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Apoptosis in health and disease. Part B /

Apoptosis in Health and Disease - Part B, Volume 126 in the Advances in Protein Chemistry and Structural Biology focuses on apoptotic responses in numerous conditions - from bacterial and parasite infections, to pathological states such as oxidative stress, pulmonary hypertension, and different canc...

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Bibliographic Details
Corporate Author: ScienceDirect (Online service)
Other Authors: Donev, Rossen (Editor)
Format: eBook
Language:English
Published: Cambridge, MA : Academic Press, 2021.
Series:Advances in protein chemistry and structural biology ; v. 126.
Subjects:
Apoptosis.
Apoptose.
Biophysics.
Biotechnology.
MEDICAL.
Biochemistry.
Life Sciences.
SCIENCE.
Cell Biology.
Genetics & Genomics.
Molecular Biology.
Apoptosis
Electronic books.
Online Access:Connect to the full text of this electronic book
Table of Contents:
  • Intro
  • Apoptosis in Health and Disease
  • Part B
  • Copyright
  • Contents
  • Contributors
  • Chapter One: Structural insights of macromolecules involved in bacteria-induced apoptosis in the pathogenesis of human di ...
  • 1. Introduction
  • 2. Pathogenesis and apoptosis
  • 3. Role of bacterial component signaling through cellular receptors
  • 4. Effector molecules of apoptosis
  • 5. Role of bacterial toxins in pore-forming mechanism
  • 6. Bacterial type-III protein secretion pathway
  • 7. Bacterial infection-induced apoptosis
  • 7.1. Neisseria meningitidis
  • 7.2. Mycobacterium tuberculosis
  • 7.3. Legionella pneumophila
  • 7.4. Haemophilus influenzae
  • 7.5. Streptococcus pneumoniae
  • 7.6. Staphylococcus aureus
  • 7.7. Bacillus anthracis
  • 8. Apoptosis regulation during bacterial infections
  • 9. The YhaK protein
  • 10. Bacterial kinase family proteins involved in apoptosis
  • 11. The effector kinase domain
  • 12. Structural insights of protein-protein interactions
  • 13. Mechanism of inhibition
  • 14. Concluding remarks
  • Acknowledgments
  • References
  • Chapter Two: Apoptosis: A friend or foe in mesenchymal stem cell-based immunosuppression
  • 1. Introduction
  • 2. Factors affecting immunosuppressive properties of MSC
  • 3. MSC-dependent immunosuppression is relied on phagocytosis of apoptotic MSC
  • 4. An important role of IDO/kynurenine pathway for immunoregulatory properties of apoptotic MSC
  • 5. Molecular and cellular mechanisms responsible for beneficial effects of apoptotic MSC in the attenuation of sepsis
  • 6. An interplay between autophagy and apoptosis in MSC-based immunomodulation
  • 7. Conclusions
  • References
  • Chapter Three: Differential roles of farnesoid X receptor (FXR) in modulating apoptosis in cancer cells
  • 1. Introduction
  • 2. FXR and diseases
  • 3. FXR is differentially expressed in different cancers.
  • 3.1. Overexpression of FXR leads to breast, colon, esophageal, lung, pancreatic, prostate, renal and thyroid cancers
  • 3.2. Low expression of FXR leads to colon, cholangiocarcinoma, liver, and prostate cancer
  • 4. Role of activators in the inhibition/induction of apoptosis
  • 5. Role of inhibitors in the inhibition/induction of apoptosis
  • 6. Conclusions
  • References
  • Chapter Four: Alternative approaches to overcome chemoresistance to apoptosis in cancer
  • 1. Apoptosis
  • 1.1. Apoptotic mechanisms
  • 1.1.1. Intrinsic pathway
  • 1.1.2. Extrinsic pathway
  • 1.2. Resistance to apoptosis in cancer
  • 1.2.1. Resistance mechanisms
  • 2. Non-apoptotic, alternate cell death mechanisms
  • 2.1. Necroptosis
  • 2.1.1. Necroptotic mechanism
  • 2.1.2. Induction of necroptosis to kill cancer cells
  • 2.2. Pyroptosis
  • 2.2.1. Pyroptotic mechanism
  • 2.2.2. Indcution of pyroptosis to kill cancer cells
  • 2.3. Autophagy
  • 2.3.1. Autophagic process
  • 2.3.2. Inhibition of autophagy to induce tumor cell death
  • 2.4. Ferroptosis
  • 2.4.1. The role of GPx4 in ferroptosis
  • 2.4.2. Regulation of ferroptosis
  • 2.4.3. Regulation of ferroptosis by iron homeostasis
  • 2.4.4. Induction of ferroptosis in cancer
  • 2.5. Methuosis
  • 3. Conclusion
  • Acknowledgments
  • Conflict of interests
  • References
  • Chapter Five: Recent developments in CCR5 regulation for HIV cure
  • 1. Introduction
  • 1.1. CCR5 biology
  • 1.2. Mechanism of HIV entry
  • 1.3. Treatment strategies
  • 1.3.1. CCR5 Antagonists
  • 1.3.2. Hematopoietic stem cells
  • 1.3.3. ZFNs/TALENs
  • 1.3.4. RNAi regulation
  • 1.3.5. CRISPR/Cas9 regulation
  • 1.4. Modeling
  • 1.4.1. Animal models
  • 1.4.2. Clinical trials
  • 2. Conclusion
  • Acknowledgments
  • References
  • Chapter Six: RNA-seeded membraneless bodies: Role of tandemly repeated RNA
  • 1. Introduction
  • 2. Mechanisms of MLO assembly.
  • 2.1. Liquid-liquid phase separation
  • 2.2. The role of RNA in MLO assembly
  • 2.3. Role of the non-coding RNA
  • 2.4. DNA-induced MLO formation
  • 3. Tandemly repeated RNA: A novel player in MLO game?
  • 3.1. Tandemly repeated DNA and its transcription
  • 3.2. TR RNA in MLO
  • 3.3. Chromatin as MLO
  • 4. MLO built on TR DNA in disease
  • 5. Conclusion
  • Competing interests
  • Author contributions
  • Acknowledgments
  • Funding
  • References
  • Chapter Seven: Cell death mechanisms and their roles in pregnancy related disorders
  • 1. Introduction
  • 2. Overview of apoptosis
  • 2.1. Regulation of apoptosis
  • 2.2. Extrinsic pathway of apoptosis
  • 2.3. Intrinsic pathway of apoptosis
  • 3. Apoptosis in normal pregnancy
  • 4. Apoptosis in different pregnancy complications
  • 5. Factors influencing apoptosis
  • 6. Overview of autophagy
  • 6.1. Regulation of autophagy
  • 7. Interplay between apoptosis and autophagy
  • 7.1. Autophagy in normal pregnancy
  • 8. Autophagy in different pregnancy complications
  • 9. Conclusion
  • Acknowledgments
  • References
  • Chapter Eight: The concept of protein folding/unfolding and its impacts on human health
  • 1. Introduction
  • 2. Establishing forces in folded proteins
  • 2.1. Hydrophobic effect
  • 2.2. Hydrogen bonds
  • 2.3. Salt bridges
  • 2.4. Conformational entropy
  • 2.5. Disulfide bonds
  • 3. Models of protein folding
  • 3.1. Jigsaw puzzle model
  • 3.2. Nucleation-growth model
  • 3.3. Diffusion-collision-adhesion model
  • 3.4. Framework model
  • 3.5. Hydrophobic collapse model
  • 3.6. Nucleation-condensation model
  • 3.7. Free energy landscape
  • 4. In vivo folding
  • 4.1. Chaperones and chaperonins
  • 4.2. Reaction cycle
  • 4.3. Folding catalysts
  • 5. Amyloid structures
  • 5.1. Instrumental studies of protein fibrillation
  • 5.2. Morphology and kinetics
  • 5.3. Thermodynamics of the amyloid state.
  • 5.4. Causes of amyloidogenesis
  • 5.5. Amyloid structures and apoptosis
  • 5.6. Microfluidics
  • 5.7. Glycation
  • 6. Molten globule and its structure
  • 6.1. The role of molten globule in protein folding
  • 6.2. Molten globule and surfactants
  • 6.3. Other intermediate structures of molten globule
  • 7. Computational approaches of protein folding
  • 7.1. All-atom models
  • 7.2. Coarse-grained models
  • 7.3. Multiscale modeling approach
  • 8. Folding of multi-domain and multi-subunit proteins
  • 8.1. Multi-domain proteins
  • 8.2. Multi-subunit proteins
  • 9. Misfolding and disease
  • 10. Concluding remarks
  • Acknowledgments
  • References
  • Chapter Nine: Apoptosis in health and diseases of the eye and brain
  • 1. Introduction: An overview of apoptosis
  • 1.1. Intrinsic pathway
  • 1.2. Extrinsic pathway
  • 1.3. T-cell mediated pathway
  • 1.4. Execution pathway
  • 2. Apoptosis in the health of the eye and the brain
  • 3. Apoptosis in diseases of the eye
  • 3.1. Glaucoma
  • 3.1.1. Detection of apoptosing retinal cells
  • 3.2. Retinal diseases
  • 3.2.1. Age related macular degeneration
  • 3.2.2. Diabetic retinopathy
  • 3.2.3. Retinitis dystrophies
  • 3.3. Dry eye disease
  • 4. Apoptosis and diseases of the brain
  • 4.1. Alzheimer´s disease
  • 4.2. Parkinson´s disease
  • 4.3. Amyotrophic lateral sclerosis
  • 4.4. Huntington´s disease
  • 5. Conclusion
  • References
  • Chapter Ten: Apoptotic signals at the endoplasmic reticulum-mitochondria interface
  • 1. Introduction
  • 2. Apoptosis: A programmed form of cell death
  • 2.1. Apoptotic signaling pathways cause caspases activation
  • 2.2. The extrinsic pathway
  • 2.3. The intrinsic pathway
  • 2.4. ER stress-induced apoptosis
  • 3. MAMs and players
  • 3.1. The IP3R-GRP75-VDAC complex
  • 3.2. The Fis1-BAP31 complex
  • 3.3. PACS2
  • 3.4. The Mfn1-Mfn2/Mfn2-Mfn2 complex
  • 3.5. The VAPB-PTPIP5 complex.
  • 4. MAMs and functions
  • 4.1. Lipid handling at ER-mitochondria interface
  • 4.2. Calcium signaling at ER-mitochondria interface
  • 5. The role of MAMs in apoptosis
  • 5.1. Ca signaling in apoptosis
  • 5.2. Pro- and anti-apoptotic players acting on Ca signaling
  • 5.3. Role of lipid metabolism in apoptosis
  • 5.4. Other players involved in transduction of apoptosis signal between ER and mitochondria
  • 6. Conclusions
  • Acknowledgments
  • References.