Thesis-PDF - IAP/TU Wien
Thesis-PDF - IAP/TU Wien
Thesis-PDF - IAP/TU Wien
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Figure 4.16: An image of Euglena spirogyra, demonstrating some of its<br />
pellicle flexibility. Image adapted from [105].<br />
key role in maintaining cell form and elasticity in at least two widely divergent cell<br />
types: mammalian erythrocytes and unicellular Euglenas. In Euglena two smaller<br />
proteins (80 and 86 kDa) associate stoichiometrically to generate filaments that<br />
are arranged perpendicularly to the cell surface. In erythrocytes and probably<br />
Euglena the peripheral membrane skeleton is attached to the plasma membranes<br />
through one or more integral membrane proteins. These membrane anchors are of<br />
considerable interest because they seem to select the specific membrane skeletal<br />
proteins that bind to the plasma membrane and they could then determine in<br />
what regions of the cell the membrane skeleton assembles. In [101] it was shown,<br />
that incubation of stripped membranes with solubilized membrane skeletal proteins<br />
results in the reformation of a membrane skeletal layer, indicating that the plasma<br />
membrane retained appropriate membrane skeletal protein binding sites in vitro.<br />
Lubrification<br />
Certain structures, mucilage producing bodies (designated M in Fig. 4.12), occur<br />
in regular association with the pellicle. Parallel to each pellicular strip a row<br />
of these structures can be found from which narrow canals pass to the groove<br />
and then to the exterior. One possible function of the muciferous bodies is to<br />
supply a lubricant - mucilage (mucus) - to the pellicle strip articulations. This is<br />
an intracellular release of mucilage, since the whole of the pellicular system lies<br />
within the plasma membrane.<br />
Mucus is typically a dilute network of proteins and polysaccharides. These<br />
molecules take on an extended configuration that causes them to become entangled,<br />
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