By Lars-Inge Larsson (auth.), Lars-Inge Larsson (eds.)
Cell fusions are very important to fertilization, placentation, improvement of skeletal muscle and bone, calcium homeostasis and the immune defence method. also, mobilephone fusions perform tissue fix and will be very important to melanoma improvement, development and treatment. plenty of elements control cellphone fusions, together with receptors and ligands, membrane area organizing proteins, proteases, signaling molecules and fusogenic proteins that deliver membranes shut jointly. within the current quantity, we interrogate what mechanisms that could be vital to cellphone fusions in mammals and what mechanisms that could be shared with reduce organisms and viruses. also, the significance of phone fusions to the pathogenesis in addition to therapy of illnesses is addressed.
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Extra resources for Cell Fusions: Regulation and Control
Landes bioscience, Georgetown, TX, pp 186–203 Kavanaugh MP, Miller DG, Zhang W et al (1994) Cell-surface receptors for gibbon ape leukemia virus and amphotropic murine retrovirus are inducible sodium-dependent phosphate symporters. Proc Natl Acad Sci USA 91:7071–7075 Kent WJ, Sugnet CW, Furey TS et al (2002) The human genome browser at UCSC. Genome Res 12:996–1006 Kjeldbjerg AL, Villesen P, Aagaard L et al (2008) Gene conversion and purifying selection of a placenta-specific ERV-V envelope gene during simian evolution.
2 Evolutionary View of HERV env Genes Since infection by retroviruses is usually harmful, evolutionary selection may neutralize endogenized retroviruses of infected germ lines. Nevertheless, some ERV loci still contain an open reading frame for one or more viral genes. A survey of the human genome identified 29 viral env genes with an ORF longer than 500 amino acids (Villesen et al. 2004, de Parseval et al. 2003), however, some of them appear to be pol-env fusion proteins, leaving 19 real env genes within the human genome.
L. Kjeldbjerg et al. Fig. 4 The point of action of peptide inhibitors of retroviral fusion. The peptide inhibitor (red) is dervied from the carboxy-terminal heptad repeat (light grey) and has affinity for the aminoterminal heptad repeat (dark grey). The inhibitor blocks the association of the two heptad repeats and thereby hinders the transition from the triple-helix structure to the six-helix bundle as needed for fusion 1995, Lu et al. 1995), which suggests that a large amount of free energy is released upon their formation.