Cellular filaments

Moulds Multi-cellular filaments that increase by vegetative growth of the filament. 

Fungus. simple organism that contains no chlorophyll, which may consist of one cell or of many cellular filaments called hyphae. If allowed to grow in HVAC equipment it may cause allergic reactions. 

Fig. 10.4 Fossilized cellular filamentous microorganisms (two examples of Primaevifilum amoenum). They are 3.456 billion years old and come from the Apex chert region in northwestern Australia. As well as the original images, drawings and the Raman spectra and Raman images, which indicate that the fossils have a carbonaceous (organic) composition, are shown. With kind permission of J. W. Schopf...

Amino acids join together to form proteins, polyamides that compose thick ropes of fibers called cellular filaments that give shape to a cell. 

A typical fungus is built up of cellular filaments called hyphae. These hyphae grow at the tip and branch. The hyphae are compartmentalized but there is cytoplasmic connection between adjacent compartments (Fig. 1.4). 

It is usually presumed that smooth muscle cells have only one kind of activity, contraction, and that the only alternative to contractile activity is a kind of estivating resting state (Figure 11). The actual situation is of course more complicated. For example, smooth muscles synthesize extracellular filament protein. They also proliferate, particularly in the cardiovascular system. Both of these processes require a considerable amount of control of the cellular economy. 

Nonmuscle cells perform mechanical work, including self-propulsion, morphogenesis, cleavage, endocytosis, exocytosis, intracellular transport, and changing cell shape. These cellular functions are carried out by an extensive intracellular network of filamentous structures constimting the cytoskeleton. The cell cytoplasm is not a sac of fluid, as once thought. Essentially all eukaryotic cells contain three types of filamentous struc-mres actin filaments (7-9.5 nm in diameter also known as microfilaments), microtubules (25 nm), and intermediate filaments (10-12 nm). Each type of filament can be distinguished biochemically and by the electron microscope. 

Although not organized as in muscle, actin filaments in nonmuscle cells interact with myosin to cause cellular movements. 

The cellular cytoskeleton, primarily composed of microfilaments, microtubules, and intermediate filaments, provides structural support and enables cell motility. The cytoskeleton is composed of biological polymers and is not static. Rather, it is capable of dynamic reassembly in less than a minute [136], The cytoskeleton is built from three key components, the actin filaments, the intermediate filaments, and the microtubules. The filaments are primarily responsible for maintaining cell shape, whereas the microtubules can be seen as the load-bearing elements that prevent a cell from collapsing [136], The cytoskeleton protects cellular structures and connects mechanotransductive pathways. Along with mechanical support, the cytoskeleton plays a critical role in many biological processes. 

The nervous system contains an unusually diverse set of intermediate filaments (Table 8-2) with distinctive cellular distributions and developmental expression [21, 22]. Despite their molecular heterogeneity, all intermediate filaments appear as solid, rope-like fibers 8-12 nm in diameter. Neuronal intermediate filaments (NFs) can be hundreds of micrometers long and have characteristic sidearm projections, while filaments in glia or other nonneuronal cells are shorter and lack sidearms (Fig. 8-2). The existence of NFs was established long before much was known about their biochemistry or properties. As stable cytoskeletal structures, NFs were noted in early electron micrographs, and many traditional histological procedures that visualize neurons are based on a specific interaction of metal stains with NFs. 

Although many cellular proteins are potential targets for phosphorylation by PKC, the myristoylated alanine-rich protein kinase C substrate (MARCKS) appears to be a major in vivo substrate. MARCKS is an acidic filamentous actin cross-linking protein that is found in high concentrations at presynaptic junctions and that is directed to... 

Myosin II is in the same subfamily as the myosins in muscle thick filaments and it forms large, two-headed myosins with two light chains per heavy chain. Although myosin II is abundantly expressed in brain, little is known about its function in the nervous system. In other nonmuscle cells, myosin II has been implicated in many types of cellular contractility and may serve a similar function in developing neurons. However, myosin II remains abundant in the mature nervous system, where examples of cell contractility are less common. 

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