By Robert D. Goldman, Robert V. Zackroff, Peter M. Steinert (auth.), Robert D. Goldman, Peter M. Steinert (eds.)

Research job on intermediate filaments (IF) has elevated dramatically during the last decade. For the main half, this surge of curiosity is because of their id as ubiquitous ingredients of the cytoskeleton and karyoskeleton (nuclear matrix) of eukaryotic cells and the truth that we all know little or no relating to their features. In sharp distinction to the opposite significant cytoskeletal platforms, microfilaments and microtubules, IF express a excessive measure of heterogeneity in regards to their protein subunit composition. certainly, you can still merely surprise on the variety of diverse IF polypeptides, their linked proteins (IFAP) and, as a result, the variety of genes occupied with encoding the a number of ingredients of a number of the IF networks present in assorted cellphone varieties. The chapters during this publication reveal how quite a few experimental techniques involv­ ing mobile, molecular, biochemical, and immunological equipment were applied to generate information about the constitution and serve as of IF. To this finish, we now have accrued jointly chapters from specialists within the significant fields of IF examine. In each one bankruptcy, the authors have mixed experiences of the on hand clinical literature with their very own principles on present and destiny instructions for IF examine. The chapters were divided into 5 significant sections that are eager about the subcellular association of IF, the molecular constitution of IF, the differential expression of IF genes, descriptions of associ­ ated proteins fascinated with the intracellular association of IF, and eventually an research of the adjustments obvious in IF in pathological conditions.

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180:303-315. , 1979, Redistribution of intermediate filament subunits during skeletal myogenesis and maturation in vitro, J. Cell Bioi. 82:577-584. , and Somlyo, A. , 1982, Dense bodies and actin polarity in vertebrate smooth muscle, J. Cell Bioi. 95:403-413. , 1982, Isolation of a new high molecular weight protein associated with desmin and vimentin filaments from avian embryonic skeletal muscle, J. Cell Bioi. 92:795-806. , Mark, G. , 1971, Fine structure of smooth muscle cells grown in tissue culture, J.

Geisler and Weber (1988) found that phosphorylation of sites in the amino-terminal head domain prevented assembly of desmin into typical, reconstituted filaments. The specific involvement of these two segments in filament assembly presumably will be clarified by future experiments. Shadowing with heavy metal has also been used to prepare desmin and vimentin filaments for examination in the electron microscope. Henderson et al. (1982) and Kaufmann et al. (198S) saw a 21-nm axial repeat along reconstituted gizzard desmin filaments transferred to mica by the glycerol spray method.

The calculated molecular weight is 53,000 based on 463 residues (Geisler and Weber, 1982, 1983). , 1982). The rod portion of desmin contains the single cysteine residue, has a relative mobility on SDS gels of 40 kDa, and contains a sequence that is remarkably similar to other intermediate filament proteins. The highly a-helical rod segment is characterized by a heptad repeat pattern of hydrophobic amino acids, which is needed to form the interchain coiled-coil packed a helices. The hydrophobic residues are usually located in the first and fourth positions in each heptad.

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