The unfolded protein response and cellular stress: B
Saved in:
| Format: | Book |
|---|---|
| Language: | English |
| Published: |
Amsterdam [u.a.]
Elsevier, AP
2011
|
| Edition: | 1. ed. |
| Series: | Methods in enzymology
490 |
| Online Access: | Inhaltsverzeichnis |
| Physical Description: | XLVII, 384 S., [4] Bl. Ill., graph. Darst, |
| ISBN: | 9780123851147 |
Staff View
MARC
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| 245 | 1 | 0 | |a The unfolded protein response and cellular stress |n B |c ed. by P. Michael Conn |
| 250 | |a 1. ed. | ||
| 264 | 1 | |a Amsterdam [u.a.] |b Elsevier, AP |c 2011 | |
| 300 | |a XLVII, 384 S., [4] Bl. |b Ill., graph. Darst, | ||
| 336 | |b txt |2 rdacontent | ||
| 337 | |b n |2 rdamedia | ||
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| 490 | 1 | |a Methods in enzymology |v 490 | |
| 490 | 0 | |a Methods in enzymology |v ... | |
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| 830 | 0 | |a Methods in enzymology |v 490 |w (DE-604)BV000000938 |9 490 | |
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Record in the Search Index
| _version_ | 1804143939721101312 |
|---|---|
| adam_text | Contents
Contributors
xi
Preface
xvii
Volumes in Series
xix
ι.
Methods for Investigating the UPR in Filamentous Fungi
1
Thomas Guillemette, Arthur F. J. Ram,
Neuza D.
S. P.
Carvalho,
Aymeric Joubert, Philippe Simoneau, and David B. Archer
1.
Introduction
2
2.
Conditions
to Study the UPR in Filamentous Fungi
5
3.
Analysis of Expression During the
ER
Stress
11
4.
Modifying the UPR Signaling by Targeted Gene Replacement
14
Acknowledgments
25
References
26
г.
Assays for Detecting the Unfolded Protein Response
31
Karen Cawley, Shane Deegan, Afshin Samali, and Sanjeev Gupta
1.
Introduction
33
2.
Experimental Approaches for the Detection of
ER
Stress
36
3.
Concluding Remarks
47
Acknowledgments
49
References
49
3.
Analysis of the Role of Nerve Growth Factor in Promoting
Cell Survival During Endoplasmic Reticulum Stress
in PC12 Cells
53
Kojí
Shimoke,
Наше
Sasaya, and Toshihiko Ikeuchi
1.
Introduction
54
2.
Induction of
ER
Stress in PC12 Cells
55
3.
Measurement of Caspase-3 Activity
62
4.
Fragmentation of
Caspase-íž
63
5.
Hyperinductîon
of 6RP78 by NGF
65
Acknowledgments
68
References
68
V¡
Contents
ц.
Measuring
ER
Stress and the Unfolded Protein Response
Using Mammalian Tissue Culture System
71
Christine M. Oslowski and Fumihiko
Urano
1.
Introduction
72
2. ER
Stress and the UPR
73
3.
Cell Culture System and
ER
Stress Induction
76
4.
Measuring
ER
Stress
78
5.
Studying the UPR Activation
79
6.
Studying UPR Downstream Markers and Responses
84
Acknowledgments
88
References
88
5.
Real-Time Monitoring of
ER
Stress in Living Cells and
Animals Using ESTRAP Assay
93
Masanori Kitamura and Nobuhiko Hiramatsu
1.
Introduction
94
2.
SEAP Reporter System
95
3.
Monitoring of
ER
Stress in Culture Cells by ESTRAP
96
4.
Monitoring of
ER
Stress In Vivo by ESTRAP
101
5.
Conclusion
104
References
105
6. HIV
Protease Inhibitors Induce Endoplasmic Reticulum Stress
and Disrupt Barrier Integrity in Intestinal Epithelial Cells
107
HuipingZhou
1.
The Pathophysiological Relevance of
HIV
Pl-lnduced
ER
Stress and UPR Activation in lECs
108
2.
Analysis of
HIV Pl-lnduced ER
Stress and UPR
Activation in Cultured lECs
109
3.
Analysis of
HIV Pl-lnduced ER
Stress and Disruption of
Barrier Integrity in the Intestine
114
4.
Summary
118
Acknowledgments
118
References
118
7.
Dexamethasone Induction of a Heat Stress Response
121
José
A. Guerrero, Vicente Vicente, and Javier Corral
1.
Introduction
122
2.
Evaluation of the Heat Stress Response in Patients
Treated with Dexamethasone
124
3.
Heat Stress Response and UPR in Mice and Cellular Models
126
References
134
Contents
vii
8.
Detecting and Quantitating Physiological Endoplasmic
Reticulum Stress
137
Ling Qi, Liu Yang, and
Hui
Chen
1.
Introduction
138
2.
Detecting UPR at the Level of UPR Sensors
139
3.
Quantitating
ER
Stress at the Level of UPR Sensors
141
4.
Detecting Levels of Other Common UPR Targets
142
5.
Important Tips
143
6.
Concluding Remarks
144
Acknowledgments
145
References
145
9.
PI 3-Kinase Regulatory Subunits as Regulators of the
Unfolded Protein Response
147
Jonathon
N.
Winnay and
С
Ronald
Kahn
1.
The Unfolded Protein Response
148
2.
PI 3-Kinase Regulatory Subunits as Modulators of the UPR
150
3.
Assessing UPR Pathway Activation
151
References
157
io.
The Emerging Role of Histone Deacetylases (HDACs) in
UPR Regulation
159
Soumen Kahali, Bhaswati
Sarcar,
and Prakash Chinnaiyan
1.
HDAC Enzymes and Cancer
159
2.
HDAC Inhibitors
160
3.
HDAC Inhibition and the UPR
162
4.
Future Directions
172
References
173
її.
Immunohistochemical Detection of Activating Transcription
Factor
3,
a Hub of the Cellular Adaptive-Response Network
175
Tsonwin
Hai,
Swati Jalgaonkar, Christopher C. Wolford, and Xin Yin
1.
Introduction
176
2.
An IHC Protocol for ATF3
181
Acknowledgments
192
References
192
12.
Experimental Approaches for Elucidation of Stress-Sensing
Mechanisms of the
Irei
Family Proteins
195
Daisuke Oikawa and Yukio Kimata
1.
Introduction
196
viii Contents
2. Monitoring In Vivo
Activity of Mutated
Irei Family
Proteins
199
3.
Interaction Between BiP and the
Irei
Family Proteins
206
4.
Direct Interaction of Unfolded Proteins with Yeast
Irei
but not with
Mammalian IREloc
210
5.
Conclusion and perspective
213
Acknowledgments
214
References
214
13.
Measurement and Modification of the Expression Level of the
Chaperone Protein and Signaling Regulator
GRP78/BÌP
in
Mammalian Cells
217
Wan-Ting Chen and Amy S. Lee
1.
Introduction
218
2.
Detection of Total GRP78
220
3.
Detection of Cytosolic GRP78
Isoform 224
4.
Detection of Cell Surface GRP78
228
Acknowledgments
231
References
232
14.
The Endoplasmic Reticulum-Associated Degradation and
Disulfide Reductase ERdj5
235
Ryo Ushioda and Kazuhiro Nagata
1.
Introduction
236
2.
Productive Folding of Newly Synthesized Proteins in the
ER 238
3.
ERAD:
A Strategy for ERQC Mechanism
242
4.
Conclusion
249
References
252
15.
Structural Insight into the Protective Role of P58(IPK) during
Unfolded Protein Response
259
Jiahui Tao and Bingdong
Sha
1.
Endoplasmic Reticulum Stress and Unfolded Protein Response
260
2.
P58(IPK) Might be a Dual-Function Protein
261
3.
Knocking Out P58(IPK) in Mouse Models
261
4.
P58QPK) is an ER-Resident Hsp40
262
5.
Crystal Structure of Mouse P58(IPK) TPR Domain
263
6.
P58(IPK) Functions as a Molecular Chaperone to Bind Unfolded
Proteins Using
Subdomain
I
264
7.
Structural Basis for P58(IPK)
J Domain-BiP
Interaction
267
8.
Working Model of P58(IPK) During UPR
267
9.
Future Research
267
References
268
Contents
¡χ
16.
Principles of
IREI
Modulation Using Chemical Tools
271
Kenneth P. K. Lee and Frank
Sichert
1.
Introduction: The Unfolded Protein Response
272
2.
Structural Biology of IRE1-XBP1 Signaling
276
3.
Chemical Approaches to Modulate
IREI
Function
282
References
292
17.
Methods to Study Stromal-Cell Derived Factor
2
in the
Context of
ER
Stress and the Unfolded Protein Response
in Arabidopsis thaliana
295
Andrea
Schott
and
Sabine Strahl
1.
Introduction
296
2.
Arabidopsis sdf2
Т
-DNA
Insertion Lines
297
3.
Inducing and Monitoring
ER
Stress in Arabidopsis sdf2 Mutants
299
4.
Analyzing the
ER
Stress-Induced Expression Pattern of SDF2 in
Arabidopsis
304
5.
The Subcellular Localization of SDF2
309
6.
Purification of
Recombinant 5DF2
Protein from
E. coli
313
Acknowledgments
316
References
317
18.
Nitrosative Stress-Induced 5-Glutathionylation of
Protein Disulfide Isomerase
321
Joachim D. Uys, Ying Xiong, and Danyelle M. Townsend
1.
Introduction
322
2.
Identification and Confirmation of S-Glutathionylated
Proteins in Cells
324
3.
Identification of Target
Cysteine
Residues
327
4.
Characterization of
Structurat
and Functional Consequences of
S-Glutathionylated PDI
329
5.
Summary
331
Acknowledgments
331
References
331
29.
Methods for Analyzing elF2 Kinases and Transtational
Control in the Unfolded Protein Response
333
Brian F. Teske, Thomas D. Baird, and Ronald
С
Wek
1.
Introduction to Translational Control in the UPR
334
2.
Measuring Activation of the elF2 Kinase Pathway During
ER
Stress
338
3.
Investigating General and Gene-Specific Translation Control
345
Contents
Acknowledgments
353
References
353
Author Index
357
Subject Index
375
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| indexdate | 2024-07-09T22:55:38Z |
| institution | BVB |
| isbn | 9780123851147 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-021213009 |
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| physical | XLVII, 384 S., [4] Bl. Ill., graph. Darst, |
| publishDate | 2011 |
| publishDateSearch | 2011 |
| publishDateSort | 2011 |
| publisher | Elsevier, AP |
| record_format | marc |
| series | Methods in enzymology |
| series2 | Methods in enzymology |
| spelling | The unfolded protein response and cellular stress B ed. by P. Michael Conn 1. ed. Amsterdam [u.a.] Elsevier, AP 2011 XLVII, 384 S., [4] Bl. Ill., graph. Darst, txt rdacontent n rdamedia nc rdacarrier Methods in enzymology 490 Methods in enzymology ... Conn, P. Michael 1949- Sonstige oth (DE-604)BV037299810 2 Methods in enzymology 490 (DE-604)BV000000938 490 Digitalisierung UB Regensburg application/pdf http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021213009&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA Inhaltsverzeichnis |
| spellingShingle | The unfolded protein response and cellular stress Methods in enzymology |
| title | The unfolded protein response and cellular stress |
| title_auth | The unfolded protein response and cellular stress |
| title_exact_search | The unfolded protein response and cellular stress |
| title_full | The unfolded protein response and cellular stress B ed. by P. Michael Conn |
| title_fullStr | The unfolded protein response and cellular stress B ed. by P. Michael Conn |
| title_full_unstemmed | The unfolded protein response and cellular stress B ed. by P. Michael Conn |
| title_short | The unfolded protein response and cellular stress |
| title_sort | the unfolded protein response and cellular stress |
| url | http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&local_base=BVB01&doc_number=021213009&sequence=000002&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA |
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