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Cytoskeleton and Calcium. a Review

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Cytoskeleton and Calcium. a Review Bull Group Int Rech Sci Stomatol et Odontol Cytoskeleton and calcium. A review DARD, M. U.F.R. Odontologie, Place A. Ricordeau, 44042 Nantes Cedex France SUMMARY The aim of the présent paper was to summarize the main features about cytoskeleton in order to under- stand the possible interactions between this System of filamentous, microfilaments structures (including microtubules, intermediate filaments, microfilaments) and calcium in mesenchymal cells of the oral cavity. KEY WORDS: Microtubules - Intermediate filaments - Microfilaments - Calcium. RÉSUMÉ Cet article fait le point des connaissances actuelles sur le cytosquelette et vise à mettre en évidence les inter¬ actions possibles entre ce système de structures fibrillaire (microtubules, filaments intermédiaires, microfi¬ laments) et le calcium, pour ce qui concerne les cellules mesenchymateuses de la cavité buccale. MOTS-CLÉS: Microtubules - Filaments intermédiaires - Microfilaments - Calcium. INTRODUCTION Structural, ultrastructural and molecular organiza- filaments, microfilaments) found in ail types of tion of cytoskeleton in eukaryotic cells is well eukaryotic cells. The cytoskeleton can be thought as documented now, but little is known about the the integrated System of molécules that gives cells physiological properties of the cytoskeleton espe- their shape, internai spatial organization, motility cially in mesenchymal cells of the oral cavity, which and communication routes with other cells and are often located near or sources. within calcium environment (Schliwa, 1986). The aim of the présent paper was to summarize the Activities related to cytoskeleton are controlled by main features about cytoskeleton in order to under- intracellular signalling Systems. One of the most im¬ stand the possible interactions between cytoskeleton and calcium in mesenchymal cells of the oral cavity. portant signal seems to be a change in the concentra¬ tion of free intracytoplasmic calcium ions. Calcium The term «cytoskeleton» refers to the System of may exert its effect alone or combined with others filamentous structures (microtubules, intermediate signais (Bennett and Weeds, 1986). 209 M. DARD MICROTUBULES Bound exchangeable GTP in the wall of microtubule is hydrolysed into GDP. Elongation is efficient in Microtubules, the universal components of ail the presence of high concentrations GTP-tubulin eukaryotic cells (Roberts and Hyams, 1979), hâve of but proceeds very slowly with concentrations the largest diameter (about 25nm) of ail cytoskeletal similar of GDP-tubulin Carlier, a fibrils. The microtubules wall, about 5nm wide, is (Hill and 1983). Since microtubule grows from its ends, «GTP-caps» are made of a single protein, the tubulin. Each tubulin necessary to induce élongation and to maintain the molécule is a hetero-dimer consisting of one a and polymer stability (Carlier et al., 1984a). Some one (3 chains. Protofilaments are constituted of these authors consider that this stability is in fact a non identical tubulin polypeptide chains, a and 13 dynamic instability of microtubules (Mitchison and (Schultheiss and Mandelkow, 1983), most often Kirschner, 1984; Sammak and Borisy, 1988). isolated from brain tissue (Field et al., 1984). Tubulin polypeptide chains hâve a molecular weight This «capping model» of élongation (Bershadsky of about 50 kD. Brain a tubulin contains 451 amino and Vasiliev, 1988) suggests that a population of acid residues, /3 tubulin 445 residues (Krauhs et al., microtubules at low GTP-tubulin concentrations 1981). These two subunits hâve about 40% of consists of two fractions: growing capped homologous residues. microtubules and shrinking uncapped microtubules. Structural studies hâve shown that protofilaments The amount of polymerised tubulin in these condi¬ are slightly staggered (Hirokawa, 1982; Murray, tions is not changed because the growth of some microtubules is 1984). Subunits of neighboring protofilaments are compensated by the shrinkage of others. shifted about lnm along the microtubule axis, so that these subunits can be connected a helical by line. It is Microtubules in most animal tissues hâve likely that cells usually contain not only 13 protofilaments (Tucker, 1984). polymerized microtubules, but also a large pool of unpolymerized tubulin. Some of the proteins attached to the outer surface of the microtubule wall are called microtubule- Cells seem to regulate not only the extent of associated proteins (MAPs) (Vallée et al., 1984). microtubules formation but also the géométrie Those isolated from the brain are most well known. organisation of polymers within the cytoplasm. It has shown These proteins form three main groups: the MAP-1 been that microtubules possess an intrin- with a molecular weight of 300-350 kD, the MAP-2 sic polarity (Heidemann and Mc Intosh, 1980; (Sloboda et al., 1975) with a molecular weight of Euteneuer et al., 1983) and that subunits add 270-285 kD and tau group (Cleveland et al., 1977) preferentially to one end (calles «plus end») of the with a molecular weight of about 60 kD. microtubule and are lost from the other (called «minus end») (Margolis et al., 1978; When these molécules are attached to the Bergen and Borisy, 1980). microtubule wall, they look like filamentous projec¬ tions, 80-100 nm long (Voter and Erikson, 1982). Thus, once a microtubule is initiated, élongation in a MAPs are suspected to participate in microtubular given direction is dictated. The sites from which interactions (Olmsted et al., 1984). Ail types of microtubules initiate or the areas with which MAPs added to pure tubulin solutions promote microtubules interact are called microtubule organiz- nucléation of the microtubules in vitro (Murphy et ing centers (MTOC) (Pickett-Heaps, 1969; Brinkley al., 1977). et al., 1981; Tucker, 1984). The two most prominent A hypothetical nucléation and élongation scheme organizing centers in cultured mammalian cells are concerning microtubules has been developped (Ber- the centrosome and the kinetochore (Bergen et al., shadsky and Vasiliev, 1988): fragments of pro¬ 1980). However little is known about the tofilaments would be formed first, followed by the mechanism by which tubulin becomes associated formation of the bidimensional fragment of the with these areas and how the ability to organise microtubules is mediated. microtubule wall, and finally a cylindrically closed short microtubule would grow from its ends. Motility is a characteristic feature of many types of Attachment of subunits to the end of the fibril is microtubular Systems, such as cilia. Mutual slidding followed by hydrolysis of the bound nucléotide. of microtubules is caused by cyclic interactions of a Elongation of microtubules is GTP-GDP (guanine- major microtubule-associated ATPase, dynein with tri, di-phosphate) bounded (Carlier and Pantaloni, microtubule walls (Johnson, 1983; Goodenough and 1981). Heuser, 1984). 210 CYTOSKELETON AND CALCIUM. A REVIEW A dynein-like ATPase called kinesin, is suspected to large central core domain of about 40 kD, consisting be responsible of organelle movements along micro- of several-helical subdomains interspersed by short tubules (Vale et al., 1985). non helical inclusions. The central core domain is flanked by two non helical terminal domains. Cell microtubules are very sensitive to calcium, espe- Although the complété sequence of the gene, coding cially in the presence of calmodulin, a calcium- for vimentin is known (Quax et al., 1983, Quax- binding protein (Alberts et al., 1983; Gratzer and Jeuken et al., 1983) well-controlled experiments are Baines, 1988). It is likely that the calcium-calmodulin still needed to relate the molecular structure of complex acts on the microtubules via MAPs (Wei- vimentin to spécifie cytoplasmic events (Geiger, senberg, 1972), activating one of the MAP-phospho- 1987). Georgatos and Biobel (1987a, 1987b) hâve rylating kinases or via dynein, by modulating its shown that purified vimentin binds to different frac¬ ATPase activity (Blum et al.). tions of avian érythrocyte membranes through two Phosphorylated MAPs are less bound to the microtu¬ distinct domains. First sites (lamin B or lamin bules and cannot promote tubuline polymerization A-lamin B hetero-oligomers), located at the carboxy¬ or stabilise microtubules (Greene et al., 1983; Wolff, terminal tail of the vimentin molécule, bind specifi- 1988). cally to the endofacial and presumably exofacial sur¬ faces of nuclear envelopes. INTERMEDIATE FILAMENTS The on mem¬ Intermediate filaments (IF) form a class of insoluble second-type of binding sites the plasma brane at the amino-terminal head of the vimentin cytoplasmic fibrils. They are thinner than microtu¬ molécule, is et bules in électron microscopie sections, 8-12 nm in provided by ankyrin (Georgatos al., diameter (Granger and Lazarides, 1982). Although 1987). the intermediate dilaments may not be universal On the basis of these results Geiger (1987) hypothe- components of the cytoskeleton of ail eukaryotic sizes that vimentin filaments are associated with the cells, they are however abundant in most cell types cell nucléus, interacting with the nuclear lamina of vertebrates. through the nuclear pores. At the cell periphery the The most typical structures formed by intermediate same intermediate filaments are apparently associa¬ filaments are three-dimensional loose networks distri- ted with the membrane. buted throughout the cytoplasm and intermixed with It is other cell components (Steinert et al., 1984). likely that cell is provided with an elaborate System of
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