: Thomas Dittmar, Kurt S. Zänker
: Cell Fusion in Health and Disease I: Cell Fusion in Health
: Springer-Verlag
: 9789400707634
: Advances in Experimental Medicine and Biology
: 1
: CHF 135.30
:
: Nichtklinische Fächer
: English
: 192
: Wasserzeichen
: PC/MAC/eReader/Tablet
: PDF
Although cell fusion is an omnipresent process in life, to date considerably less is still known about the mechanisms and the molecules being involved in this biological phenomenon in higher organisms. In Cell Fusion in Health and Disease Vol 1& Vol 2 leading experts will present up-to-date overviews about cell fusion in physiological and patho-physiological processes, which further covers the current knowledge about cell fusion-mediating molecules. Volume 1 deals with Cell Fusion in Health and will cover aspects of cell fusion in fertilization, placentation, in C. elegans, in skeletal muscle development and tissue repair, and the use of cell fusion for cellular reprogramming and cancer vaccine development. Volume 2 focuses on Cell Fusion in Disease with a particular emphasis on the role of cell fusion in cancer development and progression. Thus, Cell Fusion in Health and Disease Vol 1& Vol 2 represents a state-of-the-art work for researchers, physicians or professionals being interested in the biological phenomenon of cell fusion and beyond.
Preface6
Contents9
Contributors10
1 Introduction12
2 Heterochronic Control of AFF-1-Mediated Cell-to-Cell Fusion in C. elegans 15
2.1 Introduction15
2.2 Heterochronic Genes Regulate the Timing of Developmental Events15
2.3 The Heterochronic Gene lin-29 Determines the Final Fate of the Seam Cells16
2.4 LIN-29 Controls the Terminal Differentiation of the Epidermal Seam Cells17
2.5 AFF-1 Protein Mediates the Terminal Fusion of the Hypodermal Seam Cells18
References19
3 Role of SNAREs in Membrane Fusion22
3.1 Introduction22
3.2 Materials and Methods24
3.2.1 Preparation of Lipid Bilayer24
3.2.2 Lipid Membrane on Mica Surface25
3.2.3 Atomic Force Microscopy25
3.2.4 EPC9 Electrophysiological Lipid Bilayer Setup25
3.2.5 Preparation of Lipid Vesicles and SNARE Protein Reconstitutions25
3.2.6 Circular Dichroism Spectroscopy26
3.2.7 Wide-Angle X-Ray Diffraction26
3.3 Discussion26
3.3.1 V-SNARE and t-SNAREs Need to Reside in Opposing Membrane to Appropriately Interact and Establish Continuity Between Those Membranes26
3.3.2 Membrane Curvature Dictate the Size of the SNARE Ring Complex29
3.3.3 Disassembly of the SNARE Complex31
3.3.4 CD Spectroscopy Confirm the Requirement of Membrane for Appropriate t-/v-SNARE Complex Assembly, and that NSF-ATP Alone Can Mediated SNARE Disassembly35
3.3.5 SNAREs Bring Opposing Bilayers Closer, Enabling Calcium Bridging and Membrane Fusion38
References40
4 Molecular and Cellular Mechanisms of Mammalian Cell Fusion42
4.1 Introduction42
4.2 Programming Cellular Competence for Fusion44
4.2.1 Cytokines44
4.2.2 DNAX Activating Protein 1245
4.2.3 Phosphatidylserine45
4.2.4 Calcium46
4.2.5 Proteases47
4.2.6 Glis347
4.3 ChemoattractantReceptor Interactions and Cell Migration48
4.3.1 Secretion and Function of Chemoattractants During Myogenesis48
4.3.1.1 Hepatocyte Growth Factor48
4.3.1.2 SDF-1/CXCR4 Axis48
4.3.1.3 IL-448
4.3.2 Mouse Odorant Receptor 2349
4.3.3 Monocyte Chemoattractant Protein-149
4.3.4 Progesterone49
4.3.5 Integrins50
4.3.6 The d2 Isoform of Vacuolar ATPase V0 Domain50
4.3.7 Actin Cytoskeleton Regulators51
4.3.8 Mannose Receptor51
4.3.9 Matrix Metalloproteinases51
4.4 Membrane Recognition and Adhesion52
4.4.1 Immunoglobulin Super Family52
4.4.1.1 Orthologs of Drosophila Ig Super Family Proteins52
4.4.1.2 Other Mammalian Ig Proteins Involved in Myoblast Fusion52
4.4.1.3 Izumo53
4.4.1.4 CD47/SIRP-aInteraction53
4.4.2 Cadherins54
4.4.2.1 N-Cadherin54
4.4.2.2 M-Cadherin54
4.4.2.3 E-Cadherin and Cadherin-1154
4.4.3 Tetraspanins55
4.4.4 Integrins55
4.4.5 Glycosyl-Phosphatidylinositol (GPI)-Anchored proteins55
4.4.6 A Disintegrin And Metalloproteinase (ADAM)56
4.4.7 Dendritic Cell-Specific Transmembrane Protein (DC-STAMP)56
4.5 Fusion Pore Formation and Expansion57
4.5.1 Actin Cytoskeleton57
4.5.2 Lipid Rafts59
4.5.3 A Novel Model of Plasma Membrane Fusion59
4.5.4 Syncytin-1 and -260
4.6 Post-fusion Resetting and Cell Survival61
4.6.1 Myoferlin61
4.6.2 Bcl-2 and c-Flip61
4.7 Conclusions62
References63
5 Membrane Fusions During Mammalian Fertilization74
5.1 Introduction74
5.2 Surface Remodeling of Gametes Prior to Zona Binding76
5.2.1 The Cumulus-Oocyte Complex in the Oviduct76
5.2.2 Sperm Cell Surface Remodeling76
5.3 Zona Binding and Initiation of the Acrosome Reaction77
5.3.1 Zona Pellucida Contains Acrosome Exocytosis Inducing Binding Sites77
5.3.2 Acrosome Exocytosis