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ULTIMATE COMPUTING - Quantum Consciousness Studies

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Models of Cytoskeletal Computing 161<br />

of the filaments appears to be controlled by the microtubule system, analogous to<br />

its function in cell movement and cell shape. DeBrabander (1977) observes that in<br />

these phenomena MT act beyond their capacity as skeletal support elements and<br />

perform as signal transducers from the cell center to the periphery, and vice versa.<br />

Interactive signaling in the cytoskeleton fits with observations that local events at<br />

one site in the cell often lead to a global cellular rearrangement. DeBrabander<br />

raises several MT features which could favor signaling: MT intrinsic polarity, the<br />

existence of “centrifugal and centripetal microtubules,” the conformational<br />

propagation mechanism proposed by Atema (1973), directional organelle<br />

movement and topography, and transport of ions such as calcium along<br />

microtubules.<br />

DeBrabander and his associates (1986) have also innovated new techniques in<br />

the examination of cytoskeletal structure and dynamics. These include “Nanovid<br />

Microscopy,” a nanometer scale video microscopy in which transport of labeled<br />

particles along individual MT may be visualized, and a method of labeling<br />

individual tubulin subunits within MT which are either tyrosinated or glutamated<br />

(Geuens, Gundersen, Nuydens, Cornelissen, Bulinski, DeBrabander, 1987). As<br />

described in Chapter 5, polymerized MT may be detyrosinated in the cytoplasm<br />

subsequent to DNA directed genetic input. Tyrosine, the terminal amino acid in<br />

tubulin, may be removed to expose glutamate as the new terminal amino acid.<br />

Thus all tubulins within polymerized MT are either tyrosinated, or glutamated. A<br />

variety of cytoplasmic factors determine whether or not a particular tubulin is<br />

tyrosinated. The precise significance or function of tyrosination/glutamation is<br />

unknown but could serve as a convenient programming or memory function.<br />

DeBrabander and colleagues developed a double labeling technique in which<br />

immunogold particles bind to tubulin subunits. Large immunogold particles (10<br />

nanometers) identify glutamated tubulin and smaller particles (5 nanometers) bind<br />

to tyrosinated tubulin. Patterns of tyrosinated/glutamated tubulin within MT show<br />

heterogenous distribution, and suggest the potential for a coding mechanism.<br />

MAP attachment, tubulin conformation, calcium binding and other factors could<br />

be coupled to MT function via such patterns. Although predisposition to<br />

detyrosination may be genetically linked to tubulin isozymes, the actual patterns<br />

of tubulin detyrosination are determined by “real time” cytoplasmic factors.<br />

DeBrabander and colleagues have provided the first direct evidence of modifiable<br />

patterns of tubulin variability in intact microtubules. Consequently, MT appear<br />

capable of signal processing in addition to signal transduction.

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