Heat Shock in Vivo Induces Mallory Body Formation in Drug Primed Mouse Liver

1995 ◽  
Vol 63 (1) ◽  
pp. 63-76 ◽  
Author(s):  
Qi X. Yuan ◽  
Normand Marceau ◽  
Barbara A. French ◽  
Paul Fu ◽  
Samuel W. French
Keyword(s):  
Heat Shock ◽  
Mouse Liver ◽  
Body Formation ◽  
Primed Mouse

Dexamethasone Enhances Mallory Body Formation in Drug-Primed Mouse Liver

2000 ◽  
Vol 69 (3) ◽  
pp. 202-210 ◽  
Author(s):  
Qi X. Yuan ◽  
Yasuyuki Nagao ◽  
Barbara A. French ◽  
Yu-Jui Yvonne Wan ◽  
Samuel W. French
Keyword(s):  
Mouse Liver ◽  
Body Formation ◽  
Primed Mouse

scholarly journals Bile Acid-Induced Mallory Body Formation in Drug-Primed Mouse Liver

2002 ◽  
Vol 161 (6) ◽  
pp. 2019-2026 ◽  
Author(s):  
Peter Fickert ◽  
Michael Trauner ◽  
Andrea Fuchsbichler ◽  
Conny Stumptner ◽  
Kurt Zatloukal ◽  
...  
Keyword(s):  
Bile Acid ◽  
Mouse Liver ◽  
Body Formation ◽  
Primed Mouse

The Effect of Agents which Modify Platelet Behaviour and of Magnesium Ions on Thrombus Formation In Vivo

1979 ◽  
Vol 42 (02) ◽  
pp. 603-610 ◽  
Author(s):  
J H Adams ◽  
J R A Mitchell
Keyword(s):  
Thrombus Formation ◽  
Cerebral Arteries ◽  
Magnesium Ions ◽  
Body Formation ◽  
Inflammatory Agent ◽  
Platelet Thrombus ◽  
Magnesium Salts ◽  
Higher Doses ◽  
Do So

SummaryThe ability of potential anti-thrombotic agents to modify platelet-thrombus formation in injured cerebral arteries in the rabbit was tested. Low doses of heparin were without effect, while higher doses produced variable suppression of white body formation but at the expense of bleeding. Aspirin did not inhibit white body formation but another non-steroid anti-inflammatory agent, flurbiprofen was able to do so, as was the anti-gout agent, sulphinpyrazone. Magnesium salts both topically and parenterally, suppressed thrombus formation and increased the concentration of ADP which was required to initiate thrombus production at minor injury sites.

scholarly journals Phosphorylation of Serine 303 Is a Prerequisite for the Stress-Inducible SUMO Modification of Heat Shock Factor 1

2003 ◽  
Vol 23 (8) ◽  
pp. 2953-2968 ◽  
Author(s):  
Ville Hietakangas ◽  
Johanna K. Ahlskog ◽  
Annika M. Jakobsson ◽  
Maria Hellesuo ◽  
Niko M. Sahlberg ◽  
...  
Keyword(s):  
Heat Shock ◽  
Phosphorylation Site ◽  
Stress Granules ◽  
Heat Shock Factor ◽  
Transcriptional Level ◽  
Heat Shock Factor 1 ◽  
Protection Mechanism ◽  
Sumo Modification

ABSTRACT The heat shock response, which is accompanied by a rapid and robust upregulation of heat shock proteins (Hsps), is a highly conserved protection mechanism against protein-damaging stress. Hsp induction is mainly regulated at transcriptional level by stress-inducible heat shock factor 1 (HSF1). Upon activation, HSF1 trimerizes, binds to DNA, concentrates in the nuclear stress granules, and undergoes a marked multisite phosphorylation, which correlates with its transcriptional activity. In this study, we show that HSF1 is modified by SUMO-1 and SUMO-2 in a stress-inducible manner. Sumoylation is rapidly and transiently enhanced on lysine 298, located in the regulatory domain of HSF1, adjacent to several critical phosphorylation sites. Sumoylation analyses of HSF1 phosphorylation site mutants reveal that specifically the phosphorylation-deficient S303 mutant remains devoid of SUMO modification in vivo and the mutant mimicking phosphorylation of S303 promotes HSF1 sumoylation in vitro, indicating that S303 phosphorylation is required for K298 sumoylation. This finding is further supported by phosphopeptide mapping and analysis with S303/7 phosphospecific antibodies, which demonstrate that serine 303 is a target for strong heat-inducible phosphorylation, corresponding to the inducible HSF1 sumoylation. A transient phosphorylation-dependent colocalization of HSF1 and SUMO-1 in nuclear stress granules provides evidence for a strictly regulated subnuclear interplay between HSF1 and SUMO.

scholarly journals Molecular Characterization of Dendritic Cell-Derived Exosomes

1999 ◽  
Vol 147 (3) ◽  
pp. 599-610 ◽  
Author(s):  
Clotilde Théry ◽  
Armelle Regnault ◽  
Jérôme Garin ◽  
Joseph Wolfers ◽  
Laurence Zitvogel ◽  
...  
Keyword(s):  
Dendritic Cell ◽  
Heat Shock ◽  
Immune Responses ◽  
Milk Fat ◽  
Protein Composition ◽  
Antitumor Effects ◽  
Peripheral Tissues ◽  
Peptide Mass ◽  
Dc Maturation

Exosomes are membrane vesicles secreted by hematopoietic cells upon fusion of late multivesicular endosomes with the plasma membrane. Dendritic cell (DC)-derived exosomes induce potent antitumor immune responses in mice, resulting in the regression of established tumors (Zitvogel, L., A. Regnault, A. Lozier, J. Wolfers, C. Flament, D. Tenza, P. Ricciardi-Castagnoli, G. Raposo, and S. Amigorena. 1998. Nat. Med. 4:594–600). To unravel the molecular basis of exosome-induced immune stimulation, we now analyze the regulation of their production during DC maturation and characterize extensively their protein composition by peptide mass mapping. Exosomes contain several cytosolic proteins (including annexin II, heat shock cognate protein hsc73, and heteromeric G protein Gi2α), as well as different integral or peripherally associated membrane proteins (major histocompatiblity complex class II, Mac-1 integrin, CD9, milk fat globule-EGF-factor VIII [MFG-E8]). MFG-E8, the major exosomal component, binds integrins expressed by DCs and macrophages, suggesting that it may be involved in exosome targeting to these professional antigen-presenting cells. Another exosome component is hsc73, a cytosolic heat shock protein (hsp) also present in DC endocytic compartments. hsc73 was shown to induce antitumor immune responses in vivo, and therefore could be involved in the exosome's potent antitumor effects. Finally, exosome production is downregulated upon DC maturation, indicating that in vivo, exosomes are produced by immature DCs in peripheral tissues. Thus, DC-derived exosomes accumulate a defined subset of cellular proteins reflecting their endosomal biogenesis and accounting for their biological function.

scholarly journals Cell Cycle-Dependent Binding of Yeast Heat Shock Factor to Nucleosomes

2000 ◽  
Vol 20 (17) ◽  
pp. 6435-6448 ◽  
Author(s):  
Christina Bourgeois Venturi ◽  
Alexander M. Erkine ◽  
David S. Gross
Keyword(s):  
Heat Shock ◽  
Nuclear Dna ◽  
Heat Shock Factor ◽  
Binding Activity ◽  
S Phase ◽  
Regulatory Sequences ◽  
Prevailing Paradigm ◽  
Cycle Dependent ◽  
Gain Access

ABSTRACT In the nucleus, transcription factors must contend with the presence of chromatin in order to gain access to their cognate regulatory sequences. As most nuclear DNA is assembled into nucleosomes, activators must either invade a stable, preassembled nucleosome or preempt the formation of nucleosomes on newly replicated DNA, which is transiently free of histones. We have investigated the mechanism by which heat shock factor (HSF) binds to target nucleosomal heat shock elements (HSEs), using as our model a dinucleosomal heat shock promoter (hsp82-ΔHSE1). We find that activated HSF cannot bind a stable, sequence-positioned nucleosome in G1-arrested cells. It can do so readily, however, following release from G1 arrest or after the imposition of either an early S- or late G2-phase arrest. Surprisingly, despite the S-phase requirement, HSF nucleosomal binding activity is restored in the absence of hsp82 replication. These results contrast with the prevailing paradigm for activator-nucleosome interactions and implicate a nonreplicative, S-phase-specific event as a prerequisite for HSF binding to nucleosomal sites in vivo.

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