factors for Hsp70 Molecular Chaperones ». Dans Subcellular Biochemistry, 1–33. Cham : Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-11731-7_1.

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Bracher, Andreas, et Jacob Verghese. « Nucleotide Exchange Factors for Hsp70 Molecular Chaperones : GrpE, Hsp110/Grp170, HspBP1/Sil1, and BAG Domain Proteins ». Dans Subcellular Biochemistry, 1–39. Cham : Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-14740-1_1.

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Ramos-Pollán, Raúl, John Arévalo, Ángel Cruz-Roa et Fabio González. « High Throughput Location Proteomics in Confocal Images from the Human Protein Atlas Using a Bag-of-Features Representation ». Dans Advances in Intelligent Systems and Computing, 77–82. Cham : Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-01568-2_11.

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Basu, Sujata, Manisha Singh, Mansi Verma et Rachana R. « Multifarious Role of BAG3 in Neurodegenerative Disorders ». Dans Quality Control of Cellular Protein in Neurodegenerative Disorders, 261–81. IGI Global, 2020. http://dx.doi.org/10.4018/978-1-7998-1317-0.ch010.

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The glial cells along with cells of hematopoietic origin and microvascular endothelia work together to maintain the normal development and/or functioning of the nervous system. Disruption in functional coordination among these cells interrupts the efficiency of the nervous system, leading to neurodegeneration. Various proteins in the nerve cells maintain the normal signaling mechanism with these cells and throughout the body. Structural/functional disorganization of these proteins causes neurodegenerative disorders. The molecular mechanisms involved in these phenomena are yet to be explored extensively from therapeutic perspectives. Through this chapter, the authors have elaborated on less known protein Bcl-2 associated athanogene 3 (BAG3) involved in neurodegeneration. They have explored BAG3 protein and its role in neurodegeneration, protein homeostasis, its mechanism of action, its uses as a drug target, and its uses as a possible diagnostic marker of neurodegeneration.
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SOULIMANE, TEWFIK, REINER KIEFERSAUER et MANUEL E. THAN. « Ba3 – Type Cytochrome c Oxidase from Thermus thermophilus : Purification, Crystallization and Crystal Transformation ». Dans Membrane Protein Purification and Crystallization, 229—III. Elsevier, 2003. http://dx.doi.org/10.1016/b978-012361776-7/50015-2.

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Banerjee, Atanu, Alexis Moreno, Jorgaq Pata, Pierre Falson et Rajendra Prasad. « ABCG : a new fold of ABC exporters and a whole new bag of riddles ! » Dans Advances in Protein Chemistry and Structural Biology. Elsevier, 2020. http://dx.doi.org/10.1016/bs.apcsb.2020.09.006.

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Actes de conférences sur le sujet "BAG3 protein"

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McCollum, Andrea K., Mathew G. Angelos, Andrea D. Fischione, Marco Mineo et Elise C. Kohn. « Abstract 2032 : A novel function of WW domain binding protein 2 (WBP2) in regulating cytoskeletal function and cellular division through binding to co-chaperone BAG3 ». Dans Proceedings : AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012 ; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-2032.

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Prayitno, Agus Hadi, et Taufik Hainur Rahman. « Kajian Nilai Gizi Bakso Dengan Bahan Dasar Daging Itik Petelur Afkir ». Dans Kedaulatan Pangan Nasional Melalui Pengembangan Potensi Ternak Lokal di Era Kenormalan Baru. Animal Science : Polije Proceedings Series, 2020. http://dx.doi.org/10.25047/proc.anim.sci.2020.25.

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Penelitian ini bertujuan untuk mengkaji nilai gizi bakso dengan bahan dasar daging itik petelur afkir. Materi penelitian terdiri dari daging itik petelur afkir, tepung tapioka, putih telur, bawang putih, bawang merah, garam, lada, monosodium glutamat, sodium tripolifosfat, dan es. Nilai gizi bakso dihitung berdasarkan angka kecukupan gizi bakso yang mengacu pada rata-rata kecukupan energi bagi penduduk Indonesia per orang per hari yaitu sebesar 2.150 kkal, protein total 60 g, lemak total 67 g, dan serat pangan 30 g dengan takaran saji 50 g dengan jumlah bakso sebanyak 5 butir. Sampel diuji dengan 3 kali ulangan. Data hasil perhitungan nilai gizi bakso dianalisis secara deskriptif. Hasil penelitian menunjukkan bahwa mengkonsumsi bakso daging itik petelur afkir berdasarkan angka kecukupan gizi dengan takaran saji 50 g dapat memenuhi kebutuhan harian lemak 18,21%, protein 8,84%, dan serat pangan 0,18%.
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Shahinpoor, M., et H. Asanuma. « Dynamic Deployment of Smart Inflatable Tsunami Airbags (TABs) for Tsunami Disaster Mitigation ». Dans ASME 2015 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/smasis2015-8904.

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Presented is an initial discussion on dynamic simulation of tsunami air bag deployment in connection with a number of smart inflatable and deployable structures, called tsunami air bags (TAB) that can be rather quickly set up and strongly anchored to the ocean floor to withstand the impact of a tsunami wave and thus protect the buildings and structures on shore. These dedicated inflatable smart structures are designed such that upon tsunami impact they can perform two smart deployment tasks. The first one is for the structure to deploy in the form of a porous structure containing internal folds and pockets and reconfigure due to tsunami impact to perform energy absorption by forcing the tsunami waves to pass through the porous inflatable structure forcing the tsunami waves to lose kinetic energy due to viscous drag and pressurizing the TABs. The second task is related to a special de sign of the inflatable structure that causes it to deploy to either further vertically rise or become a hollow inflatable dam upon the tsunami impact. In these endeavors a wave generation channel was designed and constructed to perform experiments and to simulate tsunami wave impacts on inflatable structures deploying from an underwater location. The initial observation indicates that TABs have a great potential to mitigate tsunami impacts.
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Müller, N., et U. Velten. « FIBRONECTIN CONTENTS AND LEVELS IN BLOOD COMPONENTS DURING STORAGE ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644155.

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Fibronectin has been proposed to have an antithrombotic effect, protecting against platelet and fibrinogen consumption after injury. For the supply of platelets the possibility of extending platelet storage is important forthe management of platelet logistics. This study was designed to determine the effect of storage on the contents and levels of fibro-nectin (FN) in whole blood and components suchas packed RBCs, PRPs and platelet concentrates (PC) in two different plastics. For care of critically ill patients the FN present in components often used in large amounts could supplement the use of purified FN as a source of this opsonic protein. FN protein was assayed using an electroimmunoassay as well as a turbidimetric assay for quantitative determination at 2 day intervals during storage of CPDA-1 stabilized red cells at 4° C for 35 days and daily during end-over-end rotational storage of platelets at 22° C in conventional plastic containers (I) and trimellitate plasticised polyvinylchlo-ride bags (II) (F-763 Biotest). Moreover platelet functional tests, fibrinogen, F XIII and F VIII-complex were tested. FN levels in red cell componentsgradually decreased during storage until to 40% of the initial levels. Platelets maintained a concentrationof 404 ±70 ug/dl (I) and 378±66 ug/dl(II). There were no significant differences between the values determined in the two differentbags over the 8-days storage period. This study demonstrate the stabilityof FN protein during storage and formore effective use of limited donor resources the FN content of each of these products should be considered when determing the dose of FN for replacement therapy in critically ill patients with FN depletion following trauma and surgery.
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Prahardi, R., et Arundito Widikusumo. « Pentingnya Pendidikan dan Pelatihan Bagi Pekerja Radiasi ». Dans Seminar Si-INTAN. Badan Pengawas Tenaga Nuklir, 2021. http://dx.doi.org/10.53862/ssi.v1.062021.005.

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Ionizing radiation, when it hits our bodies, can ionize and excite the atomic nuclei of cells. Ionization and excitation will cause DNA damage either directly or indirectly. DNA damage is direct if ionizing radiation hits DNA, while DNA damage is indirectly through the formation of free radicals (atoms with unpaired electrons) and has a very damaging effect on DNA. Therefore, safety in ionizing radiation, including its use in the medical world, is essential. Protection includes safety avoiding deterministic effects and stochastic effects. To protect against both deterministic and stochastic effects, the role of the radiographer is significant. Heinrich (1980) estimates that (85%) accidents are the result of the contribution of unsafe work behavior (unsafe act). Radiation accidents reported by the United States Energy Atomic Commission from 1960-1968 were caused by operator error (68%), procedural errors (8%), equipment damage (15%), and others (9%). When viewed in detail, the operator's errors were not conducting a radiation survey (46%), not following procedures (36%), not using protective equipment (6%), human error (6%), and calculating radiation exposure errors (6%). Therefore, the radiographer must know and understand ionizing radiation, its dangers, and the application of radiation protection from the results of a survey conducted at Prof. Hospital. Dr. Margono Soekarjo Purwokerto to 22 radiographers showed that the level of understanding of ionizing radiation, the dangers, and the application of radiation protection is still low. Therefore education and training are very much needed for them. Keywords: Radiation Hazard, Radiation Protection, Radiographer Education and Training
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Thiyahuddin, Izzat, Zulkifli Ahamid, M. Hafis M Daud, Azam Abdul Rahman, M. Hairul Sulaiman, Ismail Abdul Hamid, Jing Xianghai, Xu Liangbiao et Wan M. Razlan Wan Razali. « Material Selection Process for Non-Metallic Flexible Buoyancy Bags Assembly in Decommissioning and Marine Salvage ». Dans SPE Asia Pacific Oil & Gas Conference and Exhibition. SPE, 2022. http://dx.doi.org/10.2118/210616-ms.

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ABSTRACT Offshore structure decommissioning and abandonment is a critical component in the life cycle of hydrocarbon production. In Malaysia, 11% of platforms and 8% of pipelines have been in service for more than 40 years, much exceeding their intended lifespan. Conventional methods of decommissioning offshore platform are inherently very costly with the mobilization and operation of HLV (Heavy Lift Vessel). This study developed an Offshore Flexible Buoyancy Tank (OFBT) as the buoyancy assembly to execute future small structure removal operation. This study applies the structured material selection process to determine suitable material as buoyancy assembly enclosure. According to the concept, material selection seeks to determine the lightest, pressure-sustaining, fracture-resistant and cost-effective buoyancy bags suitable for the application. This is a problem with 3 objectives: minimize weight, minimize cost, and withstand the internal pressure in above or submerged conditions. A range of material is tested based on the parameters, and it was determined that Two layers of PET membrane is proposed for OFBT with capacity not less than 380 kN/m. An additional layer is also required to protect the buoyancy bag from puncture or tear. Yard burst test testing is implemented to determine the accuracy of FEA model. A prototype OFBT is fabricated to consist of 3-layer flexible polymer sheet to create an air-containment enclosure. Overall, the FEA correlates well with the result from the burst test. Both burst tests indicate the failure to occur the flange area. The circumferential stiffeners were observed to fail first followed by Longitudinal stiffeners. Results from this work is integrated in the research towards the development of novel flexible offshore buoyancy tank assembly for the removal of jacket structure in decommissioning and abandonment suited to the application in Malaysia.
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Fitriyah, Ana, Chrisdina Aglistinova, Nadya Arsa Difa Rera, Feby Agung Pangestu, Habibilah, Rizki Amalia Nurfitriani et Sadarman. « Pemanfaatan daun jati (Tectona grandis) sebagai pakan ternak : Review ». Dans The 2nd National Conference of Applied Animal Science (CAAS) 2021. Politeknik Negeri Jember, 2021. http://dx.doi.org/10.25047/animpro.2021.2.

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Artikel ini bertujuan untuk mengetahui pemanfaatan daun jati (Tectona grandis) sebagai pakan ternak. Pakan memiliki peranan penting bagi ternak yakni untuk pertumbuhan dan produksi ternak. Indonesia memiliki banyak potensi alam yang dapat dijadikan sebagai pakan. Daun jati merupakan bagian dari pohon jati yang memiliki kandungan nutrient cukup baik dan berpotensi sebagai pakan ternak. Daun jati dapat mengantikan limbah pertanian dan hijauan terutama saat musim kemarau serta sebagai feed additive. Akan tetapi, pemberian daun jati tidak bisa diberikan secara langsung karena memiliki zat anti nutrisi tanin, tidak semua ternak dapat tahan terhadap zat anti nutrisi sehingga pemberian daun jati perlu pengolahan terlebih dahulu. Pengolahan daun jati selama ini dapat dilakukan melalui tiga acara yaitu dengan metode ekstraksi, penepungan, dan fermentasi. Hasil dari ketiga metode tersebut berbeda-beda sesuai tujuan pengolahannya. Penggunaan daun jati baik difermentasi, dimanfaatkan sebagai ekstrak dan tepung berpengaruh nyata terhadap produktivitas tenak. Hasil yang diperoleh yakni tepung daun jati pada level 1,2% efektif untuk menggantikan antibiotik sintetis. Fermentasi daun jati dengan dosis 10% efisien mengunakan bakteri Actinobacillus sp. dapat menurunkan kandungan serat kasar dan meningkatkan kandungan protein kasar. Suplementasi fitobiotik ekstrak daun jati dengan pemberian 1,6% mampu meningkatkan profil darah, khususnya trombosit, ayam petelur. Saran yang dapat diberikan untuk keberlanjutan pemanfaatan daun jati yaitu perlu dilakukan penelitian lebih lanjut untuk pemanfaatan daun jati pada ternak ruminansia.
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Cumming, A. M., R. T. Wensley, S. E. Cottrell et I. W. Delamore. « A STUDY ON THE RECOVERY OF FACTOR VIII PROCOAGULANT ACTIVITY FROM RECALCIFIED, HEPARINISED, CITRATED PLASMA ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644156.

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This study has been carried out to investigate the potential for increasing the recovery of factor VIII procoagulant activity (factor VIII:C),in cryoprecipitates and concentrates, by the use of heparin anticoagulant. Jhctor VIII:C in citrated plasmahas been shown to be stabilised by recalcification and heparinisation of the plasma. Donations of substantially platelet-free and platelet-product-free plasma, anticoagulated by acid citrate dextrose formula A anticoagulant (ACD A), were collected using a combined membrane filtration/centrifugation plasmapheresis device (the HemaSciences "Autopheresis C"(R)). Samples of this plasma were heparinised (over a range from0.1 to 12.8 iu/ml) and physiological Ca2+ levels were restored, levels of fibrinopeptide A (FpA) of less than 5 ng/ml were measured in all samples(including following the incubation of plasmas at 21 °C for 24 hours). This indicated minimal thrombin generation at plasma heparin concentrations as low as 0.1 iu/ml. Fibrinogen degradation fragment BJ3 1542 levelsin these plasmas were comparable to those in ACD A control plasmas and there was no upward trend with increasing heparin concentration. This suggested that heparin-induced formation of plasmin would not adversely affect the stability of factor VIII:C in plasma treated in this way. Cryoprecipitates were prepared in a routine manner from ACD A plasmas collected, by plasmapheresis, into bags containing sufficient heparin and Cacl2 to achieve plasma heparin levels of 0.1 iu/ml and physiological Ca2+ concentrations. (As a result of thissecondary heparinisation, there was no infusion of heparin into the donors). Analysis of the cryoprecipitates revealed no resolubilisation problems, a significant (P<0.02) gain inthe yield of factor VIIIsC comparedwith ACD A control cryoprecipitates, and a mean factor VIIIsC specific activity of 0.11 iu/mg of total protein (S. D. 0.03, 6 experiments). Pools of plasma collected in the above manner are currently being fractionated to evaluate the resulting factor VIII concentrates.
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Askheim, Dag O̸, et Olav Fyrileiv. « New Design Code for Interference Between Trawl Gear and Pipelines : DNV RP-F111 ». Dans 25th International Conference on Offshore Mechanics and Arctic Engineering. ASMEDC, 2006. http://dx.doi.org/10.1115/omae2006-92127.

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The offshore petroleum and the fishing industries are often operating in the same areas. Fishing, in particular bottom trawling, is of concern to pipeline integrity. Such trawling is mainly conducted with two types of trawl gear: otter or beam trawls. The otter trawl boards are steel, more or less rectangular boards which keep the trawl bag open by hydrodynamic drag forces. While the beam trawls use a 10–20 meters long beam to keep the trawl bag open. These trawl gears are dragged along the seabed and represent a potential hazard to pipelines. This paper gives a brief description of types and dimensions of trawl gear. Further it deals with methods for calculating the pipeline response when interacting with bottom trawl gear and finally adresses acceptance criteria for pipeline design and assessment during operation. The calculation methods and acceptance criteria given in this paper are based on test results and research done during the last decades including results from the Kristin, Sno̸hvit and Ormen Lange projects. The above mentioned trawl data, analysis methodology and acceptance criteria are taken from the new DNV Recommended Practice, DNV RP-F111 (2006). This Recommended Practice is an update of the former design code DNV GL 13 (1997). The update was performed mainly due to new types of trawl gear, updated trawl gear data, various experience from application of GL 13 in projects and a general harmonizing process with the pipeline code, DNV OS-F101, and the Hotpipe project, ref Collberg et al. (2005). Large sums are often spent in pipeline projects to protect against trawl gear interaction in terms of concrete coating, trenching or burial. On the other hand the costs of not providing a sufficient protection could be extremely high, with costs related to leakages, failures, stop in production and repair/replacement. This Recommended Practice provides a rational tool to optimize the costs related to trawl gear interference and still ensure that the integrity of the pipeline becomes acceptable.
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Girardi, Davide, Edoardo Marconi et Matteo Massaro. « Assessment of Shoulder and Chest Protection of Wearable Motorcycle Airbags ». Dans ASME 2019 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. American Society of Mechanical Engineers, 2019. http://dx.doi.org/10.1115/detc2019-97782.

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Abstract The application of numerical simulation to wearable airbags for motorcyclists is relatively recent and only few works about this topic can be found in the literature. This research uses multi-physics simulation to analyse a new wearable airbag geometry, primarily designed to protect the shoulders of motorcycle riders, with the aim of assessing the effect of inflation pressure on the protection performance. The finite element model of the airbag employs a simple linear-isotropic material model, calibrated though the comparison between experimental and numerical outcomes of a drop test, together with the analysis of the airbag inflated geometry. The finite element model of the wearable device is then fitted to a dummy model and a human body model, in order to be used in a parametric analysis. Two set-ups are considered. The first is a thorax impact test, used to assess the effect of inflation pressure on chest protection. A modification to the bag geometry is also proposed and tested on this configuration. The second set-up is a shoulder impact test, used to assess the effect of inflation pressure on shoulder protection. In both tests an optimal inflation pressure can be found, but the maximization of shoulder protection proved more critical and should therefore drive the choice of this parameter.
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Rapports d'organisations sur le sujet "BAG3 protein"

1

Takayama, Shin-ichi. BAG Family Proteins : Regulators of Cancer Cell Growth Through Molecular Chaperones. Fort Belvoir, VA : Defense Technical Information Center, juin 2001. http://dx.doi.org/10.21236/ada398188.

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Takayama, Shinichi. BAG Family Proteins : Regulators of Cancer Cell Growth Through Molecular Chaperones. Fort Belvoir, VA : Defense Technical Information Center, juin 2002. http://dx.doi.org/10.21236/ada407556.

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