Environ Health Perspect 1980 Apr 01;35:77-82. doi: 10.1289/ehp.803577.

Structural basis of ciliary movement.

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All motile somatic cilia, including those of the human respiratory tract, are similar in ultrastructure in that they consist of an axenome of 9 + 2 microtubules surrounded by a specialized extension of the cell membrane. The axonemal elements provide the ciliary motor, which is powered by ATP hydrolysis. In respiratory cilia, mutants occur where axonemal assembly is aberrant such that the doublet attachments known as arms (Afzelius and co-workers) or spokes (Sturgess) have been shown to be missing. These mutant cilia are apparently nonmotile. In model cilia, the arms are composed of dynein, a class of ATPase isoenzymes and associated polypeptides characterized byGibbons and colleagues. In negative stain preparations of arms, three subunits can be seen. In the presence of ATP, dynein functions with a set polarity to form transient cross-bridges that cause the microtubule doublets of the axoneme to slide relative to one another. After brief trypsin treatment, the axonemal microtubules slide almost completely apart with the arms of doublet n pushing doublet n + 1 in a tipward direction. To produce ciliary beating in vivo, sliding is carefully controlled and coordinated, in part probably by the spoke system. The ciliary membrane is responsible for maintaining the appropriate levels of ATP, Mg2+, and Ca2+, and Ca2+ (ca. 10(-7) M) around the axoneme. The beat of certain cilia--e.g., L cilia of mussel gills--can be arrested by increasing axonemal Ca2+ concentration, for example, in the presence of the ionophore A23187 and high external Ca2+. Although the net results of changes in axonemal Ca2+ concentration are not always complete stoppage of beat or of sliding, this ion is also part of the general behavioral control of ciliary motility.

???displayArticle.pubmedLink??? 6447592
???displayArticle.pmcLink??? PMC1568457
???displayArticle.link??? Environ Health Perspect
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Genes referenced: dnah3 LOC115919910 LOC115923516 LOC581395 LOC583082


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